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The Role of Lipids in Parkinson’s Disease

Helena Xicoy, Bé Wieringa, Gerard J. M. Martens

Cells · 2019 · Review · CC BY

Abstract

Parkinson’s disease (PD) is a neurodegenerative disease characterized by a progressive loss of dopaminergic neurons from the nigrostriatal pathway, formation of Lewy bodies, and microgliosis. During the past decades multiple cellular pathways have been associated with PD pathology (i.e., oxidative stress, endosomal-lysosomal dysfunction, endoplasmic reticulum stress, and immune response), yet disease-modifying treatments are not available. We have recently used genetic data from familial and sporadic cases in an unbiased approach to build a molecular landscape for PD, revealing lipids as central players in this disease. Here we extensively review the current knowledge concerning the involvement of various subclasses of fatty acyls, glycerolipids, glycerophospholipids, sphingolipids, sterols, and lipoproteins in PD pathogenesis. Our review corroborates a central role for most lipid classes, but the available information is fragmented, not always reproducible, and sometimes differs by sex, age or PD etiology of the patients. This hinders drawing firm conclusions about causal or associative effects of dietary lipids or defects in specific steps of lipid metabolism in PD. Future technological advances in lipidomics and additional systematic studies on lipid species from PD patient material may improve this situation and lead to a better appreciation of the significance of lipids for this devastating disease.

Full text

From PubMed Central, U.S. National Library of Medicine, as current on Oct 20, 2026. Paragraph numbers are ours, so an answer can point at one.

1. Introduction

1Parkinson’s disease (PD) is the second most common neurodegenerative disease affecting 1% of the population above 60 years and up to 4% of individuals in the highest age groups. Parkinson’s disease is characterized by motor symptoms, such us tremor, rigidity, bradykinesia (slowed movement) and impaired balance, and non-motor manifestations, including sleep disorders, and autonomic, gastrointestinal, sensory, and neuropsychiatric symptoms. These symptoms are associated with a progressive loss of dopaminergic (DA) neurons from the nigrostriatal pathway, formation of Lewy bodies (LB), and microgliosis. In familial PD, which explains 5–10% of all cases, these abnormalities may be caused by a mutation in one of the thus far known 19 familial genes, including SNCA, LRRK2, PRKN, PINK1 and DJ-1, among others. The remaining 90–95% of PD cases are of sporadic nature with unknown etiology.

2Despite a large number of studies on familial forms of PD or toxin-induced cell and animal PD models (e.g., use of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP), rotenone or 6-hydroxydopamine (6-OHDA)), no disease-modifying treatment for PD has been developed yet. Thus, additional approaches are necessary to advance the field of PD. Previously, we used data from genome-wide association studies and other genetic studies of PD patients to build a molecular landscape. This enabled us to identify, in an unbiased way, various processes and pathways that might be involved in PD. Interestingly, we found that lipids play a key role in most of the processes that have been (classically) associated with PD (i.e., oxidative stress, endosomal-lysosomal function, endoplasmic reticulum stress, and immune response), and thus in PD etiology. In agreement with this observation, not only mutations in the gene encoding the lipid-producing enzyme glucocerebroside (GBA) are associated with familial PD, but also multiple single-nucleotide polymorphisms (SNPs) located in other genes involved in lipid metabolism, e.g., SREBF1, DGKQ, ASAH1 or SMPD1, have been linked to sporadic PD.

3Lipids are biomolecules soluble in nonpolar organic solvents, usually insoluble in water, and primarily known for their metabolic role in energy storage. Furthermore, they are the main constituents of cellular membranes, part of membrane rafts and protein anchors, and signaling and transport molecules. There are eight different classes of lipids, classified as fatty acyls, glycerolipids, glycerophospholipids, sphingolipids, sterols, prenols, saccharolipids, and polyketides. Here we will review the current knowledge of the role of the first five lipid classes and of lipoproteins in PD (Figure 1). Certain aspects of the relationship between PD and lipids are beyond the scope of this review, including the complex interaction between (membrane) glycerophospholipids and α-synuclein, the interaction between lipid classes, and the role of cholesterol derivatives, such as bile acids, tocopherols, and tocotrienols (vitamin E), vitamin A and carotenoids, vitamin D, steroidal hormones (e.g., estrogen) and coenzyme Q10.

2. Fatty Acyls

4Fatty acyls are carboxylic acids formed by a hydrocarbon chain and a terminal carboxyl group (Figure 2). They are synthesized by chain elongation of acetyl-CoA with malonyl-CoA groups by enzymes named elongases. While humans can synthesize most fatty acyls, linoleic acid (LA) and alpha-linoleic acid (ALA) need to be obtained through the diet. Fatty acyls are not only energy sources, but also the building blocks of complex lipids and as such form a key category of metabolites. Additionally, they are membrane constituents and regulate intracellular signaling, transcription factors, gene expression, bioactive lipid production, and inflammation. Below, we will discuss the current knowledge of the roles of fatty acyls, more specifically of saturated fatty acids (SFA), monounsaturated fatty acids (MUFA), polyunsaturatedfatty acids (PUFA), eicosanoids and (acyl)carnitine, in PD, and an overview can be found in Supplementary Materials Table S1.

2.1. SFA

5The simplest fatty acids are the straight-chain SFA. Their intake does not seem to be linked to PD risk in humans per se, but SFA intake in individuals exposed to rotenone increases PD risk, when compared to pesticide exposure alone. Thus, SFA could exacerbate PD-linked pathology. Interestingly, higher levels of SFA (mainly 16:0 and 18:0) have been observed in lipid rafts from the frontal cortex of PD patients compared to controls, but not in their temporal cortex. These area-dependent changes combined with a lack of differences in SFA intake between PD patients and controls point to defects in their absorption or metabolism and region-specific and/or cell-compartment differences. Dietary supplementation with SFA 18:0, which seems to be a less potent pro-inflammatory lipid than other SFA species, regulates mitochondrial function and rescues the PD-like phenotype of PINK and PRKN mutant flies. Similarly, both acute and repeated intra-gastric gavage of SFA 8:0 reduces the impairment of DA neurotransmission in MPTP-treated mice. These findings, together with the observed higher SFA levels in the frontal cortical lipid rafts, may point towards a compensatory mechanism in PD patients. In contrast, exposure of SH-SY5Y cells, primary neurons, and astrocytes to SFA 16:0 leads to apoptosis, reduces peroxisome proliferator-activated receptor gamma coactivator 1-alpha (PPARGC1A, PGC-1alpha) and estrogen receptor alpha (ER-alpha) expression, promotes inflammation, and activates cyclooxygenase-2 (COX-2), features that have also been observed in the brains of PD patients. Since α-synuclein modulates the uptake of SFA 16:0 into the brain, accumulation of this protein in PD brains might lead to increased levels of SFA 16:0, which in turn can trigger some of its neuropathological activities.

2.2. MUFA

6Variants of SFA containing one double bond are known as MUFA. Higher MUFA intake has been variably associated with decreased PD risk, reduced risk only in women or unchanged risk. These discrepancies in findings could be due to variation in the ethnicity of the subjects, differences in the type of study (cohort or case-control), the number of participants, questionnaires employed to asses MUFA intake, the corrections used, or even PD etiology, since different MUFA levels in cerebrospinal fluid (CSF) have been described in PD patients carrying a GBA mutation and those that do not. Of note, no abnormalities in MUFA level have been observed in the temporal cortex of PD patients. Some MUFA, such as oleic acid and cis-vaccenic acid, trigger the production of dopamine in MN9D cells, and the amide of oleic acid and dopamine (N-oleoyl-dopamine) modulates the firing of nigrostriatal DA neurons. Interestingly, α-synuclein has a motif homologous to a region in fatty acid-binding proteins, allowing it to bind to oleic acid, which facilitates the interaction of α-synuclein with lipid rafts. Based on these suggestive but still tentative findings, the effect of MUFA intake on PD risk, and specifically, its effect on dopamine production and the intracellular location and function of α-synuclein, should be further examined.

2.3. PUFA

7Fatty acids containing two or more double bonds are known as PUFA and are usually classified according to the position of the first double bond counted from the tail (omega). The omega-3 family, for which ALA is the essential parent fatty acid, forms metabolic products that include eicosapentaenoic acid (EPA) and docosahexaenoic acid (DHA). Omega-6 PUFA, for which LA is the parent fatty acid, include arachidonic acid (AA), an intensely studied precursor of signaling lipids. In general, PUFA are known to play a role in inflammation, epigenetics, and brain development and function. As such, they have been widely examined in PD patients, and animal and cellular PD models.

2.3.1. Human Studies on PUFA

8Higher intake of omega-3 PUFA and ALA, but not other PUFA, such as omega-6 PUFA or LA, has been associated with reduced risk of PD, while other studies have reported a weak positive association between omega-6 PUFA and LA intake and PD risk, or have provided evidence against an association between PUFA intake and PD risk. A link between AA intake and PD risk is also controversial: one study described a positive association, while another reported an inverse association. Serum of PD patients has decreased concentrations of long-chain PUFA, including ALA, LA, and AA, compared to controls, while the CSF of PD patients has increased levels of 4-hydroxynonenal, a toxic product generated by AA peroxidation. However, as described for MUFA, PUFA levels in CSF may depend on PD etiology. The levels of PUFA in the anterior cingulate cortex and the occipital cortex of PD patients are increased or not changed, respectively. Additionally, the levels of DHA and AA are decreased in frontal cortex lipid rafts from PD patients, while reduced LA, increased DHA and docosatetraenoic acid (an omega-6 PUFA), and no changes in AA have been reported for the cytosolic fraction of PD frontal cortex. Moreover, no changes of PUFA were observed in the temporal cortex of PD patients. Therefore, there is no agreement on the impact of PUFA intake on PD risk and little information on PUFA levels in the blood, CSF and brain of PD patients is available. The only consistent finding is the altered intracellular distribution of PUFA in neurons from the frontal cortex of PD patients, i.e., reduced levels of DHA in the lipid rafts and increased DHA in the cytosolic fraction.

2.3.2. Animal and Cellular Studies on PUFA

9Omega-3 PUFA exert neuroprotective actions in MPTP-treated mice by increasing the expression of brain-derived neurotrophic factor and have also neuroprotective activity in 6-OHDA-treated rats. A decrease in the level of this class of PUFA has been observed in the brains of an MPTP-induced goldfish PD model. Furthermore, omega-3 PUFA deficiency leads to a reduced ability of the nigrostriatal system to maintain homeostasis under oxidative conditions, increasing the risk for PD. Maternal omega-3 PUFA seem to partially protect a lipopolysaccharide (LPS)-model for PD. Likewise, the omega-3 PUFA DHA protects DA neurons against MPTP–, paraquat— or rotenone-induced toxicity in rodent models and against effects of 6-OHDA-treatment in Caenorhabditis elegans, mice and rats, also when administered as TAG-DHA. Moreover, DHA plays a crucial role in the differentiation of induced pluripotent stem cells (iPSCs) into functional DA neurons and DHA supplementation protects DA neurons from the SN in MPTP-treated mice. EPA and ethyl-EPA attenuate 1-methyl-4-phenylpyridinium (MPP+)-induced cell death in SH-SY5Y cells, primary mesencephalic neurons, and brain slices, and in vivo reduce MPTP/probecenid-induced dyskinesia and memory deficits (without preventing nigrostriatal DA loss). Thus, omega-3 PUFA appear to have a neuroprotective role in animal models for PD.

10Additionally, pretreatment of rats with fish oil (which is rich in omega-3 PUFA) for 25 days before 6-OHDA treatment mitigates the loss of substantia nigra (SN) DA neurons. In contrast, a chronic supplementation of fish oil in rats does not protect DA neurons but increases dopamine turnover. These differential effects could be explained by the finding that the ethyl ester of DHA, a PUFA present in fish oil, enhances 6-OHDA-induced neuronal damage by triggering lipid peroxidation in mouse striatum. Lipid peroxidation, which occurs frequently in PUFA, may lead to mitochondrial dysfunction and α-synuclein oligomerization. It is therefore not surprising that a number of studies have demonstrated beneficial effects when using deuterium-reinforced (deuterated) PUFA (which protects the PUFA sites susceptible for oxidation), or PUFA in combination with antioxidants. Therefore, omega-3 PUFA, probably in combination with the prevention of lipid peroxidation, should be further studied as a complementary therapy for PD.

11Increased levels of omega-6 PUFA (LA and AA) have been reported in mice brain slices upon MPP+ treatment. Similarly, upregulated AA signaling has been observed in the caudate-putamen and frontal cortex of 6-OHDA-treated rats, and the striatum and midbrain of MPTP-treated mice. Both LA and AA are able to inhibit MPP+-induced toxicity in PC12 cells, while excess AA aggravates α-synuclein oligomerization in PC12 cells. Interestingly, a mouse model with impaired incorporation of AA in the brain is resistant to MPTP treatment. Hence, pharmacologically induced PD is linked to an increase in AA, the consequences of which are at present unclear and could be dose dependent.

2.3.3. Alpha-Synuclein and PUFA

12Under physiological conditions, α-synuclein and PUFA are involved in endocytic mechanisms linked to synaptic vesicle recycling upon neuronal stimulation. Moreover, α-synuclein and PUFA regulate each other, since α-synuclein increases endogenous levels of AA and DHA, and its oligomers control the ability of AA to stimulate SNARE-complex formation and endocytosis. Reciprocally, PUFA strongly interact with the N-terminal region of α-synuclein, enhancing its oligomerization both in vivo and in vitro. This might precede the formation of protective (LB-like) inclusions in DA cells.

13Studies on specific PUFA species have shown that DHA induces α-synuclein oligomerization by activating retinoic X receptor and PPAR-gamma 2, effects that were prevented by co-administering aspirin. The oligomers formed in the presence of DHA seem to be cytotoxic and affect membrane integrity and the physical properties of DHA itself (triggering formation of lipid droplets). Alpha-synuclein aggregation is also induced by AA, but the oligomers that are formed seem to be less toxic (more prone to disaggregation and enzymatic digestion) and their formation is prevented or enhanced by low or high doses of dopamine, respectively. The enhanced toxicity of dopamine might be related to its ability to form adducts with AA, which are able to trigger apoptosis.

14Interestingly, a diet poor in omega-3 PUFA (with or without DHA supplementation) did not affect α-synuclein expression. Accordingly, a DHA-rich diet had no effect on the DA system, motor impairments or α-synuclein levels in α-synuclein-overexpressing mice but increased the longevity of the mice. This latter phenomenon might be related to the role of monomeric α-synuclein in sequestering early DHA peroxidation products and thus reducing oxidative stress. The interaction between α-synuclein and (peroxidated) PUFA has recently been reviewed in more detail elsewhere.

2.4. Eicosanoids and Docosanoids

15Eicosanoids and docosanoids constitute a family of bioactive fatty acyls mainly generated by AA, EPA, and DHA oxidation. They play a local role in infection and inflammation. The family includes PGL, LT, EET, isoprostanes, HETE, isofurans, and resolvins, among others. Interestingly, one of the enzymes responsible for the formation of eicosanoids, COX-2, has been linked to PD pathology. Its role in the disease has been reviewed elsewhere.

2.4.1. PGL

16No changes in or increased PGL E2 levels have been observed in the CSF and SN of PD patients, respectively. In animal and cellular PD models, PGL E2 secretion is induced by LPS, 6-OHDA, rotenone, MPTP, and α-synuclein aggregation. Nevertheless, PGL E2 levels in the striatum, hippocampus, and cortex of 6-OHDA-treated mice are decreased following a four-week exposure. The eicosanoid PGL E2 mainly mediates its effects by binding to PGL E2 receptors (EP1-4), which trigger various intracellular pathways. The EP1 receptor knock-out (KO) has neuroprotective effects on 6-OHDA-treated mice and an EP1 antagonist protects embryonic rat mesencephalic primary cultures from 6-OHDA toxicity. An agonist of EP2 protects primary neuronal cultures from 6-OHDA-induced toxicity and an agonist of EP4 prevents DA loss in the SN of MPTP-treated mice. Therefore, the effect of PGL E2 is also dependent on which receptor it binds. Interestingly, astrocytes KO for the familial PD gene DJ-1 secrete less PGL E2 than WT astrocytes. This could impair DA neuron survival mediated by EP2. Thus, the sparse data that are available regarding the effects of PGL suggest that increased PGL E2 levels may play a role in the pathology of animal and cellular PD models, but that this occurs in a time-, location-, phenotype- and receptor-dependent manner.

17Both PGL A1 and lipocalin-type PGL D synthase (the enzyme that isomerizes PGL H2 to PGL D2) inhibit rotenone- and paraquat-induced apoptosis in SH-SY5Y cells, respectively. Furthermore, enhanced prostacyclin synthesis seems to reduce glial activation and ameliorate motor dysfunction in 6-OHDA-treated rats. Conversely, PGL J2 treatment of SK-N-SH cells leads to the formation of aggregates containing ubiquitinated α-synuclein, and infusion into the SN of mice induces a pathology that mimics the slow-onset cellular and behavioral pathology of PD, including loss of DA neurons in the SN, α-synuclein aggregation, posture impairment, and microgliosis. Hence, PGL other than PGL E2 seem to play a role in PD pathology as well, with effects being protective or detrimental. To resolve this complexity and obtain deeper insight into the contributions of these oxidized PUFAs to PD pathology further research is needed.

2.4.2. LT

18Increased plasma LT B3 has been suggested as a biomarker for PD. However, the role of LT has only been tested in animal and cellular PD models, in which MPTP treatment upregulates arachidonate 5-lipoxygenase (5-LOX, the enzyme that synthesizes LT from AA). This work has demonstrated that 5-LOX inhibition has neuroprotective effects, a finding which would be in agreement with the observation that LT B4 enhances MPP+-induced neurotoxicity in midbrain cultures. Moreover, inhibition of cysteinyl LT receptor 1 has neuroprotective effects in a rotenone-induced rat PD model. Interestingly, 5-LOX KO in mice reduces striatal dopamine levels under normal conditions. Thus, 5-LOX seems to be necessary for maintaining the DA tone but can become deleterious upon toxicant challenge.

2.4.3. EET

19In PD patients, the SNP rs10889162 located in CYP2J2 (the enzyme that metabolizes AA into EET) is associated with age of diagnosis. Interestingly, EETs are known to have cytoprotective effects in other diseases and may therefore also play a role in PD neuroinflammation. In PD models, 14,15-EET, which is released from astrocytes, enhances cell viability against oxidative stress and protects DA neuronal loss in MPTP-treated mice. Inhibition or KO of the soluble epoxide hydrolase (sEH, inhibition of which elevates endogenous EET) protects MPTP-treated mice, and a double sEH and COX-2 inhibitor has protective effects on a rotenone-induced Drosophila melanogaster PD model. Combined, these findings suggest that EET has widespread neuroprotective effects, not necessarily relevant for PD only.

2.4.4. Isoprostanes

20The role of isoprostanes in PD is controversial. Both higher levels and no change in F2-isoprostane have been found in urine and plasma of (early) PD patients. Moreover, no changes have been observed in CSF or SN of PD patients, but higher levels of F2-isoprostane have been described in anterior cingulate cortex of PD patients. Higher F2-isoprostane levels have also been observed in rotenone-, but not manganese-treated DA neurons derived from healthy iPSC. Thus, more research and proper stratification of findings need to be performed to understand the role of isoprostanes in PD.

2.4.5. Other Eicosanoids and Docosanoids

21The classic and non-classic AA-derived eicosanoids, HETE and isofurans, are increased in plasma and SN of PD patients, respectively. The docosanoid resolvin D1 attenuates MPP+-induced PD by inhibiting inflammation in PC12 cells, and resolvin D2 seems to restore LPS-induced neural injury in a rat model, also by suppression of inflammation. Thus, resolvins seem to have a protective role in PD.

2.5. Carnitine and Acylcarnitine

22Carnitine is a trimethyllysine derivative that can associate with various fatty acids, forming acylcarnitine. This association facilitates their transport from the cytosol to the mitochondrial matrix, where fatty acids undergo β-oxidation. Both carnitine and acylcarnitines are involved in processes such as neurotransmission and apoptosis. Decreased levels of carnitine and (long-chain) acylcarnitines have been detected in plasma from PD patients, while no changes in acylcarnitine levels have been found in either CSF or plasma from PD patients when compared to controls. Acetylcarnitine (acylcarnitine 2:0) protects SK-N-MC cells from rotenone-induced toxicity, and carnitine reduces the effects of MPP+ on rat forebrain primary cultures and LPS in SIM-A9 microglial cells. Moreover, the neuroprotective properties of acetylcarnitine have been found in rats treated with 6-OHDA and rotenone, and non-human primates treated with MPTP. Additionally, increased levels of carnitine and acylcarnitine 16:0 and 18:0 have been detected in the striatum of 6-OHDA-treated rats and the mesencephalon of MPTP-treated mice, respectively, suggesting a compensatory mechanism against PD-associated toxicity. Thus, while it remains unclear whether the levels of acylcarnitine change in PD patients, mounting evidence points towards decreased plasma levels and a protective role of acylcarnitine in animal and cellular PD models.

3. Glycerolipids

23The esterification of one, two or three fatty acyls with glycerol gives rise to the glycerolipids mono-, di-, and tri-substituted glycerol, known as monoacylglycerol (MAG), diacylglycerol (DAG), and triacylglycerol (TAG), respectively (Figure 3). There is little information available on the function of MAG, while DAG is a neutral lipid involved in the formation of membranes and in the synaptic vesicle cycle. Additionally, DAG fulfills a role as secondary lipid messenger. The neutral lipid TAG is the main energy storage molecule. Below, we will discuss the current knowledge of the roles of all glycerolipids with potential significance for PD, including MAG, endocannabinoids, DAG, and TAG, and an overview is given in Supplementary Materials Table S1.

3.1. MAG

24Decreased and increased expression of MAG lipase, the enzyme that degrades MAG to glycerol and free fatty acids, has been observed in the SN and the putamen of PD patients, respectively. These differential effects could be associated with the different mechanisms leading to the degeneration of these brain areas; in PD patients, the SN presents with cell loss, while the putamen has DA depletion. In PD models, pharmacological inhibition of MAG lipase has neuroprotective effects in both SH-SY5Y cells treated with MPP+ and chronic MPTP/probenecid mouse models. Although there is no information on the levels of MAG in PD patients, the model studies suggest that MAG lipase inhibition, and thus higher levels of MAG, may be protective for PD.

Endocannabinoids

25MAG include 2-arachidonoylglycerol (2-AG), which is classified as an endocannabinoid. Endocannabinoids are a heterogeneous and thus difficult to classify group of lipids, including not only 2-AG, but also fatty acyl amides, such as anandamide (AEA). They have been previously linked to PD.

26Two studies have reported high AEA levels in the CSF of untreated PD patients, which were restored upon DA treatment. Moreover, higher cannabinoid 1 receptor (CB1R) levels in the putamen, and higher and lower cannabinoid 2 receptor (CB2R) levels have been reported in the SN and putamen of PD patients, respectively. Treatment of PD patients displaying no psychiatric comorbidities with cannabidiol, a naturally occurring cannabinoid constituent of cannabis which appears to lack psychoactive effects, improves quality of life measures, but does not improve Unified Parkinson’s Disease Rating Scale scores. The toxin 6-OHDA has been found to increase CB1R mRNA expression, downregulate CB1R protein density in multiple brain regions or not produce any changes. These differential effects may be explained by the fact that 6-OHDA seems to change the expression of CB1R protein in a region- and time-specific manner. Decreased CB1R mRNA expression has been described in the striatum of reserpine-treated rats and increased CB1R protein density has been observed in PRKN KO female mice. Moreover, CB1R agonists fail to modulate spontaneous excitatory postsynaptic currents in cortical synapses of PINK1 KO mice, which points towards a CB1R dysfunction in these synapses. Hence, there is no agreement on the modulation of CB1R in different PD models and its correlation with the pathogenesis of PD in humans, making further studies necessary.

27Drug-induced animal PD models (using rotenone, 6-OHDA or LPS) show increased CB2R mRNA expression, while a genetic model for PD (LRRK2 KO) does not display changes in CB2R mRNA levels. However, CB2R agonists appear to improve PD-linked impairments in both drug- and genetically-induced rodent PD models. Thus, CB2R upregulation in animal models may reflect a compensatory mechanism, since the administration of CB2R agonists has positive effects on PD-linked pathology.

28Reduced levels of the AEA precursor synthesizing enzyme, N-acyl-transferase, and reduced activities of the AEA membrane transporter and hydrolase have been observed in the striatum of 6-OHDA-treated rats. Moreover, 6-OHDA treatment has been found to both decrease and increase striatal levels of AEA, while MPTP-lesions in monkeys increase striatal AEA levels. Interestingly, an increase of AEA levels, by inhibition of the fatty acid amide hydrolase or administration of AM404 (an endogenous cannabinoid reuptake inhibitor), has neuroprotective effects. Hence, AEA seems to have neuroprotective effects, which have been suggested to be mediated by activation of PI3K and inhibition of JNK signaling.

29All MPTP, rotenone, and reserpine treatments lead to increased 2-AG levels in a time- and region-specific manner in various animal PD models, and 2-AG administration provides protection against MPTP-induced cell death. The endocannabinoid N-arahidonoyl-dopamine has anti-inflammatory effects on both macrophages and activated BV-2 cells and modulates the activity of SN neurons, together with the endocannabinoid-like N-oleoyl-dopamine. This effect could be linked to the fact that, together with an inhibitor of endocannabinoid degradation, administration of a D2 receptor agonist improves motor performance in both a 6-OHDA-and a reserpine-model for PD. Similar to AEA, different members of the endocannabinoid group of lipids may thus be neuroprotective.

3.2. DAG

30Parkinson’s disease patients have decreased plasma levels of DAG, and increased DAG levels in frontal cortex and primary visual cortex. Interestingly, SNPs from the chromosomal region that includes the gene encoding diacylglycerol kinase theta (DGKQ), which mediates the production of phosphatidic acid (PA) from DAG, are associated with PD susceptibility, and DGKQ is linked to increased PA 36:2 production and consequent α-synuclein aggregation. The dysregulation of integral DAG metabolism in PD patients could be related to the observed genetic association between DGKQ and PD.

3.3. TAG

31TAG levels are decreased in serum and plasma of (male) PD patients, even before diagnosis, and higher serum TAG is associated with reduced risk of idiopathic PD. However, other studies have found no differences in blood TAG levels of PD patients and controls. In the primary visual cortex of PD patients, the levels of TAG are decreased. Thus, reduced levels of TAG seem to be linked to PD, although high heterogeneity has been described for TAG in PD patients. Gender, ethnicity, or the technique used to measure TAG could bias the obtained results and contribute to the observed heterogeneity. Nevertheless, the trend from the majority of the results is in line with findings in animal models for PD, in which α-synuclein A53T overexpression leads to deceased serum TAG levels, and 6-OHDA treatment decreases TAG levels in retroperitoneal white adipose tissue. Both rotenone and α-synuclein overexpression have been linked to intracellular deposition of TAG, which forms lipid droplets to which α-synuclein binds, and as such, the turnover of stored TAG is reduced and α-synuclein aggregation is enhanced. In agreement, α-synuclein A53T overexpression in N27 cells leads to increased intracellular levels of TAG. Thus, intracellular deposition and reduced turnover of TAG may explain the reduced levels of this acylglycerol in PD serum. Interestingly, Saccharomyces cereviciae that are unable to synthesize TAG are more tolerant to α-synuclein overexpression.

4. Glycerophospholipids

32Glycerophospholipids, or phospholipids, have a glycerol backbone and a polar head group, which allows their classification into distinct subgroups, known as PA, phosphatidylethanolamine (PE), phosphatidylserine (PS), phosphatidylcholine (PC), phosphatidylinositol (PI), phosphatidyllycerol (PG) and cardiolipin (CL) (Figure 4). The hydrolysis of one acyl derivative gives rise to the lipid species known as lysophospholipids. Glycerophospholipids are key components of the lipid bilayers of cells, and as such play a role in organelle function and processes like endocytosis or mitophagy. Moreover, they also act as signaling molecules and regulate lipid metabolism-related gene expression. Below, we will discuss the current research on glycerophospholipids in PD, more specifically PA, PE, PS, PC, PI, PG and CL, and an overview is given in Supplementary Materials Table S1.

4.1. PA

33One of the best-known glycerophospholipid messengers is PA, which has a broad spectrum of functions, including intracellular vesicular trafficking, cell survival, cytoskeletal organization, neuronal development, and mitochondrial function. Increased plasma PA (18:2/15:0) levels have been suggested as a biomarker for PD. Additionally, PA is known to interact with residues 1–102 of α-synuclein, thus enhancing the formation of multimeric and protease-resistant α-synuclein aggregates. ATP13A2, a lysosomal ATPase, which, when mutated, causes familial PD, constitutes another link between PA and PD. This ATPase requires the interaction with PA, and also PI(3,5)P2, to protect cells against rotenone-induced mitochondrial stress or other PD-related stress conditions, such as exposure to Fe(3+). Furthermore, overexpression of phospholipase D2 appears to induce DA neuronal cell loss via a mechanism involving PA signaling. Given PA’s role in the subcellular distribution and aggregation of α-synuclein, and in ATP13A2-mediated neuroprotection, it would be of interest to study PA levels and its partitioning in the brains of PD patients.

LPA

34Similar to PA, LPA is a lipid mediator in a wide range of biological actions, including cell proliferation, (nervous system) development, and cytokine secretion. Furthermore, LPA is involved in neuronal (DA) differentiation. The expression of LPA receptor 1 is reduced in the SN of a 6-OHDA rat PD model, and an LPA receptor ligand attenuates the MPTP mouse PD model. Unfortunately, nothing is known about LPA in PD patients.

4.2. PE

35The glycerophospholipid PE has a structural role in biological membranes, and it is a regulator of cell division, membrane fusion/fission, and hepatic secretion of very low-density lipoproteins (VLDL). Patients with PD show decreased plasma levels of PE 34:2, and those carrying a GBA mutation have decreased serum levels of PE compared to non-GBA mutation carriers. Decreased total PE levels have also been observed in the SN of PD patients before treatment, in males only after treatment, and in the primary visual cortex. In contrast, increased PE has been found in frontal cortex lipid rafts from PD patients. Of note, one of the enzymes linked to PE synthesis, phosphoethanolamine cytidylyltransferase, is elevated in the SN of PD patients. All findings combined, most evidence points towards decreased levels of PE in PD patients, but the biological implications of the reduced levels need to be examined further.

36In vitro, PE is necessary for the interaction between α-synuclein and biological membranes and for the formation of stable, highly conductive channels by α-synuclein. Both processes might have a role in the normal function of α-synuclein. Accordingly, in yeast and worm models, PE deficiency disrupts α-synuclein homeostasis and induces its aggregation. This deficiency, also seen in PD patients, could be due to increased formation of LPC from PE, which occurs in MPP+ models. Moreover, the inhibition of this metabolic step offers significant protection against cytotoxicity.

4.3. PS

37The glycerophospholipid PE is involved in the triggering of both intracellular and extracellular cascades, such as the activation of kinases or the clearance of apoptotic cells. It plays a role in neuronal survival and differentiation, and neurotransmitter release. Plasma levels of PS 40:4 are decreased in PD patients, but higher levels of PS 36:1, PS 36:1, 36:2, and 38:3, or overall PS, have been found in parkin-mutant fibroblasts, frontal cortex, and primary visual cortex of PD patients, respectively. This is in agreement with the increased PS synthase activity that has been observed in the SN of PD patients. However, some groups reported contrasting findings and claimed that total PS levels in PD SN and frontal cortex lipid rafts are not significantly altered. Yet another interesting finding is that parkin-mutant iPSC-derived neurons have a different subcellular distribution of PS, with increased and decreased PS in the mitochondrial and ER fractions, respectively.

38The exposure of PS on the cellular surface, which acts as an “eat-me” signal for phagocytosis, is triggered by 6-OHDA, rotenone, paraquat, MPP+, and WT, A53T and A30P α-synuclein. Blockade by an antibody against PS is protective in a rotenone-induced neuronal/glial PD model, pointing towards a role of microglial-mediated phagocytosis in PD. This glyceroplipid is known to be associated with the N-terminal- and mid-region of α-synuclein, with some preference for acetylated α-synuclein. This association correlates with membrane penetration, alpha-helix formation and aggregation, and vesicle and liposome binding. Taken together, these findings suggest that PS is a modulator of apoptosis and α-synuclein-mediated pathology.

4.4. PC

39The most-abundant glycerophospholipid in eukaryotic membranes, including mitochondrial membranes, where it plays a structural role, is PC. It is involved in anti-inflammation, cholesterol metabolism, and neuronal differentiation. Decreased levels of PC 34:2 and 46:2, PC 34:5, 36:5, and 38:5, and total PC, have been observed in plasma and frontal cortex from PD patients, and in SN from only male PD patients, respectively. One of the enzymes involved in PC synthesis, PC cytidylyltransferase, is elevated in the SN of PD patients. Interestingly, components of the pathway “PC biosynthesis”, together with “PPAR signaling” components, allowed accurate classification of PD and control samples, highlighting altered PC metabolism as a consistent feature of PD.

40Decreased PC levels have been found in the SN of a mouse model of early PD and in brain tissue from MPTP-treated goldfish. Interestingly, α-synuclein does not bind to but rather remodels pure PC membranes through weak interactions with this phospholipid, and α-synuclein E46K mutants form functionally distinct ion channels in PC membranes. However, others observed binding of the physiologically relevant N-terminally acetylated α-synuclein to pure PC membranes, with preference for highly curved and ordered membranes. Based on these multiple links, the significance of PC metabolism for PD pathology is an interesting and important topic for further study.

LPC

41The most-abundant lysophospholipid in the blood is LPC. Its levels are critically related to major alterations in mitochondrial function (e.g., oxidation rate) and to minor defects in mitochondrial permeability. Of note, saturated acyl LPCs have inflammatory properties, such as leukocyte extravasation and formation of pro-inflammatory mediators, which can be compensated by polyunsaturated acyl LPC, such as LPC 20:4 and LPC 22:6. Higher levels of LPC 16:0 and 18:1 have been found in the lipid profile of parkin-mutant fibroblasts compared to healthy controls. Moreover, increased plasma LPC 18:2 has been suggested as a biomarker for PD.

42Treatment with MPTP induces LPC formation, which leads to cytotoxic changes, dopamine release and inhibition of its uptake, a decreased mitochondrial potential, and increased reactive oxygen species (ROS) formation in PC12 cells. The lysophospholipid LPC inhibits D1 and D2 receptor binding activities in the striatum of rats, inhibits the dopamine transporter, and decreases striatal dopamine turnover rate, leading to hypokinesia. Interestingly, 6-OHDA treatment of rats gives rise to an overall decrease in LPC species, with the exception of LPC 16:0 and 18:1, which are increased in the SN. Thus, LPC has negative effects on the DA system, but LPC levels in PD models seem to depend on the type of pharmacological treatment used and the LPC species involved.

4.5. PI

43The glycerophospholipids PI and PI phosphates are part of intracellular signal transduction systems, but relatively little is known about their role in PD. In humans, higher levels of PI 34:1 and no changes of PI 36:1, 36:2, 38:4, 38:5, 40:5, and 40:6, or no changes in total PI have been observed in parkin-mutant skin fibroblasts, and in the lipid rafts of frontal cortex from PD patients, respectively. Decreased levels of overall PI have been observed in the SN of male PD patients. In rodents, MPTP decreases the expression level of striatal PI-transfer protein, which is involved in the transfer of PI across membranes.

PI Phosphate (PIPx)

44The role of PIPx species in PD is also poorly defined. However, PI and PIP2 effectively influence self-oligomerization of α-synuclein, while α-synuclein seems to prefer binding membranes containing PI(4,5)P2. Moreover, PIP3 is decreased in the nuclear fraction and whole-tissue homogenate, while PIP2 is increased in whole-tissue homogenate of SN from PD patients. As mentioned above, ATP13A2 requires the interaction with PI(3,5)P2 to protect cells against PD-related stress conditions, an interaction that is able to reduce proteasomal inhibitor-induced accumulation of ubiquitin proteins. Future systematic studies on the roles of the various PIPx species are required to understand their function in PD pathogenesis.

4.6. PG

45Less than 1% of total glycerophospholipids in intracellular membranes is composed of PG and it is mainly localized to mitochondrial membranes, where it can be synthesized locally. The levels of total PG are not changed in lipid rafts from PD frontal cortex, while increased PG 32:0 has been described in total extracts of the same brain area. Alpha-synuclein is able to bind PG with various degrees of affinity depending on the variability in its structure (WT ≈ truncated > A53T > A30P), and PG-containing membranes can promote α-synuclein aggregation. Additionally, α-synuclein oligomers are able to induce PG clustering, connect PG-containing vesicles and disrupt PG vesicles through large membrane bilayer defects, rather than through a pore-like mechanism, leading to vesicle docking and fusion problems. Furthermore, low concentrations of α-synuclein inhibit and high concentrations stimulate lipid peroxidation of PG. Unfortunately, information on the levels of PG in animal PD models is lacking.

4.7. CL

46The glycerophospholipid specific for mitochondrial membranes is CL. Here, it plays both a structural and functional role. No changes in total CL levels have been detected in the SN of PD patients. However, PINK1 KO mouse embryonic fibroblasts display decreased CL levels and supplementation with CL rescues mitochondrial dysfunction. Moreover, rotenone induces oxidation of highly unsaturated CL in human peripheral blood lymphocytes, and increases levels of plasma PUFA CLs, but decreases oxidizable PUFA-containing CL levels and increases mono-oxygenated CL species in the SN of rats. A proper CL content in the inner mitochondrial membrane and the presence of acyl side chains are crucial for α-synuclein localization, while CL content in the outer mitochondrial membrane buffers synucleinopathy. Moreover, α-synuclein is able to disrupt artificial membranes containing CL, and its overexpression reduces CL content in MN9D cells and in mouse brain. Additionally, the formation of complexes between CL and α-synuclein, together with cytochrome c, may be a source of oxidative stress. The role that CL plays in the interaction of α-synuclein with membranes and in mitophagy has been previously reviewed.

5. Sphingolipids

47Sphingolipids constitute a family of lipids characterized by the presence of a sphingoid-base backbone. This complex family of compounds includes the sphingoid bases (e.g., sphingosine and sphingosine-1-phosphate), ceramides, phosphosphingolipids (e.g., sphingomyelin (SM)) and glycosphingolipids (e.g., cerebrosides, ganglisodes, and sulfatides) (Figure 5). Sphingolipids are not only structural components of cell membranes, but they also play a role in apoptosis, autophagy, and immune response. Here, we will specifically focus on the involvement of sphingosine(-1-phosphate), ceramide, SM, cerebrosides, gangliosides, and sulfatides, and an overview is given in Supplementary Materials Table S1.

5.1. Sphingosine(-1-Phosphate)

48Sphingosine is a bioactive lipid known to induce apoptosis and regulate endocytosis, while its phosphorylated form, sphingosine-1-phosphate (S1P), promotes cell survival and triggers diverse intracellular signaling pathways through G-protein-coupled receptors. Sphingosine induces the formation of oligomeric α-synuclein species, which serve as template for the formation of endogenous α-synuclein aggregates in human and mammalian neurons. Similarly, S1P accumulation, e.g., due to GBA deficiency, promotes α-synuclein aggregation. Alpha-synuclein itself inhibits the expression and activity of sphingosine kinase 1, the enzyme that catalyzes the phosphorylation of sphingosine to S1P and modulates S1P receptor-mediated signaling. Sphingosine-1-phosphate supplementation of MPP+-treated cells is neuroprotective, and a selective S1P receptor agonist is protective in mouse and cellular models treated with 6-OHDA and rotenone. Therefore, while S1P is protective in animal and cellular PD models, presumably through its pro-survival effects, it is clear that both sphingosine and S1P are linked to α-synuclein aggregation. Unfortunately, the lack of studies on human samples does not allow drawing a conclusion regarding the relevance of these lipids for PD pathogenesis.

5.2. Ceramide

49Ceramide is involved in apoptosis, lipid raft formation, and regulation of the mitochondrial respiratory chain. Both higher and lower plasma levels of ceramide have been reported in PD patients, while lower ceramide 18:0 and no differences in total ceramide levels are observed in their frontal cortex and SN, respectively. Reduced levels of ceramide may be associated with α-synuclein accumulation. This is in line with the finding that reduced and increased levels of ceramide have been observed in the anterior cingulate cortex and primary visual cortex of PD patients, which display and lack α-synuclein aggregation, respectively. Thus, variation in the levels of ceramide in different tissues may be linked to α-synuclein accumulation.

50Mimicking PD with PLA2G6 KO, LRRK2 KO, PINK1 KO or rotenone treatment increases ceramide levels in fly brain, mouse brain, mouse olfactory bulb, and human erythrocytes, respectively. C2-ceramide initiates a series of events leading to neuronal death, including an early inactivation of PI3K/AKT and ERK pathways, followed by activation of JNK, GSK3β activation and neuronal death. Additionally, C2-ceramide induces cytotoxicity and ROS production in neuronal(-like) cells, which can be prevented by WT α-synuclein, PINK1 and DJ-1. However, both in vivo and in vitro C2-ceramide seems to suppress microglial activation, protect neurons against α-synuclein-induced cell injury, and reverse rotenone-induced phosphorylation and aggregation of α-synuclein. An increase in ceramide levels is thus commonly found in animal and cellular models for PD, but its effects are unclear and may be both beneficial and detrimental for different PD-related traits.

5.3. SM

51The most abundant sphingolipid in eukaryotic cells and plasma is SM. It is one of the building blocks of the cellular membrane and a source of bioactive lipids, such as ceramide, ceramide-1-phosphate and S1P, which are involved in inflammation, cell death and autophagy. In the nervous system, SM is a major constituent of myelin. Mutations in sphingomyelinase-1, which lead to SM accumulation, are a risk factor for PD. This feature may be linked to the increase in α-synuclein expression observed upon SM treatment and the presence of SM in LB inclusions. Parkinson’s disease patients carrying GBA mutations have elevated levels of total plasma SM compared to PD patients not carrying the mutation. Moreover, SM 18:1 and SM 26:1 are increased and decreased in the anterior cingulate cortex, respectively, while increased SM levels have been described in the primary visual cortex, and, in males only, in the SN of PD patients. However, no changes have been found in the putamen or cerebellum of sporadic PD patients. The role that SM accumulation appears to play in PD pathogenesis may thus be multifold, being linked to inflammation, autophagy dysfunction, and/or α-synuclein expression and aggregation.

5.4. Cerebrosides

52Cerebrosides are lipids glycosylated via the addition of either glucose or galactose and known to be involved in intracellular membrane transport and cell survival. In PD patients, cerebrosides are increased in plasma (of GBA mutation carriers) and, in males only, in the SN, whereas they are decreased in lipid rafts from the frontal cortex. More specifically, PD patients have increased levels of glucosylceramide in plasma but no changes in cerebroside levels in the temporal cortex, putamen or cerebellum, and decreased levels of galactosylceramide 24:1 and lactosylceramide 18:1 in the frontal cortex. Thus, whereas a consistent coupling between PD and increased cerebrosides in plasma has been found, cerebroside changes in the brain are region dependent and their significance for PD needs to be determined.

53Interestingly, mutations in the enzymes responsible for the degradation of cerebrosoides, namely GBA and galactocerebosides (GALC), which cause Gaucher’s disease and Krabbe’s disease, respectively, have been associated with α-synuclein aggregation and PD. Glucosylceramide, a product that accumulates upon GBA deficiency, destabilizes α-synuclein tetramers and related multimers and frees α-synuclein monomers and leads to cellular toxicity. These effects are caused by colocalization of glucosylceramide with α-synuclein and induction of a pathogenic conformational change of the protein. This promotes aggregation of WT (but not mutated) α-synuclein into a β-sheeted conformation, and conversion of α-synuclein into a proteinase-resistant form. Conversely, α-synuclein inhibits normal activity of GBA, which increases glucosylceramide, creating a feedback loop. Inhibition of glucosylceramide synthase, which decreases glucosylceramide levels, slows α-synuclein accumulation and partially protects mice against MPTP-induced toxicity. Thus, it is well established that glucosylceramide accumulation leads to α-synuclein aggregation and toxicity. Interestingly, aging of WT mice leads to brain accumulation of both glucosylceramide and lactosylceramide, suggesting that age-associated changes in its metabolism might be related to PD onset.

5.5. Gangliosides

54Gangliosides are synthesized by the addition of carbohydrate moieties to lactosylceramide. One of the simplest and most widely distributed ganglioside is monosialodihexosylganglioside (GM3) that consists of lactosylceramide and sialic acid. Gangliosides were initially discovered in the brain where they are involved in neurotransmission, receptor regulation, and stabilization of neural circuits, including the nigro-striatal DA pathway. Parkinson’s disease patients have higher plasma levels of gangliosides, GM3 gangliosides, and N-acetylneuraminic acid-3 (NANA-3) gangliosides than controls. Likewise, higher GM2 and GM3 levels have been detected in parkin-mutant iPSCs compared to controls. However, no accumulation of GM1, GM2 or GM3 has been observed in the putamen or cerebellum of sporadic (or heterozygous GBA-mutation) PD patients, nor in the SN of PD patients. Even a GM1 deficiency, together with decreased expression of ganglioside biosynthetic enzymes (B3GALT4 and ST3GAL2), has been found in the SN from PD patients. Hence, most publications point towards increased gangliosides in plasma of PD patients, but concomitant changes in ganglioside levels have not been observed in their brains.

55Interestingly, GM1 supplementation seems to have a positive disease-modifying effect in PD patients. Also, increased GM1 levels are neuroprotective in MPTP-treated animals. For example, GM1 can partially protect against 6-OHDA treatment and aging-related DA deficits as well. However, studies on MPTP-treated non-human primates have shown that a short treatment with GM1 does not lead to any improvement, while a chronic treatment does have a positive effect, which might be restricted to the surviving DA neurons in the midbrain, rather than due to the prevention of cell death. Mechanistically, GM1 treatment increases DA innervation, dopamine synthesis, and TH expression following an MPTP lesion. Moreover, GM1 inhibits the inflammatory response triggered by 6-OHDA, protects against the toxic intracellular GPR37 aggregates observed in parkinsonism and is involved in the internalization of α-synuclein into microglia. Nonetheless, evidence for an α-synuclein-linked role of GM1 is controversial: in one study it was claimed that GM1 may accelerate α-synuclein aggregation and the formation of proteinase-resistant α-synuclein, but other work demonstrated that it induces alpha-helical structure and inhibits or eliminates α-synuclein fibril formation (depending on the amount of GM1 present). It is also unclear whether membranes containing GM1 interact with α-synuclein. Hence, GM1 is a promising candidate for PD treatment, but further clarification of its specific effects on α-synuclein is urgently needed.

56Only a limited number of studies have analyzed the role of gangliosides other than GM1 in animal and cellular models. For instance, mice lacking GM2/GD2 synthase develop parkinsonism, which can be partially rescued by administration of GM1. However, GM2 accumulation, as seen in Tay Sachs and Sandhoff’s diseases, leads to α-synuclein aggregation. Thus, both deficiency and excess of GM2 may lead to PD-like pathology. Likewise, GM3 accelerates α-synuclein aggregation and regulates α-synuclein-induced channel formation in PC-containing membranes. Furthermore, deletion of GD3 synthase, which decreases production of the pro-apoptotic GD3 ganglioside, protects against MPTP treatment in mice. In contrast, ganglioside GT1b is neurotoxic in nigral DA neurons by triggering nitric oxide release from activated microglia. The gangliosides GD3 and GT1b are unchanged and decreased in the SN of (male) PD patients, respectively. Together, these results indicate that GM3, GD3, and GT1b play aggravating roles in PD pathology. Finally, 1-phenyl-2-decanoylamino-3-morpholino-1-propanol (PDMP, an inhibitor of glycosylceramide synthase that decreases ganglioside content) enhances α-synuclein toxicity, which can be rescued by ganglioside addition.

5.6. Sulfatides

57Sulfatides, which are sulfated galactocerebrosides, form a group of lipids involved in protein trafficking, immune responses and neural plasticity, among others. Higher levels of sulfatides have been detected in the plasma and visual cortex of PD patients, and in the SN of male PD patients. Arylsulfatase A, an enzyme that breaks down sulfatides, has been linked to PD recurrence. However, no changes or reductions in sulfatide levels have been described in lipid rafts from the frontal cortex of PD patients and in brain samples from PD patients, respectively. Thus, most evidence points towards increased sulfatide levels in PD, although a number of studies have not confirmed this finding, suggesting patient, technique and/or tissue-type differences among the various investigations.

6. Sterols

58Sterols are amphipathic lipids synthesized from acetyl-CoA via the β-hydroxy β-methylglutaryl-CoA reductase pathway and containing a fused four-ring core structure (Figure 6). Sterols are known to play a role in immune cell function, influence membrane fluidity and permeability, and serve as signaling molecules and hormones, among others. Here we will review the current findings on sterols in PD, more specifically cholesterol, its precursors, CE, and oxysterols (Supplementary Materials Table S1).

6.1.1. Human Studies on Cholesterol

59Cholesterol intake has been found to be negatively, positively, or not correlated with PD risk. A meta-analysis indicates a lack of association between cholesterol intake and PD. Lower plasma cholesterol has been associated with PD, and confirmed by a meta-analysis, and higher plasma cholesterol levels have been linked to reduced PD risk and slower clinical progression of PD. However, others, including a meta-analysis, have found no association between plasma cholesterol levels and PD or PD risk. Even higher plasma cholesterol levels in PD patients compared to controls have been reported. The differential outcome of these studies could be attributed to factors such as age and gender, among others, since lower plasma cholesterol levels have been reported in PD male patients of more than 55 years compared to controls, a high total cholesterol baseline has been associated with increased risk of PD in subjects of 25–54 years (but not in those above 55), and female PD patients seem to have higher cholesterol levels compared to male PD patients. Thus, proper patient stratification is necessary to determine whether plasma cholesterol is associated with PD, which would point towards defects in cholesterol metabolism.

60In PD patients, no significant changes in cholesterol levels have been observed in the putamen, SN or frontal cortex lipid rafts, while elevated levels of cholesterol have been found in the visual cortex. Finally, decreased cholesterol biosynthesis has been described in fibroblasts from PD patients. The differences in these observations could be related to tissue or brain-region specificities, technique sensitivity, and/or choice of patients. Thus, validation studies and larger cohorts are needed to determine the relevance of cholesterol changes in PD patients and their pathology. Additionally, some studies have found an association between PD and a SNP near the gene SREBF1, which encodes a transcription factor that regulates cholesterol biosynthesis, although other studies could not confirm the findings.

6.1.2. Animal and Cellular Studies on Cholesterol

61In animal and cell model studies, the link between PD and cholesterol has been demonstrated multiple times. For example, the cholesterol biosynthetic pathway controls PRKN expression, which in turn regulates fat (and cholesterol) uptake in PRKN mutant mice and human cells. Additionally, DJ-1 KO mouse embryonic fibroblasts and astrocytes display lower cellular (but not plasma) cholesterol levels and impaired endocytosis, which can be rescued by increased membrane cholesterol. In contrast, GBA KO and PRKN KO cells have increased cholesterol levels, and the N370S GBA mutation leads to cholesterol accumulation in lysosomes, while LRRK2 KO rats have higher serum cholesterol levels. Thus, cholesterol biosynthesis seems to be impaired in PD, but the direction of the change differs among PD etiologies, which could explain part of the variation observed in different studies with PD patients.

62Increased cholesterol reduces cell death and modulates presynaptic DA phenotype by increasing TH and VMAT2 expression in SH-SY5Y cells and enhancing ligand binding of DAT and VMAT2 in the brains from rats and monkeys. However, hypercholesterolemia seems to cause DA neuronal loss and oxidative stress in the SN and the striatum, leading to motor impairment. Together with the observation that cholesterol treatment of (MPP+-treated) SH-SY5Y cells reduces their viability, this finding suggests that the effect of cholesterol levels on PD is dose dependent.

6.1.3. Alpha-Synuclein and Cholesterol

63Alpha-synuclein interacts with cholesterol and cholesterol-containing vesicles, but it is unclear whether cholesterol facilitates the binding of α-synuclein to charge-neutral membranes. Alpha-synuclein-cholesterol interaction seems to be associated with α-synuclein accumulation and aggregation and is a determining factor in α-synuclein’s ability to form pores. Accordingly, reducing cholesterol levels leads to decreased α-synuclein accumulation and damage in the synapse. Hence, high levels of cholesterol aggravate α-synuclein-associated pathology. Furthermore, α-synuclein potentiates cholesterol efflux, antagonizes cholesterol in lipid rafts, and enhances production of oxidative cholesterol metabolites. Finally, A53T-α-synuclein-overexpressing mice have increased levels of serum cholesterol, while WT-α-synuclein-overexpressing mice have upregulation of genes involved in cholesterol biosynthesis in DA neurons from the SN, indicating a tight reciprocal relationship between α-synuclein and cholesterol metabolism.

6.1.4. Statins

64Statins are cholesterol-lowering drugs that have been described to decrease or not affect PD risk. Interestingly, lipophilic, but not hydrophilic, statins increase PD risk. In the current discussion on the contradictory findings regarding the effects of statins not enough attention is paid to confounding factors such as statin indication, statin-type effects or immortal time bias (span of cohort follow-up during which the outcome under study cannot occur), and healthy user effects. In animal and cellular models, atorvastatin pretreatment seems to prevent early effects of MPTP administration in rats, and lovastatin has neuroprotective effects against MPP+ and 6-OHDA and ameliorates α-synuclein accumulation. Similarly, simvastatin is neuroprotective against 6-OHDA and MPTP treatments and increases dopamine content in the striatum. However, negative effects of simvastatin and atorvastatin on MPP+-mediated toxicity have also been reported, which could be explained by the fact that statin lactones, one of the statin metabolites, are able to inhibit mitochondrial complex III, potentiating MPP+ toxicity.

6.2. Cholesterol Precursors

65In PD patients, the cholesterol-synthesizing enzymes isopentenyl diphosphate isomerases 1 and 2 have been observed in LB from the SN of PD patients. The natural cholesterol intermediate squalene seems to prevent toxicity in the striatum of 6-OHDA-treated mice, whereas α-synuclein accumulation enhances squalene production, which could be a cellular response to oxidative damage. A derivative of squalene, squalane, exacerbates 6-OHDA toxicity. The naturally occurring cholesterol precursor lanosterol induces mitochondrial uncoupling and protects DA neurons from cell death in the nigrostriatal region of MPTP-treated mice. Thus, cholesterol precursors seem to have a protective role in PD. Interestingly, inhibitors of both geranylgeranyl transferase (GGTI) and farnesyl transferase (FTI), enzymes that transfer the prenyl group geranylgeranyl or farnesyl to proteins, protect nigrostriatal neurons in MPTP-intoxicated mice.

6.3. CEs

66The esters between cholesterol and fatty acids, CEs, are synthesized from excess cholesterol in the cytosol by the enzyme acetyl-coA acetyltransferase 1, a process that can be reversed by the enzyme cholesteryl ester hydrolase. In PD patients, reduced cholesterol esterifying activity has been detected in fibroblasts and CE 20:5 is reduced in their visual cortex. Interestingly, in C. elegans the ortholog of neutral cholesteryl ester hydrolase 1 attenuates α-synuclein neurotoxicity when sufficient CE is present, while knockdown leads to neurodegeneration. However, GBA KO cells have increased levels of CE 15:1, 22:6, and 24:1, which could reflect either a protective or a pathological mechanism.

6.4. Oxysterols

67The products of cholesterol oxidation, 7beta- and 27-hydroxycholesterol, and 7-ketocholesterol, are elevated in plasma from PD patients. Additionally, 27-hydroxycholesterol CSF levels are increased in a subgroup of PD patients Moreover, increased cholesterol lipid hydroperoxides have been observed in the SN of PD patients. The CSF levels of 24-hydroxycholesterol appear to be correlated with PD duration, but higher levels have also been observed in early stage PD. Conversely, 24-hydroxycholesterol esters are reduced in plasma from PD patients. Of note, TH levels are increased by 24-hydroxycholesterol, while 27-hydroxycholesterol seems to reduce TH expression and increases α-synuclein levels. An unexpected finding was that both 24- and 27-hydroxycholesterol seem to protect against staurosporine-induced cell death. Interestingly, oxysterols, and more specifically 24(S),25-epoxycholesterol, increase DA neuronal differentiation via liver X receptors in both mouse and human embryonic stem cells.

7. Lipoproteins

68Lipoproteins transport triglycerides and cholesteryl esters. Together, these lipids form the core of the lipoprotein, which is further surrounded by glycerophospholipids and free cholesterol. Lipoproteins are classified according to their density, and thus their composition, as high-density lipoproteins (HDL), intermediate-density lipoproteins (IDL), low-density lipoproteins (LDL) or VLDL. Here, we will specifically review the current findings concerning HDL, LDL and VLDL (Supplementary Table S1).

7.1. HDL

69The assembly complex HDL is composed of proteins (around 40%, mainly apolipoprotein A1 (ApoA1), but also apolipoprotein C (ApoC), apolipoprotein E (ApoE), and apolipoprotein J (ApoJ)) and lipids (including around 30% of glycerophospholipids, 25% of cholesterol/CE, and 5% of TAG). The main biological role of HDL is in cargo transport, in particular of lipids and proteins, but it is now also known to bring miRNAs to recipient cells. Lower plasma HDL and ApoA1 levels have been associated with earlier PD onset and higher PD risk, and HDL levels are positively correlated with disease duration. Plasma levels of HDL-cholesterol are lower or not different in PD patients compared to controls. This controversial relationship is complex, as both sex and APOE polymorphisms seem to affect HDL-cholesterol levels in PD patients.

7.2. LDL

70About 20% of LDL consists of proteins (mainly apolipoprotein B (ApoB)) and the remainder consists of lipids (including about 22% of glycerophospholipids, 50% of cholesterol/CE, and 8% of TAG). High LDL-cholesterol levels in plasma are protective for PD and associated with preserved executive and fine motor functions in PD, while lower LDL-cholesterol levels are associated with higher PD risk. One study reported that plasma LDL levels are not different between PD patients and controls. A number of other studies have reported no difference in baseline LDL-cholesterol, and two meta-analyses have found no association. Furthermore, in contrast to HDL, LDL-cholesterol levels do not differ between male and female PD patients. However, one study reported increased LDL-cholesterol levels in PD patients compared to controls. Interestingly, compared to controls PD patients seem to have higher levels of oxidized LDL, which is able to enter neuronal cells and elicit neurotoxicity. Finally, male DJ-1 KO mice have higher LDL-cholesterol levels in serum, which could be due to the fact that the LDLR is a transcriptional target of DJ-1.

7.3. VLDL

71Very low-density lipoproteins are mainly composed of lipids (including around 15% of glycerophospholipids, 20% of cholesterol/CE, and 60% of TAG) and only minor amounts of protein (around 5%, mainly ApoB and ApoC). Parkinson’s disease patients appear to have lower levels of both VLDL and VLDL-cholesterol than controls, but the role of VLDL in PD remains unclear.

8. The Cellular Lipidome

72Above we have given an overview of the changes in lipid composition that have been observed in multiple studies involving PD patients, and animal and cellular PD models. The question arises what the significance of such changes is from a biological point of view. In mammalian cells, about 5% of the genes are involved in the generation and transport of an estimate of 10,000 individual lipid species, which have structural, signaling, and energy storage roles. More specifically, above-mentioned molecules such as glycerophospholipids, sphingolipids, and sterols represent the main components of the cell’s plasma and mitochondrial membranes, endoplasmic reticulum, the Golgi complex, and endosomes. In a dynamic manner, lipid composition defines organelle identity, controls the recruitment of proteins, and lipid bilayer properties, such as thickness, elastic compression, and intrinsic curvature, can be an allosteric regulator of membrane protein function. Alterations in membranes thus dynamically control important processes such as (synaptic) vesicle trafficking, endocytosis-exocytosis or α-synuclein aggregation, processes that have already been associated with PD.

73Lipids also play an important role in intracellular and intercellular signaling in the brain by direct interaction with receptors and other signal-transducing proteins that regulate integral physiological processes linked to PD. For example, PUFA are involved in inflammation, neurogenesis, and neuroprotection. Endocannabinoids are lipid-based retrograde neurotransmitters that modulate synaptic plasticity, and LPA modulates processes like proliferation, survival and migration. Additionally, although most energy consumed by brain cells comes from glucose, lipids have been suggested to provide up to 20% of the total energy consumption of the adult brain. Therefore, changes in lipid composition or content, such as the ones that have been described here for PD, can have vast consequences for key processes in the maintenance of normal neuronal and brain function. However, unlike what holds for genes and proteins, most lipid species cannot be associated with specific functions: their role is dictated by the concentration and location of individual lipid species, and, most importantly, by their interaction with other lipid species. Since most of the available information is a description of changes in lipid concentration, firm conclusions regarding the effects of these changes are hard to draw.

74This lack of precise knowledge regarding the (patho)biological significance of lipidome abnormalities is predominantly caused by the fact that lipids form a vast and enormously complex group of biomolecules. This creates two major challenges. First, it is currently very difficult—if not impossible—to characterize all lipids present in the lipidome of a sample, due to limitations in the separation methods. This precludes simultaneous analysis of all lipid classes, which is especially hindered by the presence of isomeric (i.e., same mass) lipids. Second, no methodology is currently available to accurately determine the concentrations of the various lipid species. This lack of information hampers the interpretation of lipidomic studies and the creation of reliable databases that, on its turn, impedes the identification of pathways in which a combination of lipid species plays a role.

75As mentioned, not only their composition in the lipidome but also the tissue distribution and intracellular localization of individual lipids are crucial for their function, which makes it of great importance to develop techniques to identify and quantify lipids at the single-cell level and with the spatial organization of the cell still intact. These developments will help to elucidate the interplay of different lipid species in a time- and location-dependent manner both in health and disease. Indeed, it would allow us to obtain more information about (i) the lipidomes of various cell types, which are now identified in growing numbers within different tissues and organs by RNAseq, and (ii) the dynamic changes in lipidome composition that are associated with disease progression. Unfortunately, proper sample preparation, even more than the detection limits for lipids in mass-spectrometry, currently forms the biggest barrier to develop effective single-cell lipidomics. Moreover, the interplay between lipids and other biomolecules necessitates the integration of lipidomics with other omics strategies.

76It is also important to note that the lipidome composition is not only defined by the activity of genes involved in lipid metabolism, but also strongly depends on exogenous factors. These include (1) the direct dietary intake of lipids and lipid precursors from food, (2) life-style factors, i.e., exercise, sleep patterns, and intrinsic and extrinsic motivation factors that determine the choice of food composition, and (3) the effects of drugs that affect metabolism or cell behavior. For example, accumulating evidence suggests that tight bidirectional interactions exist between dietary lipids and composition and structure of the gastrointestinal tract microbiota. This could be especially relevant for PD, since dysbiosis (i.e., the change in microbiota structure relative to that found in healthy individuals), has been repeatedly observed in PD patients from early stages of the disease onwards.

77Filling in the current gaps in lipidomics technology and knowledge is crucial to exploit its potential to help us further understand the molecular mechanisms underlying PD, better define its stages and classification, and identify biomarkers, create dietary interventions, or perform compound screening, preclinical testing and monitoring of drug responses.

9. Conclusions

78From this review, it is clear that a strong correlation exists between PD and abnormalities in lipid metabolism. More specifically, there is an association between PD and the levels of fatty acyls (SFA, MUFA, PUFA, a number of eicosanoids, and acylcarnitine), glycerolipids (MAG, DAG, and TAG), glycerophospholipids (PA, LPA, PE, PS, PC, LPC, PI, PIPx, PG, and CL), sphingolipids (sphingosine(-1P), ceramide, SM, cerebrosides, gangliosides, and sulfatides), sterols (cholesterol precursors, cholesterol, CE, and oxysterols) and lipoproteins (HDL, LDL, and VLDL). Furthermore, there is a conspicuous relationship between the folding, aggregation, and distribution of α-synuclein and the lipids that drive some of the neuropathological features of PD. Yet, it is presently unclear whether links exist between PD and some eicosanoids (eoxins, thromboxanes, oxoeicoanoids, hepoxilins, lipoxins, and epoxyeiconsatetraenoic acid), glycerophospholipids (lysoPE, lysoPS, lysoPI, lysoPG, lysoCL, and Bis(monoacylglycero)phosphate), sphingolipids (globosides), and lipoproteins (IDL).

79One of the main concerns regarding the findings summarized in this review is that most lipid classes have not been consistently found to be associated with PD. Variables such as sex, age, PD etiology, specific DNA polymorphisms or the microbiome may have influenced the findings. Thus, proper stratification of PD patients is necessary to understand the biological implications of the lipid changes observed. Additionally, more accurate description of the lipid profiles of plasma, CSF and/or fibroblasts from PD patients will help to classify the patients more accurately.

80A further concern is that most studies have focused on plasma levels of lipids, but these may not correlate with their brain levels, e.g., levels of ganglioside species are increased in plasma but not in brains of PD patients. Thus, CSF (and brain) lipidomes of PD patients have to be determined to get insight into the actual pathological lipid composition and processes. Moreover, it is often unclear whether the changes in the levels of lipid species reflect a pathological or rather a compensatory mechanism. Finally, studies on cellular and animal PD models do not always show the same directionality of lipid level changes as found in studies on PD patients.

81In conclusion, ample evidence for a central role of lipids in PD is available, but current data yield a picture that is still too fragmented. This hinders the unraveling of the specific pathological mechanisms in which lipids are involved. Technological advances to better characterize the lipidome and explore the functions of specific lipid species, together with additional studies on CSF and/or brain tissue from PD patients are now urgently needed to further our understanding of the pathobiology of the relationship between PD and lipids and will help us to identify biomarkers and druggable targets for the development of disease-modifying therapies for this devastating neurodegenerative disease.

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83.
Mori M.A., Delattre A.M., Carabelli B., Pudell C., Bortolanza M., Staziaki P.V., Visentainer J.V., Montanher P.F., Del Bel E.A., Ferraz A.C. Neuroprotective effect of omega-3 polyunsaturated fatty acids in the 6-OHDA model of Parkinson’s disease is mediated by a reduction of inducible nitric oxide synthase. Nutr. Neurosci. 2018;21:341-351.
Not in our library10.1080/1028415x.2017.1290928
84.
Delattre A.M., Kiss A., Szawka R.E., Anselmo-Franci J.A., Bagatini P.B., Xavier L.L., Rigon P., Achaval M., Iagher F., de David C., et al. Evaluation of chronic omega-3 fatty acids supplementation on behavioral and neurochemical alterations in 6-hydroxydopamine-lesion model of Parkinson’s disease. Neurosci. Res. 2010;66:256-264.
Not in our library10.1016/j.neures.2009.11.006
85.
Kabuto H., Amakawa M., Mankura M., Yamanushi T.T., Mori A. Docosahexaenoic acid ethyl ester enhances 6-hydroxydopamine-induced neuronal damage by induction of lipid peroxidation in mouse striatum. Neurochem. Res. 2009;34:1299-1303.
Not in our library10.1007/s11064-008-9909-0
86.
Anderson E.J., Katunga L.A., Willis M.S. Mitochondria as a source and target of lipid peroxidation products in healthy and diseased heart. Clin. Exp. Pharmacol. Physiol. 2012;39:179-193.
Not in our library10.1111/j.1440-1681.2011.05641.x
87.
Shamoto-Nagai M., Hisaka S., Naoi M., Maruyama W. Modification of α-synuclein by lipid peroxidation products derived from polyunsaturated fatty acids promotes toxic oligomerization: Its relevance to Parkinson disease. J. Clin. Biochem. Nutr. 2018;62:207-212.
Not in our library10.3164/jcbn.18-25
88.
Lipid peroxidation is essential for α‐synuclein‐induced cell death · 2015
No notice
89.
Shchepinov M.S., Chou V.P., Pollock E., Langston J.W., Cantor C.R., Molinari R.J., Manning-Boğ A.B. Isotopic reinforcement of essential polyunsaturated fatty acids diminishes nigrostriatal degeneration in a mouse model of Parkinson’s disease. Toxicol. Lett. 2011;207:97-103.
Not in our library10.1016/j.toxlet.2011.07.020
90.
Kinghorn K.J., Castillo-Quan J.I., Bartolome F., Angelova P.R., Li L., Pope S., Cochemé H.M., Khan S., Asghari S., Bhatia K.P., et al. Loss of PLA2G6 leads to elevated mitochondrial lipid peroxidation and mitochondrial dysfunction. Brain. 2015;138:1801-1816.
Not in our library10.1093/brain/awv132
91.
Denny Joseph K.M., Muralidhara. Combined oral supplementation of fish oil and quercetin enhances neuroprotection in a chronic rotenone rat model: Relevance to Parkinson’s disease. Neurochem. Res. 2015;40:894-905.
Not in our library10.1007/s11064-015-1542-0
92.
Lee H.J., Bazinet R.P., Rapoport S.I., Bhattacharjee A.K. Brain arachidonic acid cascade enzymes are upregulated in a rat model of unilateral Parkinson disease. Neurochem. Res. 2010;35:613-619.
Not in our library10.1007/s11064-009-0106-6
93.
Chalimoniuk M., Stolecka A., Ziemińska E., Stepień A., Langfort J., Strosznajder J.B. Involvement of multiple protein kinases in cPLA2 phosphorylation, arachidonic acid release, and cell death in in vivo and in vitro models of 1-methyl-4-phenylpyridinium-induced parkinsonism—The possible key role of PKG. J. Neurochem. 2009;110:307-317.
Not in our library10.1111/j.1471-4159.2009.06147.x
94.
Tang K.S. Protective effect of arachidonic acid and linoleic acid on 1-methyl-4-phenylpyridinium-induced toxicity in PC12 cells. Lipids Health Dis. 2014;13:197.
Not in our library10.1186/1476-511x-13-197
95.
Shioda N., Yabuki Y., Kobayashi Y., Onozato M., Owada Y., Fukunaga K. FABP3 protein promotes α-synuclein oligomerization associated with 1-methyl-1, 2, 3, 6-tetrahydropiridine-induced neurotoxicity. J. Biol. Chem. 2014;289:18957-18965.
Not in our library10.1074/jbc.m113.527341
96.
Wang Y., Plastina P., Vincken J.P., Jansen R., Balvers M., Ten Klooster J.P., Gruppen H., Witkamp R., Meijerink J. N-Docosahexaenoyl Dopamine, an Endocannabinoid-like Conjugate of Dopamine and the n-3 Fatty Acid Docosahexaenoic Acid, Attenuates Lipopolysaccharide-Induced Activation of Microglia and Macrophages via COX-2. ACS Chem. Neurosci. 2017;8:548-557.
Not in our library10.1021/acschemneuro.6b00298
97.
Ben Gedalya T., Loeb V., Israeli E., Altschuler Y., Selkoe D.J., Sharon R. Alpha-synuclein and polyunsaturated fatty acids promote clathrin-mediated endocytosis and synaptic vesicle recycling. Traffic. 2009;10:218-234.
Not in our library10.1111/j.1600-0854.2008.00853.x
98.
Darios F., Ruipérez V., López I., Villanueva J., Gutierrez L.M., Davletov B. Alpha-synuclein sequesters arachidonic acid to modulate SNARE-mediated exocytosis. EMBO Rep. 2010;11:528-533.
Not in our library10.1038/embor.2010.66
99.
Karube H., Sakamoto M., Arawaka S., Hara S., Sato H., Ren C.H., Goto S., Koyama S., Wada M., Kawanami T., et al. N-terminal region of alpha-synuclein is essential for the fatty acid-induced oligomerization of the molecules. FEBS Lett. 2008;582:3693-3700.
Not in our library10.1016/j.febslet.2008.10.001
100.
Israeli E., Sharon R. Beta-synuclein occurs in vivo in lipid-associated oligomers and forms hetero-oligomers with alpha-synuclein. J. Neurochem. 2009;108:465-474.
Not in our library10.1111/j.1471-4159.2008.05776.x
101.
Sharon R., Bar-Joseph I., Frosch M.P., Walsh D.M., Hamilton J.A., Selkoe D.J. The formation of highly soluble oligomers of alpha-synuclein is regulated by fatty acids and enhanced in Parkinson’s disease. Neuron. 2003;37:583-595.
Not in our library10.1016/s0896-6273(03)00024-2
102.
Perrin R.J., Woods W.S., Clayton D.F., George J.M. Exposure to long chain polyunsaturated fatty acids triggers rapid multimerization of synucleins. J. Biol. Chem. 2001;276:41958-41962.
Not in our library10.1074/jbc.m105022200
103.
Assayag K., Yakunin E., Loeb V., Selkoe D.J., Sharon R. Polyunsaturated fatty acids induce alpha-synuclein-related pathogenic changes in neuronal cells. Am. J. Pathol. 2007;171:2000-2011.
Not in our library10.2353/ajpath.2007.070373
104.
Broersen K., van den Brink D., Fraser G., Goedert M., Davletov B. Alpha-synuclein adopts an alpha-helical conformation in the presence of polyunsaturated fatty acids to hinder micelle formation. Biochemistry. 2006;45:15610-15616.
Not in our library10.1021/bi061743l
105.
Yakunin E., Loeb V., Kisos H., Biala Y., Yehuda S., Yaari Y., Selkoe D.J., Sharon R. A-synuclein neuropathology is controlled by nuclear hormone receptors and enhanced by docosahexaenoic acid in a mouse model for Parkinson’s disease. Brain Pathol. 2012;22:280-294.
Not in our library10.1111/j.1750-3639.2011.00530.x
106.
Fu Y., Zhen J., Lu Z. Synergetic Neuroprotective Effect of Docosahexaenoic Acid and Aspirin in SH-Y5Y by Inhibiting miR-21 and Activating RXRα and PPARα. DNA Cell Biol. 2017;36:482-489.
Not in our library10.1089/dna.2017.3643
107.
De Franceschi G., Frare E., Pivato M., Relini A., Penco A., Greggio E., Bubacco L., Fontana A., de Laureto P.P. Structural and morphological characterization of aggregated species of α-synuclein induced by docosahexaenoic acid. J. Biol. Chem. 2011;286:22262-22274.
Not in our library10.1074/jbc.m110.202937
108.
Fecchio C., De Franceschi G., Relini A., Greggio E., Dalla Serra M., Bubacco L., de Laureto P.P. α-Synuclein oligomers induced by docosahexaenoic acid affect membrane integrity. PLoS ONE. 2013;8:e82732.
Not in our library10.1371/journal.pone.0082732
109.
De Franceschi G., Frare E., Bubacco L., Mammi S., Fontana A., de Laureto P.P. Molecular insights into the interaction between alpha-synuclein and docosahexaenoic acid. J. Mol. Biol. 2009;394:94-107.
Not in our library10.1016/j.jmb.2009.09.008
110.
Broersen K., Ruiperez V., Davletov B. Structural and Aggregation Properties of Alpha-Synuclein Linked to Phospholipase A2 Action. Protein Pept. Lett. 2018;25:368-378.
Not in our library10.2174/0929866525666180326120052
111.
Iljina M., Tosatto L., Choi M.L., Sang J.C., Ye Y., Hughes C.D., Bryant C.E., Gandhi S., Klenerman D. Arachidonic acid mediates the formation of abundant alpha-helical multimers of alpha-synuclein. Sci. Rep. 2016;6:33928.
Not in our library10.1038/srep33928
112.
Jiang P., Gan M., Yen S.H.C. Dopamine prevents lipid peroxidation-induced accumulation of toxic α-synuclein oligomers by preserving autophagy-lysosomal function. Front. Cell. Neurosci. 2013;7:81.
Not in our library10.3389/fncel.2013.00081
113.
Liu X., Yamada N., Maruyama W., Osawa T. Formation of dopamine adducts derived from brain polyunsaturated fatty acids: Mechanism for Parkinson disease. J. Biol. Chem. 2008;283:34887-34895.
Not in our library10.1074/jbc.m805682200
114.
Muntané G., Janué A., Fernandez N., Odena M.A., Oliveira E., Boluda S., Porero-Otin M., Naudí A., Boada J., Pamplona R., et al. Modification of brain lipids but not phenotype in alpha-synucleinopathy transgenic mice by long-term dietary n-3 fatty acids. Neurochem. Int. 2010;56:318-328.
Not in our library10.1016/j.neuint.2009.10.015
115.
Coulombe K., Kerdiles O., Tremblay C., Emond V., Lebel M., Boulianne A.S., Plourde M., Cicchetti F., Calon F. Impact of DHA intake in a mouse model of synucleinopathy. Exp. Neurol. 2018;301:39-49.
Not in our library10.1016/j.expneurol.2017.12.002
116.
De Franceschi G., Fecchio C., Sharon R., Schapira A.H.V., Proukakis C., Bellotti V., de Laureto P.P. α-Synuclein structural features inhibit harmful polyunsaturated fatty acid oxidation, suggesting roles in neuroprotection. J. Biol. Chem. 2017;292:6927-6937.
Not in our library10.1074/jbc.m116.765149
117.
Fecchio C., Palazzi L., de Laureto P.P. α-Synuclein and Polyunsaturated Fatty Acids: Molecular Basis of the Interaction and Implication in Neurodegeneration. Molecules. 2018;23:1531.
Not in our library10.3390/molecules23071531
118.
Dennis E.A., Norris P.C. Eicosanoid storm in infection and inflammation. Nat. Rev. Immunol. 2015;15:511-523.
Not in our library10.1038/nri3859
119.
Pretorius E., Swanepoel A.C., Buys A.V., Vermeulen N., Duim W., Kell D.B. Eryptosis as a marker of Parkinson’s disease. Aging. 2014;6:788-819.
Not in our library10.18632/aging.100695
120.
Teismann P., Tieu K., Choi D.K., Wu D.C., Naini A., Hunot S., Vila M., Jackson-Lewis V., Przedborski S. Cyclooxygenase-2 is instrumental in Parkinson’s disease neurodegeneration. Proc. Natl. Acad. Sci. USA. 2003;100:5473-5478.
Not in our library10.1073/pnas.0837397100
121.
Yu S.Y., Zuo L.J., Wang F., Chen Z.J., Hu Y., Wang Y.J., Wang X.M., Zhang W. Potential biomarkers relating pathological proteins, neuroinflammatory factors and free radicals in PD patients with cognitive impairment: A cross-sectional study. BMC Neurol. 2014;14:113.
Not in our library10.1186/1471-2377-14-113
122.
Mattammal M.B., Strong R., Lakshmi V.M., Chung H.D., Stephenson A.H. Prostaglandin H synthetase-mediated metabolism of dopamine: Implication for Parkinson’s disease. J. Neurochem. 1995;64:1645-1654.
Not in our library10.1046/j.1471-4159.1995.64041645.x
123.
Geng Y., Fang M., Wang J., Yu H., Hu Z., Yew D.T., Chen W. Triptolide down-regulates COX-2 expression and PGE2 release by suppressing the activity of NF-κB and MAP kinases in lipopolysaccharide-treated PC12 cells. Phytother. Res. 2012;26:337-343.
Not in our library10.1002/ptr.3538
124.
Zeng K.W., Zhang T., Fu H., Liu G.X., Wang X.M. Schisandrin B exerts anti-neuroinflammatory activity by inhibiting the Toll-like receptor 4-dependent MyD88/IKK/NF-κB signaling pathway in lipopolysaccharide-induced microglia. Eur. J. Pharmacol. 2012;692:29-37.
Not in our library10.1016/j.ejphar.2012.05.030
125.
Bai L., Zhang X., Li X., Liu N., Lou F., Ma H., Luo X., Ren Y. Somatostatin prevents lipopolysaccharide-induced neurodegeneration in the rat substantia nigra by inhibiting the activation of microglia. Mol. Med. Rep. 2015;12:1002-1008.
Not in our library10.3892/mmr.2015.3494
126.
Fu Q., Song R., Yang Z., Shan Q., Chen W. 6-Hydroxydopamine induces brain vascular endothelial inflammation. IUBMB Life. 2017;69:887-895.
Not in our library10.1002/iub.1685
127.
Wang H.M., Zhang T., Li Q., Huang J.K., Chen R.F., Sun X.J. Inhibition of glycogen synthase kinase-3β by lithium chloride suppresses 6-hydroxydopamine-induced inflammatory response in primary cultured astrocytes. Neurochem. Int. 2013;63:345-353.
Not in our library10.1016/j.neuint.2013.07.003
128.
Yildirim F.B., Ozsoy O., Tanriover G., Kaya Y., Ogut E., Gemici B., Dilmac S., Ozkan A., Agar A., Aslan M. Mechanism of the beneficial effect of melatonin in experimental Parkinson’s disease. Neurochem. Int. 2014;79:1-11.
Not in our library10.1016/j.neuint.2014.09.005
129.
Zhou F., Yao H.H., Wu J.Y., Ding J.H., Sun T., Hu G. Opening of microglial K(ATP) channels inhibits rotenone-induced neuroinflammation. J. Cell. Mol. Med. 2008;12:1559-1570.
Not in our library10.1111/j.1582-4934.2007.00144.x
130.
Hu J.H., Zhu X.Z. Rotenone-induced neurotoxicity of THP-1 cells requires production of reactive oxygen species and activation of phosphatidylinositol 3-kinase. Brain Res. 2007;1153:12-19.
Not in our library10.1016/j.brainres.2007.03.006
131.
Wang T., Pei Z., Zhang W., Liu B., Langenbach R., Lee C., Wilson B., Reece J.M., Miller D.S., Hong J.S. MPP+-induced COX-2 activation and subsequent dopaminergic neurodegeneration. FASEB J. 2005;19:1134-1136.
Not in our library10.1096/fj.04-2457fje
132.
Ozsoy O., Tanriover G., Derin N., Uysal N., Demir N., Gemici B., Kencebay C., Yargicoglu P., Agar A., Aslan M. The effect of docosahexaenoic Acid on visual evoked potentials in a mouse model of Parkinson’s disease: The role of cyclooxygenase-2 and nuclear factor kappa-B. Neurotox. Res. 2011;20:250-262.
Not in our library10.1007/s12640-011-9238-y
133.
Liu J., Zhou Y., Wang Y., Fong H., Murray T.M., Zhang J. Identification of proteins involved in microglial endocytosis of alpha-synuclein. J. Proteome Res. 2007;6:3614-3627.
Not in our library10.1021/pr0701512
134.
Zhang W., Wang T., Pei Z., Miller D.S., Wu X., Block M.L., Wilson B., Zhang W., Zhou Y., Hong J.S., et al. Aggregated alpha-synuclein activates microglia: A process leading to disease progression in Parkinson’s disease. FASEB J. 2005;19:533-542.
Not in our library10.1096/fj.04-2751com
135.
Branchi I., D’Andrea I., Armida M., Carnevale D., Ajmone-Cat M.A., Pèzzola A., Potenza R.L., Morgese M.G., Cassano T., Minghetti L., et al. Striatal 6-OHDA lesion in mice: Investigating early neurochemical changes underlying Parkinson’s disease. Behav. Brain Res. 2010;208:137-143.
Not in our library10.1016/j.bbr.2009.11.020
136.
Dey I., Lejeune M., Chadee K. Prostaglandin E2 receptor distribution and function in the gastrointestinal tract. Br. J. Pharmacol. 2006;149:611-623.
Not in our library10.1038/sj.bjp.0706923
137.
Ahmad A.S., Maruyama T., Narumiya S., Doré S. PGE2 EP1 receptor deletion attenuates 6-OHDA-induced Parkinsonism in mice: Old switch, new target. Neurotox. Res. 2013;23:260-266.
Not in our library10.1007/s12640-013-9381-8
138.
Carrasco E., Casper D., Werner P. PGE(2) receptor EP1 renders dopaminergic neurons selectively vulnerable to low-level oxidative stress and direct PGE(2) neurotoxicity. J. Neurosci. Res. 2007;85:3109-3117.
Not in our library10.1002/jnr.21425
139.
Carrasco E., Werner P., Casper D. Prostaglandin receptor EP2 protects dopaminergic neurons against 6-OHDA-mediated low oxidative stress. Neurosci. Lett. 2008;441:44-49.
Not in our library10.1016/j.neulet.2008.05.111
140.
Pradhan S.S., Salinas K., Garduno A.C., Johansson J.U., Wang Q., Manning-Bog A., Andreasson K.I. Anti-Inflammatory and Neuroprotective Effects of PGE2 EP4 Signaling in Models of Parkinson’s Disease. J. Neuroimmune Pharmacol. 2017;12:292-304.
Not in our library10.1007/s11481-016-9713-6
141.
Ashley A.K., Hinds A.I., Hanneman W.H., Tjalkens R.B., Legare M.E. DJ-1 mutation decreases astroglial release of inflammatory mediators. Neurotoxicology. 2016;52:198-203.
Not in our library10.1016/j.neuro.2015.12.007
142.
Parga J.A., García-Garrote M., Martínez S., Raya Á., Labandeira-García J.L., Rodríguez-Pallares J. Prostaglandin EP2 Receptors Mediate Mesenchymal Stromal Cell-Neuroprotective Effects on Dopaminergic Neurons. Mol. Neurobiol. 2018;55:4763-4776.
Not in our library10.1007/s12035-017-0681-5
143.
Wang X., Qin Z.H., Leng Y., Wang Y., Jin X., Chase T.N., Bennett M.C. Prostaglandin A1 inhibits rotenone-induced apoptosis in SH-SY5Y cells. J. Neurochem. 2002;83:1094-1102.
Not in our library10.1046/j.1471-4159.2002.01224.x
144.
Fujimori K., Fukuhara A., Inui T., Allhorn M. Prevention of paraquat-induced apoptosis in human neuronal SH-SY5Y cells by lipocalin-type prostaglandin D synthase. J. Neurochem. 2012;120:279-291.
Not in our library10.1111/j.1471-4159.2011.07570.x
145.
Tsai M.J., Weng C.F., Yu N.C., Liou D.Y., Kuo F.S., Huang M.C., Tam K., Shyue S.K., Cheng H. Enhanced prostacyclin synthesis by adenoviral gene transfer reduced glial activation and ameliorated dopaminergic dysfunction in hemiparkinsonian rats. Oxid. Med. Cell. Longev. 2013;2013:649809.
Not in our library10.1155/2013/649809
146.
Ogburn K.D., Figueiredo-Pereira M.E. Cytoskeleton/endoplasmic reticulum collapse induced by prostaglandin J2 parallels centrosomal deposition of ubiquitinated protein aggregates. J. Biol. Chem. 2006;281:23274-23284.
Not in our library10.1074/jbc.m600635200
147.
Shivers K.Y., Nikolopoulou A., Machlovi S.I., Vallabhajosula S., Figueiredo-Pereira M.E. PACAP27 prevents Parkinson-like neuronal loss and motor deficits but not microglia activation induced by prostaglandin J2. Biochim. Biophys. Acta. 2014;1842:1707-1719.
Not in our library10.1016/j.bbadis.2014.06.020
148.
Pierre S.R., Lemmens M.A.M., Figueiredo-Pereira M.E. Subchronic infusion of the product of inflammation prostaglandin J2 models sporadic Parkinson’s disease in mice. J. Neuroinflamm. 2009;6:18.
Not in our library10.1186/1742-2094-6-18
149.
Zhao H., Wang C., Zhao N., Li W., Yang Z., Liu X., Le W., Zhang X. Potential biomarkers of Parkinson’s disease revealed by plasma metabolic profiling. J. Chromatogr. B Anal. Technol. Biomed. Life Sci. 2018;1081–1082:101-108.
Not in our library10.1016/j.jchromb.2018.01.025
150.
Kang K.H., Liou H.H., Hour M.J., Liou H.C., Fu W.M. Protection of dopaminergic neurons by 5-lipoxygenase inhibitor. Neuropharmacology. 2013;73:380-387.
Not in our library10.1016/j.neuropharm.2013.06.014
151.
Nagarajan V.B., Marathe P.A. Effect of montelukast in experimental model of Parkinson’s disease. Neurosci. Lett. 2018;682:100-105.
Not in our library10.1016/j.neulet.2018.05.052
152.
Mansour R.M., Ahmed M.A.E., El-Sahar A.E., El Sayed N.S. Montelukast attenuates rotenone-induced microglial activation/p38 MAPK expression in rats: Possible role of its antioxidant, anti-inflammatory and antiapoptotic effects. Toxicol. Appl. Pharmacol. 2018;358:76-85.
Not in our library10.1016/j.taap.2018.09.012
153.
Chou V.P., Ko N., Holman T.R., Manning-Boğ A.B. Gene-environment interaction models to unmask susceptibility mechanisms in Parkinson’s disease. J. Vis. Exp. 2014;e50960.
Not in our library10.3791/50960
154.
Searles Nielsen S., Bammler T.K., Gallagher L.G., Farin F.M., Longstreth W., Franklin G.M., Swanson P.D., Checkoway H. Genotype and age at Parkinson disease diagnosis. Int. J. Mol. Epidemiol. Genet. 2013;4:61-69.
Not in our library
155.
Lakkappa N., Krishnamurthy P.T., Hammock B.D., Velmurugan D., Bharath M.M.S. Possible role of Epoxyeicosatrienoic acid in prevention of oxidative stress mediated neuroinflammation in Parkinson disorders. Med. Hypotheses. 2016;93:161-165.
Not in our library10.1016/j.mehy.2016.06.003
156.
Terashvili M., Sarkar P., Nostrand M.V., Falck J.R., Harder D.R. The protective effect of astrocyte-derived 14, 15-epoxyeicosatrienoic acid on hydrogen peroxide-induced cell injury in astrocyte-dopaminergic neuronal cell line co-culture. Neuroscience. 2012;223:68-76.
Not in our library10.1016/j.neuroscience.2012.07.045
157.
Qin X., Wu Q., Lin L., Sun A., Liu S., Li X., Cao X., Gao T., Luo P., et al. Soluble Epoxide Hydrolase Deficiency or Inhibition Attenuates MPTP-Induced Parkinsonism. Mol. Neurobiol. 2015;52:187-195.
Not in our library10.1007/s12035-014-8833-3
158.
Ren Q., Ma M., Yang J., Nonaka R., Yamaguchi A., Ishikawa K.I., Kobayashi K., Murayama S., Hwang S.H., Saiki S., et al. Soluble epoxide hydrolase plays a key role in the pathogenesis of Parkinson’s disease. Proc. Natl. Acad. Sci. USA. 2018;115:E5815-E5823.
Not in our library10.1073/pnas.1802179115
159.
Lakkappa N., Krishnamurthy P.T., Yamjala K., Hwang S.H., Hammock B.D., Babu B. Evaluation of antiparkinson activity of PTUPB by measuring dopamine and its metabolites in Drosophila melanogaster: LC-MS/MS method development. J. Pharm. Biomed. Anal. 2018;149:457-464.
Not in our library10.1016/j.jpba.2017.11.043
160.
Connolly J., Siderowf A., Clark C.M., Mu D., Pratico D. F2 isoprostane levels in plasma and urine do not support increased lipid peroxidation in cognitively impaired Parkinson disease patients. Cogn. Behav. Neurol. 2008;21:83-86.
Not in our library10.1097/wnn.0b013e31817995e7
161.
Lee C.Y.J., Seet R.C.S., Huang S.H., Long L.H., Halliwell B. Different patterns of oxidized lipid products in plasma and urine of dengue fever, stroke, and Parkinson’s disease patients: Cautions in the use of biomarkers of oxidative stress. Antioxid. Redox Signal. 2009;11:407-420.
Not in our library10.1089/ars.2008.2179
162.
Seet R.C.S., Lee C.Y.J., Lim E.C.H., Tan J.J.H., Quek A.M.L., Chong W.L., Looi W.F., Huang S.H., Wang H., Chang Y.H., et al. Oxidative damage in Parkinson disease: Measurement using accurate biomarkers. Free Radic. Biol. Med. 2010;48:560-566.
Not in our library10.1016/j.freeradbiomed.2009.11.026
163.
Irizarry M.C., Yao Y., Hyman B.T., Growdon J.H., Praticò D. Plasma F2A isoprostane levels in Alzheimer’s and Parkinson’s disease. Neurodegener. Dis. 2007;4:403-405.
Not in our library10.1159/000107699
164.
Fessel J.P., Hulette C., Powell S., Roberts L.J., Zhang J. Isofurans, but not F2-isoprostanes, are increased in the substantia nigra of patients with Parkinson’s disease and with dementia with Lewy body disease. J. Neurochem. 2003;85:645-650.
Not in our library10.1046/j.1471-4159.2003.01709.x
165.
Neely M.D., Davison C.A., Aschner M., Bowman A.B. From the Cover: Manganese and Rotenone-Induced Oxidative Stress Signatures Differ in iPSC-Derived Human Dopamine Neurons. Toxicol. Sci. 2017;159:366-379.
Not in our library10.1093/toxsci/kfx145
166.
Xu J., Gao X., Yang C., Chen L., Chen Z. Resolvin D1 Attenuates Mpp+-Induced Parkinson Disease via Inhibiting Inflammation in PC12 Cells. Med. Sci. Monit. 2017;23:2684-2691.
Not in our library10.12659/msm.901995
167.
Tian Y., Zhang Y., Zhang R., Qiao S., Fan J. Resolvin D2 recovers neural injury by suppressing inflammatory mediators expression in lipopolysaccharide-induced Parkinson’s disease rat model. Biochem. Biophys. Res. Commun. 2015;460:799-805.
Not in our library10.1016/j.bbrc.2015.03.109
168.
Traina G. The neurobiology of acetyl-l-carnitine. Front. Biosci. 2016;21:1314-1329.
Not in our library10.2741/4459
169.
Decreased long-chain acylcarnitines from insufficient β-oxidation as potential early diagnostic markers for Parkinson’s disease · 2017
No notice
170.
Crooks S.A., Bech S., Halling J., Christiansen D.H., Ritz B., Petersen M.S. Carnitine levels and mutations in the SLC22A5 gene in Faroes patients with Parkinson’s disease. Neurosci. Lett. 2018;675:116-119.
Not in our library10.1016/j.neulet.2018.03.064
171.
Jiménez-Jiménez F.J., Rubio J.C., Molina J.A., Martín M.A., Campos Y., Benito-León J., Ortí-Pareja M., Gassalla T., Arenas J. Cerebrospinal fluid carnitine levels in patients with Parkinson’s disease. J. Neurol. Sci. 1997;145:183-185.
Not in our library10.1016/s0022-510x(96)00259-6
172.
Zhang H., Jia H., Liu J., Ao N., Yan B., Shen W., Wang X., Li X., Luo C., Liu J. Combined R-alpha-lipoic acid and acetyl-l-carnitine exerts efficient preventative effects in a cellular model of Parkinson’s disease. J. Cell. Mol. Med. 2010;14:215-225.
Not in our library10.1111/j.1582-4934.2008.00390.x
173.
Wang C., Sadovova N., Ali H.K., Duhart H.M., Fu X., Zou X., Patterson T.A., Ninienda Z.K., Virmani A., Paule M.G., et al. L-carnitine protects neurons from 1-methyl-4-phenylpyridinium-induced neuronal apoptosis in rat forebrain culture. Neuroscience. 2007;144:46-55.
Not in our library10.1016/j.neuroscience.2006.08.083
174.
Gill E.L., Raman S., Yost R.A., Garrett T.J., Vedam-Mai V. l-Carnitine Inhibits Lipopolysaccharide-Induced Nitric Oxide Production of SIM-A9 Microglia Cells. ACS Chem. Neurosci. 2018;9:901-905.
Not in our library10.1021/acschemneuro.7b00468
175.
Singh S., Mishra A., Mishra S.K., Shukla S. ALCAR promote adult hippocampal neurogenesis by regulating cell-survival and cell death-related signals in rat model of Parkinson’s disease like-phenotypes. Neurochem. Int. 2017;108:388-396.
Not in our library10.1016/j.neuint.2017.05.017
176.
Afshin-Majd S., Bashiri K., Kiasalari Z., Baluchnejadmojarad T., Sedaghat R., Roghani M. Acetyl-l-carnitine protects dopaminergic nigrostriatal pathway in 6-hydroxydopamine-induced model of Parkinson’s disease in the rat. Biomed. Pharmacother. 2017;89:1-9.
Not in our library10.1016/j.biopha.2017.02.007
177.
Singh S., Mishra A., Srivastava N., Shukla R., Shukla S. Acetyl-l-Carnitine via Upegulating Dopamine D1 Receptor and Attenuating Microglial Activation Prevents Neuronal Loss and Improves Memory Functions in Parkinsonian Rats. Mol. Neurobiol. 2018;55:583-602.
Not in our library10.1007/s12035-016-0293-5
178.
Sarkar S., Gough B., Raymick J., Beaudoin M.A., Ali S.F., Virmani A., Binienda Z.K. Histopathological and electrophysiological indices of rotenone-evoked dopaminergic toxicity: Neuroprotective effects of acetyl-l-carnitine. Neurosci. Lett. 2015;606:53-59.
Not in our library10.1016/j.neulet.2015.08.044
179.
Zaitone S.A., Abo-Elmatty D.M., Shaalan A.A. Acetyl-l-carnitine and α-lipoic acid affect rotenone-induced damage in nigral dopaminergic neurons of rat brain, implication for Parkinson’s disease therapy. Pharmacol. Biochem. Behav. 2012;100:347-360.
Not in our library10.1016/j.pbb.2011.09.002
180.
Bodis-Wollner I., Chung E., Ghilardi M.F., Glover A., Onofrj M., Pasik P., Samson Y. Acetyl-levo-carnitine protects against MPTP-induced parkinsonism in primates. J. Neural Transm. Park Dis. Dement. Sect. 1991;3:63-72.
Not in our library10.1007/bf02251137
181.
Vetel S., Sérrière S., Vercouillie J., Vergote J., Chicheri G., Deloye J.B., Dollé F., Bodard S., Tronel C., Nadal-Desbarats L., et al. Extensive exploration of a novel rat model of Parkinson’s disease using partial 6-hydroxydopamine lesion of dopaminergic neurons suggests new therapeutic approaches. Synapse. 2018.
Not in our library10.1002/syn.22077
182.
Li X., Zhang S., Lu F., Liu C., Wang Y., Bai Y., Wang N., Liu S.M. Cerebral metabonomics study on Parkinson’s disease mice treated with extract of Acanthopanax senticosus harms. Phytomedicine. 2013;20:1219-1229.
Not in our library10.1016/j.phymed.2013.06.002
183.
Tu-Sekine B., Goldschmidt H., Raben D.M. Diacylglycerol, phosphatidic acid, and their metabolic enzymes in synaptic vesicle recycling. Adv. Biol. Regul. 2015;57:147-152.
Not in our library10.1016/j.jbior.2014.09.010
184.
Almena M., Mérida I. Shaping up the membrane: Diacylglycerol coordinates spatial orientation of signaling. Trends Biochem. Sci. 2011;36:593-603.
Not in our library10.1016/j.tibs.2011.06.005
185.
Ahmadian M., Duncan R.E., Jaworski K., Sarkadi-Nagy E., Sul H.S. Triacylglycerol metabolism in adipose tissue. Future Lipidol. 2007;2:229-237.
Not in our library10.2217/17460875.2.2.229
186.
Navarrete F., García-Gutiérrez M.S., Aracil-Fernández A., Lanciego J.L., Manzanares J. Cannabinoid CB1 and CB2 Receptors, and Monoacylglycerol Lipase Gene Expression Alterations in the Basal Ganglia of Patients with Parkinson’s Disease. Neurotherapeutics. 2018;15:459-469.
Not in our library10.1007/s13311-018-0603-x
187.
Fearnley J.M., Lees A.J. Ageing and Parkinson’s disease: Substantia nigra regional selectivity. Brain. 1991;114:2283-2301.
Not in our library10.1093/brain/114.5.2283
188.
Kish S.J., Shannak K., Hornykiewicz O. Uneven pattern of dopamine loss in the striatum of patients with idiopathic Parkinson’s disease. Pathophysiologic and clinical implications. N. Engl. J. Med. 1988;318:876-880.
Not in our library10.1056/nejm198804073181402
189.
Aymerich M.S., Rojo-Bustamante E., Molina C., Celorrio M., Sánchez-Arias J.A., Franco R. Neuroprotective Effect of JZL184 in MPP(+)-Treated SH-SY5Y Cells Through CB2 Receptors. Mol. Neurobiol. 2016;53:2312-2319.
Not in our library10.1007/s12035-015-9213-3
190.
Pasquarelli N., Porazik C., Bayer H., Buck E., Schildknecht S., Weydt P., Witting A., Ferger B. Contrasting effects of selective MAGL and FAAH inhibition on dopamine depletion and GDNF expression in a chronic MPTP mouse model of Parkinson’s disease. Neurochem. Int. 2017;110:14-24.
Not in our library10.1016/j.neuint.2017.08.003
191.
Fernández-Suárez D., Celorrio M., Riezu-Boj J.I., Ugarte A., Pacheco R., González H., Oyarzabal J., Hillard C.J., Franco R., Aymerich M.S. Monoacylglycerol lipase inhibitor JZL184 is neuroprotective and alters glial cell phenotype in the chronic MPTP mouse model. Neurobiol. Aging. 2014;35:2603-2616.
Not in our library10.1016/j.neurobiolaging.2014.05.021
192.
Stampanoni Bassi M., Sancesario A., Morace R., Centonze D., Iezzi E. Cannabinoids in Parkinson’s Disease. Cannabis Cannabinoid Res. 2017;2:21-29.
Not in our library10.1089/can.2017.0002
193.
Pisani A., Fezza F., Galati S., Battista N., Napolitano S., Finazzi-Agrò A., Bernardi G., Bursa L., Pierantozzi M., Stanzione P., et al. High endogenous cannabinoid levels in the cerebrospinal fluid of untreated Parkinson’s disease patients. Ann. Neurol. 2005;57:777-779.
Not in our library10.1002/ana.20462
194.
Pisani V., Moschella V., Bari M., Fezza F., Galati S., Bernardi G., Stacione P., Pisani A., Maccarrone M. Dynamic changes of anandamide in the cerebrospinal fluid of Parkinson’s disease patients. Mov. Disord. 2010;25:920-924.
Not in our library10.1002/mds.23014
195.
Chagas M.H.N., Zuardi A.W., Tumas V., Pena-Pereira M.A., Sobreira E.T., Bergamaschi M.M., dos Santos A.C., Teixeira A.L., Hallack J.E., Crippa J.A. Effects of cannabidiol in the treatment of patients with Parkinson’s disease: An exploratory double-blind trial. J. Psychopharmacol. 2014;28:1088-1098.
Not in our library10.1177/0269881114550355
196.
Oki M., Kaneko S., Morise S., Takenouchi N., Hashizume T., Tsuge A., Nakamura M., Wate R., Kausaka H. Zonisamide ameliorates levodopa-induced dyskinesia and reduces expression of striatal genes in Parkinson model rats. Neurosci. Res. 2017;122:45-50.
Not in our library10.1016/j.neures.2017.04.003
197.
Mackovski N., Liao J., Weng R., Wei X., Wang R., Chen Z., Liu X., Yu Y., Meyer B.J., Xia Y., et al. Reversal effect of simvastatin on the decrease in cannabinoid receptor 1 density in 6-hydroxydopamine lesioned rat brains. Life Sci. 2016;155:123-132.
Not in our library10.1016/j.lfs.2016.05.005
198.
Casteels C., Lauwers E., Baitar A., Bormans G., Baekelandt V., Van Laere K. In vivo type 1 cannabinoid receptor mapping in the 6-hydroxydopamine lesion rat model of Parkinson’s disease. Brain Res. 2010;1316:153-162.
Not in our library10.1016/j.brainres.2009.12.026
199.
Walsh S., Mnich K., Mackie K., Gorman A.M., Finn D.P., Dowd E. Loss of cannabinoid CB1 receptor expression in the 6-hydroxydopamine-induced nigrostriatal terminal lesion model of Parkinson’s disease in the rat. Brain Res. Bull. 2010;81:543-548.
Not in our library10.1016/j.brainresbull.2010.01.009
200.
Chaves-Kirsten G.P., Mazucanti C.H.Y., Real C.C., Souza B.M., Britto L.R.G., Torrão A.S. Temporal changes of CB1 cannabinoid receptor in the basal ganglia as a possible structure-specific plasticity process in 6-OHDA lesioned rats. PLoS ONE. 2013;8:e76874.
Not in our library10.1371/journal.pone.0076874
201.
Silverdale M.A., McGuire S., McInnes A., Crossman A.R., Brotchie J.M. Striatal cannabinoid CB1 receptor mRNA expression is decreased in the reserpine-treated rat model of Parkinson’s disease. Exp. Neurol. 2001;169:400-406.
Not in our library10.1006/exnr.2001.7649
202.
González S., Mena M.A., Lastres-Becker I., Serrano A., de Yébenes J.G., Ramos J.A., Fernández-Ruiz J. Cannabinoid CB(1) receptors in the basal ganglia and motor response to activation or blockade of these receptors in parkin-null mice. Brain Res. 2005;1046:195-206.
Not in our library10.1016/j.brainres.2005.04.010
203.
Madeo G., Schirinzi T., Maltese M., Martella G., Rapino C., Fezza F., Mastrengelo N., Bonsi P., Maccarrone M., Pisani A. Dopamine-dependent CB1 receptor dysfunction at corticostriatal synapses in homozygous PINK1 knockout mice. Neuropharmacology. 2016;101:460-470.
Not in our library10.1016/j.neuropharm.2015.10.021
204.
Concannon R.M., Okine B.N., Finn D.P., Dowd E. Upregulation of the cannabinoid CB2 receptor in environmental and viral inflammation-driven rat models of Parkinson’s disease. Exp. Neurol. 2016;283:204-212.
Not in our library10.1016/j.expneurol.2016.06.014
205.
Concannon R.M., Okine B.N., Finn D.P., Dowd E. Differential upregulation of the cannabinoid CB2 receptor in neurotoxic and inflammation-driven rat models of Parkinson’s disease. Exp. Neurol. 2015;269:133-141.
Not in our library10.1016/j.expneurol.2015.04.007
206.
Palomo-Garo C., Gómez-Gálvez Y., García C., Fernández-Ruiz J. Targeting the cannabinoid CB2 receptor to attenuate the progression of motor deficits in LRRK2-transgenic mice. Pharmacol. Res. 2016;110:181-192.
Not in our library10.1016/j.phrs.2016.04.004
207.
Cannabinoid Type 2 (CB2) Receptors Activation Protects against Oxidative Stress and Neuroinflammation Associated Dopaminergic Neurodegeneration in Rotenone Model of Parkinson's Disease · 2016
No notice
208.
García-Arencibia M., González S., de Lago E., Ramos J.A., Mechoulam R., Fernández-Ruiz J. Evaluation of the neuroprotective effect of cannabinoids in a rat model of Parkinson’s disease: Importance of antioxidant and cannabinoid receptor-independent properties. Brain Res. 2007;1134:162-170.
Not in our library10.1016/j.brainres.2006.11.063
209.
Fernandez-Espejo E., Caraballo I., Rodriguez de Fonseca F., Ferrer B., El Banoua F., Flores J.A., Galan-Rodriguez B. Experimental parkinsonism alters anandamide precursor synthesis, and functional deficits are improved by AM404: A modulator of endocannabinoid function. Neuropsychopharmacology. 2004;29:1134-1142.
Not in our library10.1038/sj.npp.1300407
210.
Maccarrone M., Gubellini P., Bari M., Picconi B., Battista N., Centonze D., Bernardi G., Finazzi-Agrò A., Calabresi P. Levodopa treatment reverses endocannabinoid system abnormalities in experimental parkinsonism. J. Neurochem. 2003;85:1018-1025.
Not in our library10.1046/j.1471-4159.2003.01759.x
211.
Gubellini P., Picconi B., Bari M., Battista N., Calabresi P., Centonze D., Bernardi G., Finazzi-Agrò A., Maccarrone M. Experimental parkinsonism alters endocannabinoid degradation: Implications for striatal glutamatergic transmission. J. Neurosci. 2002;22:6900-6907.
Not in our library10.1523/jneurosci.22-16-06900.2002
212.
Ferrer B., Asbrock N., Kathuria S., Piomelli D., Giuffrida A. Effects of levodopa on endocannabinoid levels in rat basal ganglia: Implications for the treatment of levodopa-induced dyskinesias. Eur. J. Neurosci. 2003;18:1607-1614.
Not in our library10.1046/j.1460-9568.2003.02896.x
213.
Van der Stelt M., Fox S.H., Hill M., Crossman A.R., Petrosino S., Di Marzo V., Brotchie J.M. A role for endocannabinoids in the generation of parkinsonism and levodopa-induced dyskinesia in MPTP-lesioned non-human primate models of Parkinson’s disease. FASEB J. 2005;19:1140-1142.
Not in our library10.1096/fj.04-3010fje
214.
Viveros-Paredes J.M., Gonzalez-Castañeda R.E., Escalante-Castañeda A., Tejeda-Martínez A.R., Castañeda-Achutiguí F., Flores-Soto M.E. Effect of inhibition of fatty acid amide hydrolase on MPTP-induced dopaminergic neuronal damage. Neurologia. 2017.
Not in our library10.1016/j.nrleng.2018.10.015
215.
Celorrio M., Fernández-Suárez D., Rojo-Bustamante E., Echeverry-Alzate V., Ramírez M.J., Hillard C.J., López-Morenoa J.A., Maldonado R., Oyarzábal J., Franco R., et al. Fatty acid amide hydrolase inhibition for the symptomatic relief of Parkinson’s disease. Brain Behav. Immun. 2016;57:94-105.
Not in our library10.1016/j.bbi.2016.06.010
216.
Mnich K., Finn D.P., Dowd E., Gorman A.M. Inhibition by anandamide of 6-hydroxydopamine-induced cell death in PC12 cells. Int. J. Cell Biol. 2010;2010:818497.
Not in our library10.1155/2010/818497
217.
Mounsey R.B., Mustafa S., Robinson L., Ross R.A., Riedel G., Pertwee R.G., Tesimann P. Increasing levels of the endocannabinoid 2-AG is neuroprotective in the 1-methyl-4-phenyl-1, 2, 3, 6-tetrahydropyridine mouse model of Parkinson’s disease. Exp. Neurol. 2015;273:36-44.
Not in our library10.1016/j.expneurol.2015.07.024
218.
Lack of neuroprotection in the absence of P2X7 receptors in toxin-induced animal models of Parkinson's disease · 2011
Not checked
219.
Di Marzo V., Hill M.P., Bisogno T., Crossman A.R., Brotchie J.M. Enhanced levels of endogenous cannabinoids in the globus pallidus are associated with a reduction in movement in an animal model of Parkinson’s disease. FASEB J. 2000;14:1432-1438.
Not in our library10.1096/fj.14.10.1432
220.
Freestone P.S., Guatteo E., Piscitelli F., di Marzo V., Lipski J., Mercuri N.B. Glutamate spillover drives endocannabinoid production and inhibits GABAergic transmission in the Substantia Nigra pars compacta. Neuropharmacology. 2014;79:467-475.
Not in our library10.1016/j.neuropharm.2013.12.007
221.
Kreitzer A.C., Malenka R.C. Endocannabinoid-mediated rescue of striatal LTD and motor deficits in Parkinson’s disease models. Nature. 2007;445:643-647.
Not in our library10.1038/nature05506
222.
Zhang J., Zhang X., Wang L., Yang C. High Performance Liquid Chromatography-Mass Spectrometry (LC-MS) Based Quantitative Lipidomics Study of Ganglioside-NANA-3 Plasma to Establish Its Association with Parkinson’s Disease Patients. Med. Sci. Monit. 2017;23:5345-5353.
Not in our library10.12659/msm.904399
223.
Chan R.B., Perotte A.J., Zhou B., Liong C., Shorr E.J., Marder K.S., et al. Elevated GM3 plasma concentration in idiopathic Parkinson’s disease: A lipidomic analysis. PLoS ONE. 2017;12:e0172348.
Not in our library10.1371/journal.pone.0172348
224.
Wood P.L., Tippireddy S., Feriante J., Woltjer R.L. Augmented frontal cortex diacylglycerol levels in Parkinson’s disease and Lewy Body Disease. PLoS ONE. 2018;13:e0191815.
Not in our library10.1371/journal.pone.0191815
225.
Lipid Pathway Alterations in Parkinson's Disease Primary Visual Cortex · 2011
No notice
226.
Simón-Sánchez J., van Hilten J.J., van de Warrenburg B., Post B., Berendse H.W., Arepalli S., Hernandez D.G., de Bie R.M., Velseboar D., Scheffer H., et al. Genome-wide association study confirms extant PD risk loci among the Dutch. Eur. J. Hum. Genet. 2011;19:655-661.
Not in our library10.1038/ejhg.2010.254
227.
Chen Y.P., Song W., Huang R., Chen K., Zhao B., Li J., Yang Y., Shang H.F. GAK rs1564282 and DGKQ rs11248060 increase the risk for Parkinson’s disease in a Chinese population. J. Clin. Neurosci. 2013;20:880-883.
Not in our library10.1016/j.jocn.2012.07.011
228.
Sakane F., Mizuno S., Takahashi D., Sakai H. Where do substrates of diacylglycerol kinases come from? Diacylglycerol kinases utilize diacylglycerol species supplied from phosphatidylinositol turnover-independent pathways. Adv. Biol. Regul. 2018;67:101-108.
Not in our library10.1016/j.jbior.2017.09.003
229.
Guo X., Song W., Chen K., Chen X., Zheng Z., Cao B., Huang R., Zhao B., Wu Y., Shang H.F. The serum lipid profile of Parkinson’s disease patients: A study from China. Int. J. Neurosci. 2015;125:838-844.
Not in our library10.3109/00207454.2014.979288
230.
Wei Q., Wang H., Tian Y., Xu F., Chen X., Wang K. Reduced serum levels of triglyceride, very low density lipoprotein cholesterol and apolipoprotein B in Parkinson’s disease patients. PLoS ONE. 2013;8:e75743.
Not in our library10.1371/journal.pone.0075743
231.
Gregório M.L., Pinhel M.A.S., Sado C.L., Longo G.S., Oliveira F.N., Amorim G.S., Nakazone M.A., Florim G.M., Mazeti C.M., Martins D.P., et al. Impact of genetic variants of apolipoprotein E on lipid profile in patients with Parkinson’s disease. Biomed. Res. Int. 2013;2013:641515.
Not in our library10.1155/2013/641515
232.
Cereda E., Cassani E., Barichella M., Spadafranca A., Caccialanza R., Bertoli S., Battezzati A., Pezzoli G. Low cardiometabolic risk in Parkinson’s disease is independent of nutritional status, body composition and fat distribution. Clin. Nutr. 2012;31:699-704.
Not in our library10.1016/j.clnu.2012.02.004
233.
Sääksjärvi K., Knekt P., Männistö S., Lyytinen J., Heliövaara M. Prospective study on the components of metabolic syndrome and the incidence of Parkinson’s disease. Park. Relat. Disord. 2015;21:1148-1155.
Not in our library10.1016/j.parkreldis.2015.07.017
234.
Vikdahl M., Bäckman L., Johansson I., Forsgren L., Håglin L. Cardiovascular risk factors and the risk of Parkinson’s disease. Eur. J. Clin. Nutr. 2015;69:729-733.
Not in our library10.1038/ejcn.2014.259
235.
Scigliano G., Musicco M., Soliveri P., Piccolo I., Ronchetti G., Girotti F. Reduced risk factors for vascular disorders in Parkinson disease patients: A case-control study. Stroke. 2006;37:1184-1188.
Not in our library10.1161/01.str.0000217384.03237.9c
236.
Fukui Y., Hishikawa N., Shang J., Sato K., Nakano Y., Morihara R., Ohta Y., Yamashita T., Abe K. Peripheral arterial endothelial dysfunction of neurodegenerative diseases. J. Neurol. Sci. 2016;366:94-99.
Not in our library10.1016/j.jns.2016.04.042
237.
Ya L., Lu Z. Differences in ABCA1 R219K Polymorphisms and Serum Indexes in Alzheimer and Parkinson Diseases in Northern China. Med. Sci. Monit. 2017;23:4591-4600.
Not in our library10.12659/msm.903636
238.
Oxidative Stress in Parkinson's Disease: A Systematic Review and Meta-Analysis · 2018
No notice
239.
Guerreiro P.S., Coelho J.E., Sousa-Lima I., Macedo P., Lopes L.V., Outeiro T.F., Pais T.F. Mutant A53T α-Synuclein Improves Rotarod Performance Before Motor Deficits and Affects Metabolic Pathways. Neuromol. Med. 2017;19:113-121.
Not in our library10.1007/s12017-016-8435-5
240.
Meng X., Zheng R., Zhang Y., Qiao M., Liu L., Jing P., Wang L., Liu J., Gao Y. An activated sympathetic nervous system affects white adipocyte differentiation and lipolysis in a rat model of Parkinson’s disease. J. Neurosci. Res. 2015;93:350-360.
Not in our library10.1002/jnr.23488
241.
He Q., Wang M., Petucci C., Gardell S.J., Han X. Rotenone induces reductive stress and triacylglycerol deposition in C2C12 cells. Int. J. Biochem. Cell Biol. 2013;45:2749-2755.
Not in our library10.1016/j.biocel.2013.09.011
242.
Sere Y.Y., Regnacq M., Colas J., Berges T. A Saccharomyces cerevisiae strain unable to store neutral lipids is tolerant to oxidative stress induced by α-synuclein. Free Radic. Biol. Med. 2010;49:1755-1764.
Not in our library10.1016/j.freeradbiomed.2010.09.007
243.
Cole N.B., Murphy D.D., Grider T., Rueter S., Brasaemle D., Nussbaum R.L. Lipid droplet binding and oligomerization properties of the Parkinson’s disease protein alpha-synuclein. J. Biol. Chem. 2002;277:6344-6352.
Not in our library10.1074/jbc.m108414200
244.
Sánchez Campos S., Alza N.P., Salvador G.A. Lipid metabolism alterations in the neuronal response to A53T α-synuclein and Fe-induced injury. Arch. Biochem. Biophys. 2018;655:43-54.
Not in our library10.1016/j.abb.2018.08.007
245.
Antonny B., Vanni S., Shindou H., Ferreira T. From zero to six double bonds: Phospholipid unsaturation and organelle function. Trends Cell Biol. 2015;25:427-436.
Not in our library10.1016/j.tcb.2015.03.004
246.
Bohdanowicz M., Grinstein S. Role of phospholipids in endocytosis, phagocytosis, and macropinocytosis. Physiol. Rev. 2013;93:69-106.
Not in our library10.1152/physrev.00002.2012
247.
Zhang Q., Tamura Y., Roy M., Adachi Y., Iijima M., Sesaki H. Biosynthesis and roles of phospholipids in mitochondrial fusion, division and mitophagy. Cell. Mol. Life Sci. 2014;71:3767-3778.
Not in our library10.1007/s00018-014-1648-6
248.
Boss W.F., Im Y.J. Phosphoinositide signaling. Annu. Rev. Plant Biol. 2012;63:409-429.
Not in our library10.1146/annurev-arplant-042110-103840
249.
Yung Y.C., Stoddard N.C., Mirendil H., Chun J. Lysophosphatidic Acid signaling in the nervous system. Neuron. 2015;85:669-682.
Not in our library10.1016/j.neuron.2015.01.009
250.
Kay J.G., Grinstein S. Phosphatidylserine-mediated cellular signaling. Adv. Exp. Med. Biol. 2013;991:177-193.
Not in our library10.1007/978-94-007-6331-9_10
251.
Musille P.M., Kohn J.A., Ortlund E.A. Phospholipid—Driven gene regulation. FEBS Lett. 2013;587:1238-1246.
Not in our library10.1016/j.febslet.2013.01.004
252.
Liu Y., Su Y., Wang X. Phosphatidic acid-mediated signaling. Adv. Exp. Med. Biol. 2013;991:159-176.
Not in our library10.1007/978-94-007-6331-9_9
253.
Ammar M.R., Kassas N., Bader M.F., Vitale N. Phosphatidic acid in neuronal development: A node for membrane and cytoskeleton rearrangements. Biochimie. 2014;107:51-57.
Not in our library10.1016/j.biochi.2014.07.026
254.
Yang C.Y., Frohman M.A. Mitochondria: Signaling with phosphatidic acid. Int. J. Biochem. Cell Biol. 2012;44:1346-1350.
Not in our library10.1016/j.biocel.2012.05.006
255.
Jiang Z., Hess S.K., Heinrich F., Lee J.C. Molecular details of α-synuclein membrane association revealed by neutrons and photons. J. Phys. Chem. B. 2015;119:4812-4823.
Not in our library10.1021/jp512499r
256.
Perrin R.J., Woods W.S., Clayton D.F., George J.M. Interaction of human alpha-Synuclein and Parkinson’s disease variants with phospholipids. Structural analysis using site-directed mutagenesis. J. Biol. Chem. 2000;275:34393-34398.
Not in our library10.1074/jbc.m004851200
257.
Mizuno S., Sasai H., Kume A., Takahashi D., Satoh M., Kado S., Sakane F. Dioleoyl-phosphatidic acid selectively binds to α-synuclein and strongly induces its aggregation. FEBS Lett. 2017;591:784-791.
Not in our library10.1002/1873-3468.12592
258.
Soper J.H., Kehm V., Burd C.G., Bankaitis V.A., Lee V.M.Y. Aggregation of α-synuclein in S. cerevisiae is associated with defects in endosomal trafficking and phospholipid biosynthesis. J. Mol. Neurosci. 2011;43:391-405.
Not in our library10.1007/s12031-010-9455-5
259.
Holemans T., Sørensen D.M., van Veen S., Martin S., Hermans D., Kemmer G.C., Van den Haute C., Baekelandt V., Günther Pomorski T., Agostinis P., et al. A lipid switch unlocks Parkinson’s disease-associated ATP13A2. Proc. Natl. Acad. Sci. USA. 2015;112:9040-9045.
Not in our library10.1073/pnas.1508220112
260.
Martin S., van Veen S., Holemans T., Demirsoy S., van den Haute C., Baekelandt V., Agostinis P., Eggermont J., Vangheluwe P. Protection against Mitochondrial and Metal Toxicity Depends on Functional Lipid Binding Sites in ATP13A2. Park. Dis. 2016;2016:9531917.
Not in our library10.1155/2016/9531917
261.
Mendez-Gomez H.R., Singh J., Meyers C., Chen W., Gorbatyuk O.S., Muzyczka N. The Lipase Activity of Phospholipase D2 is Responsible for Nigral Neurodegeneration in a Rat Model of Parkinson’s Disease. Neuroscience. 2018;377:174-183.
Not in our library10.1016/j.neuroscience.2018.02.047
262.
Binder B.Y.K., Williams P.A., Silva E.A., Leach J.K. Lysophosphatidic Acid and Sphingosine-1-Phosphate: A Concise Review of Biological Function and Applications for Tissue Engineering. Tissue Eng. Part B Rev. 2015;21:531-542.
Not in our library10.1089/ten.teb.2015.0107
263.
Sheng X., Yung Y.C., Chen A., Chun J. Lysophosphatidic acid signalling in development. Development. 2015;142:1390-1395.
Not in our library10.1242/dev.121723
264.
Aikawa S., Hashimoto T., Kano K., Aoki J. Lysophosphatidic acid as a lipid mediator with multiple biological actions. J. Biochem. 2015;157:81-89.
Not in our library10.1093/jb/mvu077
265.
Yang X.Y., Zhao E.Y., Zhuang W.X., Sun F.X., Han H.L., Han H.R., Lin Z.J., Pan Z.F., Qu M.H., Zeng X.W., et al. LPA signaling is required for dopaminergic neuron development and is reduced through low expression of the LPA1 receptor in a 6-OHDA lesion model of Parkinson’s disease. Neurol. Sci. 2015;36:2027-2033.
Not in our library10.1007/s10072-015-2295-x
266.
Choi J.H., Jang M., Oh S., Nah S.Y., Cho I.H. Multi-Target Protective Effects of Gintonin in 1-Methyl-4-phenyl-1, 2, 3, 6-tetrahydropyridine-Mediated Model of Parkinson’s Disease via Lysophosphatidic Acid Receptors. Front. Pharmacol. 2018;9:515.
Not in our library10.3389/fphar.2018.00515
267.
Vance J.E. Phosphatidylserine and phosphatidylethanolamine in mammalian cells: Two metabolically related aminophospholipids. J. Lipid Res. 2008;49:1377-1387.
Not in our library10.1194/jlr.r700020-jlr200
268.
Guedes L.C., Chan R.B., Gomes M.A., Conceição V.A., Machado R.B., Soares T., Xu Y., Gaspar P., Carriço J.A., Alacaly R.N., et al. Serum lipid alterations in GBA-associated Parkinson’s disease. Park. Relat. Disord. 2017;44:58-65.
Not in our library10.1016/j.parkreldis.2017.08.026
269.
Riekkinen P., Rinne U.K., Pelliniemi T.T., Sonninen V. Interaction between dopamine and phospholipids. Studies of the substantia nigra in Parkinson disease patients. Arch. Neurol. 1975;32:25-27.
Not in our library10.1001/archneur.1975.00490430047006
270.
Seyfried T.N., Choi H., Chevalier A., Hogan D., Akgoc Z., Schneider J.S. Sex-Related Abnormalities in Substantia Nigra Lipids in Parkinson’s Disease. ASN Neuro. 2018;10.
Not in our library10.1177/1759091418781889
271.
Ross B.M., Mamalias N., Moszczynska A., Rajput A.H., Kish S.J. Elevated activity of phospholipid biosynthetic enzymes in substantia nigra of patients with Parkinson’s disease. Neuroscience. 2001;102:899-904.
Not in our library10.1016/s0306-4522(00)00501-7
272.
Jo E., McLaurin J., Yip C.M., St George-Hyslop P., Fraser P.E. alpha-Synuclein membrane interactions and lipid specificity. J. Biol. Chem. 2000;275:34328-34334.
Not in our library10.1074/jbc.m004345200
273.
Zakharov S.D., Hulleman J.D., Dutseva E.A., Antonenko Y.N., Rochet J.C., Cramer W.A. Helical alpha-synuclein forms highly conductive ion channels. Biochemistry. 2007;46:14369-14379.
Not in our library10.1021/bi701275p
274.
Wang S., Zhang S., Liou L.C., Ren Q., Zhang Z., Caldwell G.A., Witt S.N. Phosphatidylethanolamine deficiency disrupts α-synuclein homeostasis in yeast and worm models of Parkinson disease. Proc. Natl. Acad. Sci. USA. 2014;111:E3976-E3985.
Not in our library10.1073/pnas.1411694111
275.
Wang S., Zhang S., Xu C., Barron A., Galiano F., Patel D., Lee Y.J., Caldwell G.A., Caldwell K.A., Witt S.N. Chemical Compensation of Mitochondrial Phospholipid Depletion in Yeast and Animal Models of Parkinson’s Disease. PLoS ONE. 2016;11:e0164465.
Not in our library10.1371/journal.pone.0164465
276.
Lee E.S., Charlton C.G. 1-Methyl-4-phenyl-pyridinium increases S-adenosyl-L-methionine dependent phospholipid methylation. Pharmacol. Biochem. Behav. 2001;70:105-114.
Not in our library10.1016/s0091-3057(01)00588-3
277.
Lee E.S.Y., Chen H., Charlton C.G., Soliman K.F.A. The role of phospholipid methylation in 1-methyl-4-phenyl-pyridinium ion (MPP+)-induced neurotoxicity in PC12 cells. Neurotoxicology. 2005;26:945-957.
Not in our library10.1016/j.neuro.2005.04.005
278.
Leventis P.A., Grinstein S. The distribution and function of phosphatidylserine in cellular membranes. Annu. Rev. Biophys. 2010;39:407-427.
Not in our library10.1146/annurev.biophys.093008.131234
279.
Kim H.Y., Huang B.X., Spector A.A. Phosphatidylserine in the brain: Metabolism and function. Prog. Lipid Res. 2014;56:1-18.
Not in our library10.1016/j.plipres.2014.06.002
280.
Lobasso S., Tanzarella P., Vergara D., Maffia M., Cocco T., Corcelli A. Lipid profiling of parkin-mutant human skin fibroblasts. J. Cell. Physiol. 2017;232:3540-3551.
Not in our library10.1002/jcp.25815
281.
Valadas J.S., Esposito G., Vandekerkhove D., Miskiewicz K., Deaulmerie L., Raitano S., Seibler P., Lein C., Verstreken P. ER Lipid Defects in Neuropeptidergic Neurons Impair Sleep Patterns in Parkinson’s Disease. Neuron. 2018;98:1155-1169.e6.
Not in our library10.1016/j.neuron.2018.05.022
282.
Wei L., Sun C., Lei M., Li G., Yi L., Luo F., Li Y., Ding L., Liu Z., Li S., et al. Activation of Wnt/β-catenin pathway by exogenous Wnt1 protects SH-SY5Y cells against 6-hydroxydopamine toxicity. J. Mol. Neurosci. 2013;49:105-115.
Not in our library10.1007/s12031-012-9900-8
283.
Lupescu A., Jilani K., Zbidah M., Lang F. Induction of apoptotic erythrocyte death by rotenone. Toxicology. 2012;300:132-137.
Not in our library10.1016/j.tox.2012.06.007
284.
González-Polo R.A., Niso-Santano M., Ortíz-Ortíz M.A., Gómez-Martín A., Morán J.M., García-Rubio L., Francisco-Mocillo J., Zaragoza C., Soler G., Fuentes J.M. Inhibition of paraquat-induced autophagy accelerates the apoptotic cell death in neuroblastoma SH-SY5Y cells. Toxicol. Sci. 2007;97:448-458.
Not in our library10.1093/toxsci/kfm040
285.
Ye S., Koon H.K., Fan W., Xu Y., Wei W., Xu C., Cai J. Effect of a Traditional Chinese Herbal Medicine Formulation on Cell Survival and Apoptosis of MPP+-Treated MES 23.5 Dopaminergic Cells. Park. Dis. 2017;2017:4764212.
Not in our library10.1155/2017/4764212
286.
Flower T.R., Chesnokova L.S., Froelich C.A., Dixon C., Witt S.N. Heat shock prevents alpha-synuclein-induced apoptosis in a yeast model of Parkinson’s disease. J. Mol. Biol. 2005;351:1081-1100.
Not in our library10.1016/j.jmb.2005.06.060
287.
Emmrich J.V., Hornik T.C., Neher J.J., Brown G.C. Rotenone induces neuronal death by microglial phagocytosis of neurons. FEBS J. 2013;280:5030-5038.
Not in our library10.1111/febs.12401
288.
Almandoz-Gil L., Lindström V., Sigvardson J., Kahle P.J., Lannfelt L., Ingelsson M., Bergström J. Mapping of Surface-Exposed Epitopes of In Vitro and In Vivo Aggregated Species of Alpha-Synuclein. Cell. Mol. Neurobiol. 2017;37:1217-1226.
Not in our library10.1007/s10571-016-0454-0
289.
N-Alpha-Acetylation of α-Synuclein Increases Its Helical Folding Propensity, GM1 Binding Specificity and Resistance to Aggregation · 2014
No notice
290.
Araki K., Sugawara K., Hayakawa E.H., Ubukawa K., Kobayashi I., Wakui H., Takahasi N., Sawada K., Mochizuki H., Nunomura W. The localization of α-synuclein in the process of differentiation of human erythroid cells. Int. J. Hematol. 2018;108:130-138.
Not in our library10.1007/s12185-018-2457-8
291.
Hu R., Diao J., Li J., Tang Z., Li X., Leitz J., Long J., Liu J., Yu D., Zhao Q. Intrinsic and membrane-facilitated α-synuclein oligomerization revealed by label-free detection through solid-state nanopores. Sci. Rep. 2016;6:20776.
Not in our library10.1038/srep20776
292.
Lou X., Kim J., Hawk B.J., Shin Y.K. α-Synuclein may cross-bridge v-SNARE and acidic phospholipids to facilitate SNARE-dependent vesicle docking. Biochem. J. 2017;474:2039-2049.
Not in our library10.1042/bcj20170200
293.
Mejia E.M., Hatch G.M. Mitochondrial phospholipids: Role in mitochondrial function. J. Bioenerg. Biomembr. 2016;48:99-112.
Not in our library10.1007/s10863-015-9601-4
294.
Treede I., Braun A., Sparla R., Kühnel M., Giese T., Turner J.R., Anes E., Kulaksiz H., Füllekrug J., Stremmel W., et al. Anti-inflammatory effects of phosphatidylcholine. J. Biol. Chem. 2007;282:27155-27164.
Not in our library10.1074/jbc.m704408200
295.
Lagace T.A. Phosphatidylcholine: Greasing the Cholesterol Transport Machinery. Lipid Insights. 2015;8(Suppl. 1):65-73.
Not in our library10.4137/lpi.s31746
296.
Marcucci H., Paoletti L., Jackowski S., Banchio C. Phosphatidylcholine biosynthesis during neuronal differentiation and its role in cell fate determination. J. Biol. Chem. 2010;285:25382-25393.
Not in our library10.1074/jbc.m110.139477
297.
Li T., Tang W., Zhang L. Monte Carlo cross-validation analysis screens pathway cross-talk associated with Parkinson’s disease. Neurol. Sci. 2016;37:1327-1333.
Not in our library10.1007/s10072-016-2595-9
298.
Farmer K., Smith C.A., Hayley S., Smith J. Major Alterations of Phosphatidylcholine and Lysophosphotidylcholine Lipids in the Substantia Nigra Using an Early Stage Model of Parkinson’s Disease. Int. J. Mol. Sci. 2015;16:18865-18877.
Not in our library10.3390/ijms160818865
299.
Stöckl M., Fischer P., Wanker E., Herrmann A. Alpha-synuclein selectively binds to anionic phospholipids embedded in liquid-disordered domains. J. Mol. Biol. 2008;375:1394-1404.
Not in our library10.1016/j.jmb.2007.11.051
300.
Jiang Z., de Messieres M., Lee J.C. Membrane remodeling by α-synuclein and effects on amyloid formation. J. Am. Chem. Soc. 2013;135:15970-15973.
Not in our library10.1021/ja405993r
301.
Di Pasquale E., Fantini J., Chahinian H., Maresca M., Taïeb N., Yahi N. Altered ion channel formation by the Parkinson’s-disease-linked E46K mutant of alpha-synuclein is corrected by GM3 but not by GM1 gangliosides. J. Mol. Biol. 2010;397:202-218.
Not in our library10.1016/j.jmb.2010.01.046
302.
O’Leary E.I., Jiang Z., Strub M.P., Lee J.C. Effects of phosphatidylcholine membrane fluidity on the conformation and aggregation of N-terminally acetylated α-synuclein. J. Biol. Chem. 2018;293:11195-11205.
Not in our library10.1074/jbc.ra118.002780
303.
Hollie N.I., Cash J.G., Matlib M.A., Wortman M., Basford J.E., Abplanalp W., Hui D.Y. Micromolar changes in lysophosphatidylcholine concentration cause minor effects on mitochondrial permeability but major alterations in function. Biochim. Biophys. Acta. 2014;1841:888-895.
Not in our library10.1016/j.bbalip.2013.11.013
304.
Li X., Fang P., Li Y., Kuo Y.M., Andrews A.J., Nanayakkara G., Johnson C., Fu H., Shan H., Du F., et al. Mitochondrial Reactive Oxygen Species Mediate Lysophosphatidylcholine-Induced Endothelial Cell Activation. Arterioscler. Thromb. Vasc. Biol. 2016;36:1090-1100.
Not in our library10.1161/atvbaha.115.306964
305.
Hung N.D., Sok D.E., Kim M.R. Prevention of 1-palmitoyl lysophosphatidylcholine-induced inflammation by polyunsaturated acyl lysophosphatidylcholine. Inflamm. Res. 2012;61:473-483.
Not in our library10.1007/s00011-012-0434-x
306.
Lee E.S.Y., Chen H., Shepherd K.R., Lamango N.S., Soliman K.F.A., Charlton C.G. Inhibitory effects of lysophosphatidylcholine on the dopaminergic system. Neurochem. Res. 2004;29:1333-1342.
Not in our library10.1023/b:nere.0000026394.92363.ee
307.
Lee E.S.Y., Soliman K.F.A., Charlton C.G. Lysophosphatidylcholine decreases locomotor activities and dopamine turnover rate in rats. Neurotoxicology. 2005;26:27-38.
Not in our library10.1016/j.neuro.2004.07.009
308.
Pacheco M.A., Jope R.S. Phosphoinositide signaling in human brain. Prog. Neurobiol. 1996;50:255-273.
Not in our library10.1016/s0301-0082(96)00035-4
309.
Chalimoniuk M., Snoek G.T., Adamczyk A., Małecki A., Strosznajder J.B. Phosphatidylinositol transfer protein expression altered by aging and Parkinson disease. Cell. Mol. Neurobiol. 2006;26:1153-1166.
Not in our library10.1007/s10571-006-9078-0
310.
Cockcroft S. The diverse functions of phosphatidylinositol transfer proteins. Curr. Top. Microbiol. Immunol. 2012;362:185-208.
Not in our library10.1007/978-94-007-5025-8_9
311.
Lee E.N., Lee S.Y., Lee D., Kim J., Paik S.R. Lipid interaction of alpha-synuclein during the metal-catalyzed oxidation in the presence of Cu2+ and H2O2. J. Neurochem. 2003;84:1128-1142.
Not in our library10.1046/j.1471-4159.2003.01612.x
312.
Narayanan V., Guo Y., Scarlata S. Fluorescence studies suggest a role for alpha-synuclein in the phosphatidylinositol lipid signaling pathway. Biochemistry. 2005;44:462-470.
Not in our library10.1021/bi0487140
313.
Sekar S., Taghibiglou C. Elevated nuclear phosphatase and tensin homolog (PTEN) and altered insulin signaling in substantia nigral region of patients with Parkinson’s disease. Neurosci. Lett. 2018;666:139-143.
Not in our library10.1016/j.neulet.2017.12.049
314.
Demirsoy S., Martin S., Motamedi S., van Veen S., Holemans T., Van den Haute C., Jordanova A., Baekelandt V., Vangheluwe P., Agostinis P. ATP13A2/PARK9 regulates endo-/lysosomal cargo sorting and proteostasis through a novel PI(3, 5)P2-mediated scaffolding function. Hum. Mol. Genet. 2017;26:1656-1669.
Not in our library10.1093/hmg/ddx070
315.
Horvath S.E., Daum G. Lipids of mitochondria. Prog. Lipid Res. 2013;52:590-614.
Not in our library10.1016/j.plipres.2013.07.002
316.
Ramakrishnan M., Jensen P.H., Marsh D. Association of alpha-synuclein and mutants with lipid membranes: Spin-label ESR and polarized IR. Biochemistry. 2006;45:3386-3395.
Not in our library10.1021/bi052344d
317.
Jiang Z., Flynn J.D., Teague W.E., Gawrisch K., Lee J.C. Stimulation of α-synuclein amyloid formation by phosphatidylglycerol micellar tubules. Biochim. Biophys. Acta. 2018.
Not in our library10.1016/j.bbamem.2018.02.025
318.
Bédard L., Lefèvre T., Morin-Michaud É., Auger M. Besides fibrillization: Putative role of the peptide fragment 71-82 on the structural and assembly behavior of α-synuclein. Biochemistry. 2014;53:6463-6472.
Not in our library10.1021/bi5008707
319.
Pandey A.P., Haque F., Rochet J.C., Hovis J.S. Clustering of alpha-synuclein on supported lipid bilayers: Role of anionic lipid, protein, and divalent ion concentration. Biophys. J. 2009;96:540-551.
Not in our library10.1016/j.bpj.2008.10.011
320.
Stefanovic A.N.D., Claessens M.M.A.E., Blum C., Subramaniam V. Alpha-synuclein amyloid oligomers act as multivalent nanoparticles to cause hemifusion in negatively charged vesicles. Small. 2015;11:2257-2262.
Not in our library10.1002/smll.201402674
321.
Van Rooijen B.D., Claessens M.M.A.E., Subramaniam V. Lipid bilayer disruption by oligomeric alpha-synuclein depends on bilayer charge and accessibility of the hydrophobic core. Biochim. Biophys. Acta. 2009;1788:1271-1278.
Not in our library10.1016/j.bbamem.2009.03.010
322.
Membrane Permeabilization by Oligomeric α-Synuclein: In Search of the Mechanism · 2010
No notice
323.
Zhu M., Qin Z.J., Hu D., Munishkina L.A., Fink A.L. Alpha-synuclein can function as an antioxidant preventing oxidation of unsaturated lipid in vesicles. Biochemistry. 2006;45:8135-8142.
Not in our library10.1021/bi052584t
324.
Ren M., Phoon C.K.L., Schlame M. Metabolism and function of mitochondrial cardiolipin. Prog. Lipid Res. 2014;55:1-16.
Not in our library10.1016/j.plipres.2014.04.001
325.
Paradies G., Paradies V., Ruggiero F.M., Petrosillo G. Cardiolipin and mitochondrial function in health and disease. Antioxid. Redox. Signal. 2014;20:1925-1953.
Not in our library10.1089/ars.2013.5280
326.
Paradies G., Paradies V., De Benedictis V., Ruggiero F.M., Petrosillo G. Functional role of cardiolipin in mitochondrial bioenergetics. Biochim. Biophys. Acta. 2014;1837:408-417.
Not in our library10.1016/j.bbabio.2013.10.006
327.
Vos M., Geens A., Böhm C., Deaulmerie L., Swerts J., Rossi M., Craessaerts K., Leites E.P., Seibler P., Rakovic A., et al. Cardiolipin promotes electron transport between ubiquinone and complex I to rescue PINK1 deficiency. J. Cell Biol. 2017;216:695-708.
Not in our library10.1083/jcb.201511044
328.
Tyurina Y.Y., Winnica D.E., Kapralova V.I., Kapralov A.A., Tyurin V.A., Kagan V.E. LC/MS characterization of rotenone induced cardiolipin oxidation in human lymphocytes: Implications for mitochondrial dysfunction associated with Parkinson’s disease. Mol. Nutr. Food Res. 2013;57:1410-1422.
Not in our library10.1002/mnfr.201200801
329.
Tyurina Y.Y., Polimova A.M., Maciel E., Tyurin V.A., Kapralova V.I., Winnica D.E., Vikulina A.S., Domigues M.R., McCoy J., Samders L.H., et al. LC/MS analysis of cardiolipins in substantia nigra and plasma of rotenone-treated rats: Implication for mitochondrial dysfunction in Parkinson’s disease. Free Radic. Res. 2015;49:681-691.
Not in our library10.3109/10715762.2015.1005085
330.
Zigoneanu I.G., Yang Y.J., Krois A.S., Haque E., Pielak G.J. Interaction of α-synuclein with vesicles that mimic mitochondrial membranes. Biochim. Biophys. Acta. 2012;1818:512-519.
Not in our library10.1016/j.bbamem.2011.11.024
331.
Robotta M., Gerding H.R., Vogel A., Hauser K., Schildknecht S., Karreman C., Leist M., Subramaniam V., Drescher M. Alpha-synuclein binds to the inner membrane of mitochondria in an α-helical conformation. Chembiochem. 2014;15:2499-2502.
Not in our library10.1002/cbic.201402281
332.
Cardiolipin exposure on the outer mitochondrial membrane modulates α-synuclein · 2018
No notice
333.
Nakamura K., Nemani V.M., Azarbal F., Skibinski G., Levy J.M., Egami K., Munushkina L., Zhang J., Gardner B., Wakabayashi J., et al. Direct membrane association drives mitochondrial fission by the Parkinson disease-associated protein alpha-synuclein. J. Biol. Chem. 2011;286:20710-20726.
Not in our library10.1074/jbc.m110.213538
334.
Shen J., Du T., Wang X., Duan C., Gao G., Zhang J., Lu L., Yang H. α-Synuclein amino terminus regulates mitochondrial membrane permeability. Brain Res. 2014;1591:14-26.
Not in our library10.1016/j.brainres.2014.09.046
335.
Gao G., Wang Z., Lu L., Duan C., Wang X., Yang H. Morphological analysis of mitochondria for evaluating the toxicity of α-synuclein in transgenic mice and isolated preparations by atomic force microscopy. Biomed. Pharmacother. 2017;96:1380-1388.
Not in our library10.1016/j.biopha.2017.11.057
336.
Bayir H., Kapralov A.A., Jiang J., Huang Z., Tyurina Y.Y., Tyurin V.A., Zhao Q., Belikova N.A., Vlasova I.I., Maeda A., et al. Peroxidase mechanism of lipid-dependent cross-linking of synuclein with cytochrome C: Protection against apoptosis versus delayed oxidative stress in Parkinson disease. J. Biol. Chem. 2009;284:15951-15969.
Not in our library10.1074/jbc.m900418200
337.
Ghio S., Kamp F., Cauchi R., Giese A., Vassallo N. Interaction of α-synuclein with biomembranes in Parkinson’s disease—Role of cardiolipin. Prog. Lipid Res. 2016;61:73-82.
Not in our library10.1016/j.plipres.2015.10.005
338.
Chu C.T., Bayır H., Kagan V.E. LC3 binds externalized cardiolipin on injured mitochondria to signal mitophagy in neurons: Implications for Parkinson disease. Autophagy. 2014;10:376-378.
Not in our library10.4161/auto.27191
339.
Bioactive sphingolipids: metabolism and function · 2009
Not checked
340.
Xu Y.H., Barnes S., Sun Y., Grabowski G.A. Multi-system disorders of glycosphingolipid and ganglioside metabolism. J. Lipid Res. 2010;51:1643-1675.
Not in our library10.1194/jlr.r003996
341.
Proia R.L., Hla T. Emerging biology of sphingosine-1-phosphate: Its role in pathogenesis and therapy. J. Clin. Investig. 2015;125:1379-1387.
Not in our library10.1172/jci76369
342.
Martin R., Sospedra M. Sphingosine-1 phosphate and central nervous system. Curr. Top. Microbiol. Immunol. 2014;378:149-170.
Not in our library10.1007/978-3-319-05879-5_7
343.
Taguchi Y.V., Liu J., Ruan J., Pacheco J., Zhang X., Abbasi J., Keutzer J., Mistry P.K., Chandra S.S. Glucosylsphingosine Promotes α-Synuclein Pathology in Mutant GBA-Associated Parkinson’s Disease. J. Neurosci. 2017;37:9617-9631.
Not in our library10.1523/jneurosci.1525-17.2017
344.
Motyl J., Wencel P.L., Cieślik M., Strosznajder R.P., Strosznajder J.B. Alpha-synuclein alters differently gene expression of Sirts, PARPs and other stress response proteins: Implications for neurodegenerative disorders. Mol. Neurobiol. 2018;55:727-740.
Not in our library10.1007/s12035-016-0317-1
345.
Zhang L., Okada T., Badawy S.M.M., Hirai C., Kajimoto T., Nakamura S.I. Extracellular α-synuclein induces sphingosine 1-phosphate receptor subtype 1 uncoupled from inhibitory G-protein leaving β-arrestin signal intact. Sci. Rep. 2017;7:44248.
Not in our library10.1038/srep44248
346.
Badawy S.M.M., Okada T., Kajimoto T., Hirase M., Matovelo S.A., Nakamura S., Yoshida D., Ijuin T., Nakamura S.I. Extracellular α-synuclein drives sphingosine 1-phosphate receptor subtype 1 out of lipid rafts, leading to impaired inhibitory G-protein signaling. J. Biol. Chem. 2018;293:8208-8216.
Not in our library10.1074/jbc.ra118.001986
347.
Sivasubramanian M., Kanagaraj N., Dheen S.T., Tay S.S.W. Sphingosine kinase 2 and sphingosine-1-phosphate promotes mitochondrial function in dopaminergic neurons of mouse model of Parkinson’s disease and in MPP+-treated MN9D cells in vitro. Neuroscience. 2015;290:636-648.
Not in our library10.1016/j.neuroscience.2015.01.032
348.
Pyszko J.A., Strosznajder J.B. The key role of sphingosine kinases in the molecular mechanism of neuronal cell survival and death in an experimental model of Parkinson’s disease. Folia Neuropathol. 2014;52:260-269.
Not in our library10.5114/fn.2014.45567
349.
Pyszko J., Strosznajder J.B. Sphingosine kinase 1 and sphingosine-1-phosphate in oxidative stress evoked by 1-methyl-4-phenylpyridinium (MPP+) in human dopaminergic neuronal cells. Mol. Neurobiol. 2014;50:38-48.
Not in our library10.1007/s12035-013-8622-4
350.
Zhao P., Yang X., Yang L., Li M., Wood K., Liu Q., Zhu X. Neuroprotective effects of fingolimod in mouse models of Parkinson’s disease. FASEB J. 2017;31:172-179.
Not in our library10.1096/fj.201600751r
351.
Ceramide function in the brain: when a slight tilt is enough · 2012
No notice
352.
Castro B.M., Prieto M., Silva L.C. Ceramide: A simple sphingolipid with unique biophysical properties. Prog. Lipid Res. 2014;54:53-67.
Not in our library10.1016/j.plipres.2014.01.004
353.
Kogot-Levin A., Saada A. Ceramide and the mitochondrial respiratory chain. Biochimie. 2014;100:88-94.
Not in our library10.1016/j.biochi.2013.07.027
354.
Plasma Ceramide and Glucosylceramide Metabolism Is Altered in Sporadic Parkinson's Disease and Associated with Cognitive Impairment: A Pilot Study · 2013
No notice
355.
Atashrazm F., Hammond D., Perera G., Dobson-Stone C., Mueller N., Pickford R., Kim W.S., Kwok J.B., Lewis S.J.G., Halliday G.M., et al. Reduced glucocerebrosidase activity in monocytes from patients with Parkinson’s disease. Sci. Rep. 2018;8:15446.
Not in our library10.1038/s41598-018-33921-x
356.
Murphy K.E., Gysbers A.M., Abbott S.K., Tayebi N., Kim W.S., Sidransky E., Cooper A., Garner B., Halliday G.M. Reduced glucocerebrosidase is associated with increased α-synuclein in sporadic Parkinson’s disease. Brain. 2014;137:834-848.
Not in our library10.1093/brain/awt367
357.
Kim M.J., Jeon S., Burbulla L.F., Krainc D. Acid ceramidase inhibition ameliorates α-synuclein accumulation upon loss of GBA1 function. Hum. Mol. Genet. 2018;27:1972-1988.
Not in our library10.1093/hmg/ddy105
358.
Abbott S.K., Li H., Muñoz S.S., Knoch B., Batterham M., Murphy K.E., Halliday G.M., Garner B. Altered ceramide acyl chain length and ceramide synthase gene expression in Parkinson’s disease. Mov. Disord. 2014;29:518-526.
Not in our library10.1002/mds.25729
359.
Halliday G.M., McCann H. The progression of pathology in Parkinson’s disease. Ann. N. Y. Acad. Sci. 2010;1184:188-195.
Not in our library10.1111/j.1749-6632.2009.05118.x
360.
Lin G., Lee P.T., Chen K., Mao D., Tan K.L., Zuo Z., Lin W.W., Wang L., Bellen H.J. Phospholipase PLA2G6, a Parkinsonism-Associated Gene, Affects Vps26 and Vps35, Retromer Function, and Ceramide Levels, Similar to α-Synuclein Gain. Cell Metab. 2018.
Not in our library10.1016/j.cmet.2018.05.019
361.
Ferrazza R., Cogo S., Melrose H., Bubacco L., Greggio E., Guella G., Civiero L., Plotegher N. LRRK2 deficiency impacts ceramide metabolism in brain. Biochem. Biophys. Res. Commun. 2016;478:1141-1146.
Not in our library10.1016/j.bbrc.2016.08.082
362.
Torres-Odio S., Key J., Hoepken H.H., Canet-Pons J., Valek L., Roller B., Walter M., Morales-Gordo B., Meierhofer D., Harter P.N., et al. Progression of pathology in PINK1-deficient mouse brain from splicing via ubiquitination, ER stress, and mitophagy changes to neuroinflammation. J. Neuroinflamm. 2017;14:154.
Not in our library10.1186/s12974-017-0928-0
363.
Arboleda G., Cárdenas Y., Rodríguez Y., Morales L.C., Matheus L., Arboleda H. Differential regulation of AKT, MAPK and GSK3β during C2-ceramide-induced neuronal death. Neurotoxicology. 2010;31:687-693.
Not in our library10.1016/j.neuro.2010.08.001
364.
Ceramide sphingolipid signaling mediates Tumor Necrosis Factor (TNF)-dependent toxicity via caspase signaling in dopaminergic neurons · 2012
Not checked
365.
France-Lanord V., Brugg B., Michel P.P., Agid Y., Ruberg M. Mitochondrial free radical signal in ceramide-dependent apoptosis: A putative mechanism for neuronal death in Parkinson’s disease. J. Neurochem. 1997;69:1612-1621.
Not in our library10.1046/j.1471-4159.1997.69041612.x
366.
Arboleda G., Waters C., Gibson R. Inhibition of caspases but not of calpains temporarily protect against C2-ceramide-induced death of CAD cells. Neurosci. Lett. 2007;421:245-249.
Not in our library10.1016/j.neulet.2007.05.032
367.
Da Costa C.A., Ancolio K., Checler F. Wild-type but not Parkinson’s disease-related ala-53→Thr mutant alpha -synuclein protects neuronal cells from apoptotic stimuli. J. Biol. Chem. 2000;275:24065-24069.
Not in our library10.1074/jbc.m002413200
368.
Sánchez-Mora R.M., Arboleda H., Arboleda G. PINK1 overexpression protects against C2-ceramide-induced CAD cell death through the PI3K/AKT pathway. J. Mol. Neurosci. 2012;47:582-594.
Not in our library10.1007/s12031-011-9687-z
369.
Rojas-Charry L., Cookson M.R., Niño A., Arboleda H., Arboleda G. Downregulation of Pink1 influences mitochondrial fusion-fission machinery and sensitizes to neurotoxins in dopaminergic cells. Neurotoxicology. 2014;44:140-148.
Not in our library10.1016/j.neuro.2014.04.007
370.
Jaramillo-Gómez J., Niño A., Arboleda H., Arboleda G. Overexpression of DJ-1 protects against C2-ceramide-induced neuronal death through activation of the PI3K/AKT pathway and inhibition of autophagy. Neurosci. Lett. 2015;603:71-76.
Not in our library10.1016/j.neulet.2015.07.032
371.
Jung J.S., Shin K.O., Lee Y.M., Shin J.A., Park E.M., Jeong J., Kim D.H., Choi J.W., Kim H.S. Anti-inflammatory mechanism of exogenous C2 ceramide in lipopolysaccharide-stimulated microglia. Biochim. Biophys. Acta. 2013;1831:1016-1026.
Not in our library10.1016/j.bbalip.2013.01.020
372.
Yang W., Wang X., Duan C., Lu L., Yang H. Alpha-synuclein overexpression increases phospho-protein phosphatase 2A levels via formation of calmodulin/Src complex. Neurochem. Int. 2013;63:180-194.
Not in our library10.1016/j.neuint.2013.06.010
373.
Wang Y., Liu J., Chen M., Du T., Duan C., Gao G., Yang H. The novel mechanism of rotenone-induced α-synuclein phosphorylation via reduced protein phosphatase 2A activity. Int. J. Biochem. Cell Biol. 2016;75:34-44.
Not in our library10.1016/j.biocel.2016.03.007
374.
Nixon G.F. Sphingolipids in inflammation: Pathological implications and potential therapeutic targets. Br. J. Pharmacol. 2009;158:982-993.
Not in our library10.1111/j.1476-5381.2009.00281.x
375.
Dietary and Endogenous Sphingolipid Metabolism in Chronic Inflammation · 2017
No notice
376.
Kiraz Y., Adan A., Kartal Yandim M., Baran Y. Major apoptotic mechanisms and genes involved in apoptosis. Tumour Biol. 2016;37:8471-8486.
Not in our library10.1007/s13277-016-5035-9
377.
Ceramides in Alzheimer’s Disease: Key Mediators of Neuronal Apoptosis Induced by Oxidative Stress and A β Accumulation · 2015
No notice
378.
Tommasino C., Marconi M., Ciarlo L., Matarrese P., Malorni W. Autophagic flux and autophagosome morphogenesis require the participation of sphingolipids. Apoptosis. 2015;20:645-657.
Not in our library10.1007/s10495-015-1102-8
379.
Foo J.N., Liany H., Bei J.X., Yu X.-Q., Liu J., Au W.L., Prakash K.M., Tan L.C., Tan E.K. Rare lysosomal enzyme gene SMPD1 variant (p.R591C) associates with Parkinson’s disease. Neurobiol. Aging. 2013;34:2890.e13-5.
Not in our library10.1016/j.neurobiolaging.2013.06.010
380.
Mao C.Y., Yang J., Wang H., Zhang S.Y., Yang Z.H., Luo H.Y., Li F., Shi M., Liu Y.T., Zhuang Z.P., et al. SMPD1 variants in Chinese Han patients with sporadic Parkinson’s disease. Park. Relat. Disord. 2017;34:59-61.
Not in our library10.1016/j.parkreldis.2016.10.014
381.
Kim W.S., Halliday G.M. Changes in sphingomyelin level affect alpha-synuclein and ABCA5 expression. J. Park. Dis. 2012;2:41-46.
Not in our library10.3233/jpd-2012-11059
382.
Den Jager W.A. Sphingomyelin in Lewy inclusion bodies in Parkinson’s disease. Arch. Neurol. 1969;21:615-619.
Not in our library10.1001/archneur.1969.00480180071006
383.
No evidence for substrate accumulation in Parkinson brains with GBA mutations · 2015
No notice
384.
Merrill A.H. Sphingolipid and glycosphingolipid metabolic pathways in the era of sphingolipidomics. Chem. Rev. 2011;111:6387-6422.
Not in our library10.1021/cr2002917
385.
Kurup R.K., Kurup P.A. Hypothalamic digoxin-mediated model for Parkinson’s disease. Int. J. Neurosci. 2003;113:515-536.
Not in our library10.1080/00207450390162263
386.
Boutin M., Sun Y., Shacka J.J., Auray-Blais C. Tandem Mass Spectrometry Multiplex Analysis of Glucosylceramide and Galactosylceramide Isoforms in Brain Tissues at Different Stages of Parkinson Disease. Anal. Chem. 2016;88:1856-1863.
Not in our library10.1021/acs.analchem.5b04227
387.
Gegg M.E., Schapira A.H.V. The role of glucocerebrosidase in Parkinson disease pathogenesis. FEBS J. 2018.
Not in our library10.1111/febs.14393
388.
Marshall M.S., Bongarzone E.R. Beyond Krabbe’s disease: The potential contribution of galactosylceramidase deficiency to neuronal vulnerability in late-onset synucleinopathies. J. Neurosci. Res. 2016;94:1328-1332.
Not in our library10.1002/jnr.23751
389.
Kim S., Yun S.P., Lee S., Umanah G.E., Bandaru V.V.R., Yin X., Rhee P., Karuppagounder S.S., Kwon S.H., Lee H., et al. GBA1 deficiency negatively affects physiological α-synuclein tetramers and related multimers. Proc. Natl. Acad. Sci. USA. 2018;115:798-803.
Not in our library10.1073/pnas.1700465115
390.
Zunke F., Moise A.C., Belur N.R., Gelyana E., Stojkovska I., Dzaferbegovic H., Toker N.J., Jeon S., Fredriksen K., Mazzulli J.R. Reversible Conformational Conversion of α-Synuclein into Toxic Assemblies by Glucosylceramide. Neuron. 2017;97:92-107.e10.
Not in our library10.1016/j.neuron.2017.12.012
391.
Xu Y.H., Sun Y., Ran H., Quinn B., Witte D., Grabowski G.A. Accumulation and distribution of α-synuclein and ubiquitin in the CNS of Gaucher disease mouse models. Mol. Genet. Metab. 2011;102:436-447.
Not in our library10.1016/j.ymgme.2010.12.014
392.
Suzuki M., Fujikake N., Takeuchi T., Kohyama-Koganeya A., Nakajima K., Hirabayashi Y., Wada K., Nagai Y. Glucocerebrosidase deficiency accelerates the accumulation of proteinase K-resistant α-synuclein and aggravates neurodegeneration in a Drosophila model of Parkinson’s disease. Hum. Mol. Genet. 2015;24:6675-6686.
Not in our library10.1093/hmg/ddv372
393.
Mazzulli J.R., Xu Y.H., Sun Y., Knight A.L., McLean P.J., Caldwell G.A., Sidransky E., Grabowski G.A., Krainc D. Gaucher disease glucocerebrosidase and α-synuclein form a bidirectional pathogenic loop in synucleinopathies. Cell. 2011;146:37-52.
Not in our library10.1016/j.cell.2011.06.001
394.
Sardi S.P., Viel C., Clarke J., Treleaven C.M., Richards A.M., Park H., Olszewski M.A., Dodge J.C., Marshall J., Makino E., et al. Glucosylceramide synthase inhibition alleviates aberrations in synucleinopathy models. Proc. Natl. Acad. Sci. USA. 2017;114:2699-2704.
Not in our library10.1073/pnas.1616152114
395.
Noelker C., Lu L., Höllerhage M., Vulinovic F., Sturn A., Roscher R., Höglinger G.U., Hirsch E.C., Oertel W.H., Alvarez-Fisher D., et al. Glucocerebrosidase deficiency and mitochondrial impairment in experimental Parkinson disease. J. Neurol. Sci. 2015;356:129-136.
Not in our library10.1016/j.jns.2015.06.030
396.
Hallett P.J., Huebecker M., Brekk O.R., Moloney E.B., Rocha E.M., Priestman D.A., Platt F.M., Isacson O. Glycosphingolipid levels and glucocerebrosidase activity are altered in normal aging of the mouse brain. Neurobiol. Aging. 2018;67:189-200.
Not in our library10.1016/j.neurobiolaging.2018.02.028
397.
Yu R.K., Tsai Y.T., Ariga T., Yanagisawa M. Structures, biosynthesis, and functions of gangliosides—An overview. J. Oleo Sci. 2011;60:537-544.
Not in our library10.5650/jos.60.537
398.
The Role of Gangliosides in Neurodevelopment · 2015
No notice
399.
Schnaar R.L. Gangliosides of the Vertebrate Nervous System. J. Mol. Biol. 2016;428:3325-3336.
Not in our library10.1016/j.jmb.2016.05.020
400.
Wu G., Lu Z.H., Kulkarni N., Ledeen R.W. Deficiency of ganglioside GM1 correlates with Parkinson’s disease in mice and humans. J. Neurosci. Res. 2012;90:1997-2008.
Not in our library10.1002/jnr.23090
401.
Schneider J.S. Altered expression of genes involved in ganglioside biosynthesis in substantia nigra neurons in Parkinson’s disease. PLoS ONE. 2018;13:e0199189.
Not in our library10.1371/journal.pone.0199189
402.
Schneider J.S., Cambi F., Gollomp S.M., Kuwabara H., Brašić J.R., Leiby B., Sendek S., Wong D.F. GM1 ganglioside in Parkinson’s disease: Pilot study of effects on dopamine transporter binding. J. Neurol. Sci. 2015;356:118-123.
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403.
Schneider J.S., Gollomp S.M., Sendek S., Colcher A., Cambi F., Du W. A randomized, controlled, delayed start trial of GM1 ganglioside in treated Parkinson’s disease patients. J. Neurol. Sci. 2013;324:140-148.
Not in our library10.1016/j.jns.2012.10.024
404.
Schneider J.S., Sendek S., Daskalakis C., Cambi F. GM1 ganglioside in Parkinson’s disease: Results of a five year open study. J. Neurol. Sci. 2010;292:45-51.
Not in our library10.1016/j.jns.2010.02.009
405.
Schneider J.S. GM1 ganglioside in the treatment of Parkinson’s disease. Ann. N. Y. Acad. Sci. 1998;845:363-373.
Not in our library10.1111/j.1749-6632.1998.tb09688.x
406.
Schneider J.S., Roeltgen D.P., Mancall E.L., Chapas-Crilly J., Rothblat D.S., Tatarian G.T. Parkinson’s disease: Improved function with GM1 ganglioside treatment in a randomized placebo-controlled study. Neurology. 1998;50:1630-1636.
Not in our library10.1212/wnl.50.6.1630
407.
Schneider J.S., Roeltgen D.P., Rothblat D.S., Chapas-Crilly J., Seraydarian L., Rao J. GM1 ganglioside treatment of Parkinson’s disease: An open pilot study of safety and efficacy. Neurology. 1995;45:1149-1154.
Not in our library10.1212/wnl.45.6.1149
408.
Schneider J.S., Seyfried T.N., Choi H.S., Kidd S.K. Intraventricular Sialidase Administration Enhances GM1 Ganglioside Expression and Is Partially Neuroprotective in a Mouse Model of Parkinson’s Disease. PLoS ONE. 2015;10:e0143351.
Not in our library10.1371/journal.pone.0143351
409.
Xu R., Zhou Y., Fang X., Lu Y., Li J., Zhang J., Deng X., Li S. The possible mechanism of Parkinson’s disease progressive damage and the preventive effect of GM1 in the rat model induced by 6-hydroxydopamine. Brain Res. 2014;1592:73-81.
Not in our library10.1016/j.brainres.2014.09.053
410.
Goettl V.M., Wemlinger T.A., Duchemin A.M., Neff N.H., Hadjiconstantinou M. GM1 ganglioside restores dopaminergic neurochemical and morphological markers in aged rats. Neuroscience. 1999;92:991-1000.
Not in our library10.1016/s0306-4522(98)00756-8
411.
Emborg M.E., Colombo J.A. Long-term MPTP-treated monkeys are resistant to GM1 systemic therapy. Mol. Chem. Neuropathol. 1994;21:75-82.
Not in our library10.1007/bf03160086
412.
Pope-Coleman A., Schneider J.S. Effects of Chronic GM1 Ganglioside Treatment on Cognitieve and Motor Deficits in a Slowly Progressing Model of Parkinsonism in Non-Human Primates. Restor. Neurol. Neurosci. 1998;12:255-266.
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413.
Herrero M.T., Perez-Otaño I., Oset C., Kastner A., Hirsch E.C., Agid Y., Luguin M.R., Obeso J.A., Del Río J. GM-1 ganglioside promotes the recovery of surviving midbrain dopaminergic neurons in MPTP-treated monkeys. Neuroscience. 1993;56:965-972.
Not in our library10.1016/0306-4522(93)90142-3
414.
Rothblat D.S., Schneider J.S. Effects of GM1 ganglioside treatment on dopamine innervation of the striatum of MPTP-treated mice. Ann. N. Y. Acad. Sci. 1998;845:274-277.
Not in our library10.1111/j.1749-6632.1998.tb09680.x
415.
Schneider J.S., Kean A., DiStefano L. GM1 ganglioside rescues substantia nigra pars compacta neurons and increases dopamine synthesis in residual nigrostriatal dopaminergic neurons in MPTP-treated mice. J. Neurosci. Res. 1995;42:117-123.
Not in our library10.1002/jnr.490420113
416.
Kastner A., Herrero M.T., Hirsch E.C., Guillen J., Luquin M.R., Javoy-Agid F., Obeso J.A., Agid Y. Decreased tyrosine hydroxylase content in the dopaminergic neurons of MPTP-intoxicated monkeys: Effect of levodopa and GM1 ganglioside therapy. Ann. Neurol. 1994;36:206-214.
Not in our library10.1002/ana.410360213
417.
Herrero M.T., Kastner A., Perez-Otaño I., Hirsch E.C., Luquin M.R., Javoy-Agid F., Del Río J., Obeso J.A., Agid Y. Gangliosides and parkinsonism. Neurology. 1993;43:2132-2134.
Not in our library10.1212/wnl.43.10.2132
418.
Schneider J.S., Pope A., Simpson K., Taggart J., Smith M.G., DiStefano L. Recovery from experimental parkinsonism in primates with GM1 ganglioside treatment. Science. 1992;256:843-846.
Not in our library10.1126/science.1350379
419.
Schneider J.S. MPTP-induced parkinsonism: Acceleration of biochemical and behavioral recovery by GM1 ganglioside treatment. J. Neurosci. Res. 1992;31:112-119.
Not in our library10.1002/jnr.490310116
420.
Fazzini E., Durso R., Davoudi H., Szabo G.K., Albert M.L. GM1 gangliosides alter acute MPTP-induced behavioral and neurochemical toxicity in mice. J. Neurol. Sci. 1990;99:59-68.
Not in our library10.1016/0022-510x(90)90199-w
421.
Gupta M., Schwarz J., Chen X.L., Roisen F.J. Gangliosides prevent MPTP toxicity in mice—An immunocytochemical study. Brain Res. 1990;527:330-334.
Not in our library10.1016/0006-8993(90)91154-9
422.
Schneider J.S., Yuwiler A. GM1 ganglioside treatment promotes recovery of striatal dopamine concentrations in the mouse model of MPTP-induced parkinsonism. Exp. Neurol. 1989;105:177-183.
Not in our library10.1016/0014-4886(89)90117-9
423.
Hadjiconstantinou M., Mariani A.P., Neff N.H. GM1 ganglioside-induced recovery of nigrostriatal dopaminergic neurons after MPTP: An immunohistochemical study. Brain Res. 1989;484:297-303.
Not in our library10.1016/0006-8993(89)90373-9
424.
Ba X. Therapeutic effects of GM1 on Parkinson’s disease in rats and its mechanism. Int. J. Neurosci. 2016;126:163-167.
Not in our library10.3109/00207454.2014.996640
425.
Lundius E.G., Vukojevic V., Hertz E., Stroth N., Cederlund A., Hiraiwa M., Terenius L., Svennigsson P. GPR37 protein trafficking to the plasma membrane regulated by prosaposin and GM1 gangliosides promotes cell viability. J. Biol. Chem. 2014;289:4660-4673.
Not in our library10.1074/jbc.m113.510883
426.
Park J.Y., Kim K.S., Lee S.B., Ryu J.S., Chung K.C., Choo Y.K., Jou I., Kim J., Park S.M. On the mechanism of internalization of alpha-synuclein into microglia: Roles of ganglioside GM1 and lipid raft. J. Neurochem. 2009;110:400-411.
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427.
Acceleration of α-Synuclein Aggregation by Exosomes · 2015
No notice
428.
Martinez Z., Zhu M., Han S., Fink A.L. GM1 specifically interacts with alpha-synuclein and inhibits fibrillation. Biochemistry. 2007;46:1868-1877.
Not in our library10.1021/bi061749a
429.
Garten M., Prévost C., Cadart C., Gautier R., Bousset L., Melki R., Bassereau P., Vanni S. Methyl-branched lipids promote the membrane adsorption of α-synuclein by enhancing shallow lipid-packing defects. Phys. Chem. Chem. Phys. 2015;17:15589-15597.
Not in our library10.1039/c5cp00244c
430.
Wu G., Lu Z.H., Kulkarni N., Amin R., Ledeen R.W. Mice lacking major brain gangliosides develop parkinsonism. Neurochem. Res. 2011;36:1706-1714.
Not in our library10.1007/s11064-011-0437-y
431.
Suzuki K., Iseki E., Togo T., Yamaguchi A., Katsuse O., Katsuyama K., Kanzaki S., Shiozaki K., Kawanishi C., Yamashita S., et al. Neuronal and glial accumulation of alpha- and beta-synucleins in human lipidoses. Acta Neuropathol. 2007;114:481-489.
Not in our library10.1007/s00401-007-0264-z
432.
Akkhawattanangkul Y., Maiti P., Xue Y., Aryal D., Wetsel W.C., Hamilton D., Fowler S.C., McDonald M.P. Targeted deletion of GD3 synthase protects against MPTP-induced neurodegeneration. Genes Brain Behav. 2017;16:522-536.
Not in our library10.1111/gbb.12377
433.
Ryu J.K., Shin W.H., Kim J., Joe E.H., Lee Y.B., Cho K.G., Oh Y.J., Kim S.U., Jun B.K. Trisialoganglioside GT1b induces in vivo degeneration of nigral dopaminergic neurons: Role of microglia. Glia. 2002;38:15-23.
Not in our library10.1002/glia.10047
434.
Wei J., Fujita M., Nakai M., Waragai M., Sekigawa A., Sugama S., Takenouchi T., Masliah E., Hashimoto M. Protective role of endogenous gangliosides for lysosomal pathology in a cellular model of synucleinopathies. Am. J. Pathol. 2009;174:1891-1909.
Not in our library10.2353/ajpath.2009.080680
435.
Xiao S., Finkielstein C.V., Capelluto D.G.S. The enigmatic role of sulfatides: New insights into cellular functions and mechanisms of protein recognition. Adv. Exp. Med. Biol. 2013;991:27-40.
Not in our library10.1007/978-94-007-6331-9_3
436.
Antelmi E., Rizzo G., Fabbri M., Capellari S., Scaglione C., Martinelli P. Arylsulphatase A activity in familial parkinsonism: A pathogenetic role? J. Neurol. 2014;261:1803-1809.
Not in our library10.1007/s00415-014-7425-5
437.
Martinelli P., Ippoliti M., Montanari M., Martinelli A., Mochi M., Giuliani S., Sangiorgi S. Arylsulphatase A (ASA) activity in parkinsonism and symptomatic essential tremor. Acta Neurol. Scand. 1994;89:171-174.
Not in our library10.1111/j.1600-0404.1994.tb01656.x
438.
Cheng H., Xu J., McKeel D.W., Han X. Specificity and potential mechanism of sulfatide deficiency in Alzheimer’s disease: An electrospray ionization mass spectrometric study. Cell. Mol. Biol. (Noisy-le-grand). 2003;49:809-818.
Not in our library
439.
Spann N.J., Glass C.K. Sterols and oxysterols in immune cell function. Nat. Immunol. 2013;14:893-900.
Not in our library10.1038/ni.2681
440.
Hannich J.T., Umebayashi K., Riezman H. Distribution and Functions of Sterols and Sphingolipids. Cold Spring Harb. Perspect. Biol. 2011;3:a004762.
Not in our library10.1101/cshperspect.a004762
441.
Powers K.M., Smith-Weller T., Franklin G.M., Longstreth W.T., Swanson P.D., Checkoway H. Dietary fats, cholesterol and iron as risk factors for Parkinson’s disease. Park. Relat. Disord. 2009;15:47-52.
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442.
Johnson C.C., Gorell J.M., Rybicki B.A., Sanders K., Peterson E.L. Adult nutrient intake as a risk factor for Parkinson’s disease. Int. J. Epidemiol. 1999;28:1102-1109.
Not in our library10.1093/ije/28.6.1102
443.
Abbott R.D., Ross G.W., White L.R., Sanderson W.T., Burchfiel C.M., Kashon M., Sharp D.S., Masaki K.H., Curb J.D., Petrovitch H. Environmental, life-style, and physical precursors of clinical Parkinson’s disease: Recent findings from the Honolulu-Asia Aging Study. J. Neurol. 2003;250(Suppl. 3):III30-III39.
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444.
Wang A., Lin Y., Wu Y., Zhang D. Macronutrients intake and risk of Parkinson’s disease: A meta-analysis. Geriatr. Gerontol. Int. 2015;15:606-616.
Not in our library10.1111/ggi.12321
445.
Zhang L., Wang X., Wang M., Sterling N.W., Du G., Lewis M.M., Yao T., Mailman R.B., Li R., Huang X. Circulating Cholesterol Levels May Link to the Factors Influencing Parkinson’s Risk. Front. Neurol. 2017;8:501.
Not in our library10.3389/fneur.2017.00501
446.
Kirbas A., Kirbas S., Cure M.C., Tufekci A. Paraoxonase and arylesterase activity and total oxidative/anti-oxidative status in patients with idiopathic Parkinson’s disease. J. Clin. Neurosci. 2014;21:451-455.
Not in our library10.1016/j.jocn.2013.04.025
447.
Ikeda K., Nakamura Y., Kiyozuka T., Aoyagi J., Hirayama T., Nagata R., Ito H., Iwamoto K., Murata K., Yoshii Y., et al. Serological profiles of urate, paraoxonase-1, ferritin and lipid in Parkinson’s disease: Changes linked to disease progression. Neurodegener. Dis. 2011;8:252-258.
Not in our library10.1159/000323265
448.
Huang X., Alonso A., Guo X., Umbach D.M., Lichtenstein M.L., Ballantyne C.M., Mailman R.B., Mosley T.H., Chen H. Statins, plasma cholesterol, and risk of Parkinson’s disease: A prospective study. Mov. Disord. 2015;30:552-559.
Not in our library10.1002/mds.26152
449.
Miyake Y., Tanaka K., Fukushima W., Sasaki S., Kiyohara C., Tsuboi Y., Yamada T., Oeda T., Miki T., Kawamura N., et al. Case-control study of risk of Parkinson’s disease in relation to hypertension, hypercholesterolemia, and diabetes in Japan. J. Neurol. Sci. 2010;293:82-86.
Not in our library10.1016/j.jns.2010.03.002
450.
Simon K.C., Chen H., Schwarzschild M., Ascherio A. Hypertension, hypercholesterolemia, diabetes, and risk of Parkinson disease. Neurology. 2007;69:1688-1695.
Not in our library10.1212/01.wnl.0000271883.45010.8a
451.
De Lau L.M.L., Koudstaal P.J., Hofman A., Breteler M.M.B. Serum cholesterol levels and the risk of Parkinson’s disease. Am. J. Epidemiol. 2006;164:998-1002.
Not in our library10.1093/aje/kwj283
452.
Rozani V., Gurevich T., Giladi N., El-Ad B., Tsamir J., Hemo B., Peretz C. Higher serum cholesterol and decreased Parkinson’s disease risk: A statin-free cohort study. Mov. Disord. 2018;33:1298-1305.
Not in our library10.1002/mds.27413
453.
Huang X., Auinger P., Eberly S., Oakes D., Schwarzschild M., Ascherio A., Mailman R., Chen H., Parkinson Study Group DATATOP Investigators. Serum cholesterol the progression of Parkinson’s disease: Results from DATATOP. PLoS ONE. 2011;6:e22854.
Not in our library10.1371/journal.pone.0022854
454.
Gudala K., Bansal D., Muthyala H. Role of serum cholesterol in Parkinson’s disease: A meta-analysis of evidence. J. Park. Dis. 2013;3:363-370.
Not in our library10.3233/jpd-130196
455.
Sterling N.W., Lichtenstein M., Lee E.Y., Lewis M.M., Evans A., Eslinger P.J., Du G., Gao X., Chen H., Kong L., et al. Higher Plasma LDL-Cholesterol is Associated with Preserved Executive and Fine Motor Functions in Parkinson’s Disease. Aging Dis. 2016;7:237-245.
Not in our library10.14336/ad.2015.1030
456.
Savica R., Grossardt B.R., Ahlskog J.E., Rocca W.A. Metabolic markers or conditions preceding Parkinson’s disease: A case-control study. Mov. Disord. 2012;27:974-979.
Not in our library10.1002/mds.25016
457.
Singh N.K., Banerjee B.D., Bala K., Mitrabasu Dung Dung A.A., Chhillar N. APOE and LRPAP1 gene polymorphism and risk of Parkinson’s disease. Neurol. Sci. 2014;35:1075-1081.
Not in our library10.1007/s10072-014-1651-6
458.
Mollenhauer B., Trautmann E., Sixel-Döring F., Wicke T., Ebentheuer J., Schaumburg M., Lang E., Focke N.K., Kumar K.R., Lohmann K., et al. Nonmotor and diagnostic findings in subjects with de novo Parkinson disease of the DeNoPa cohort. Neurology. 2013;81:1226-1234.
Not in our library10.1212/wnl.0b013e3182a6cbd5
459.
Hu G., Antikainen R., Jousilahti P., Kivipelto M., Tuomilehto J. Total cholesterol and the risk of Parkinson disease. Neurology. 2008;70:1972-1979.
Not in our library10.1212/01.wnl.0000312511.62699.a8
460.
Cereda E., Cassani E., Barichella M., Caccialanza R., Pezzoli G. Anthropometric indices of fat distribution and cardiometabolic risk in Parkinson’s disease. Nutr. Metab. Cardiovasc. Dis. 2013;23:264-271.
Not in our library10.1016/j.numecd.2011.04.004
461.
Musanti R., Parati E., Lamperti E., Ghiselli G. Decreased cholesterol biosynthesis in fibroblasts from patients with Parkinson disease. Biochem. Med. Metab. Biol. 1993;49:133-142.
Not in our library10.1006/bmmb.1993.1016
462.
Shulman J.M., Yu L., Buchman A.S., Evans D.A., Schneider J.A., Bennett D.A., De Jager P.L. Association of Parkinson Disease Risk Loci With Mild Parkinsonian Signs in Older Persons. JAMA Neurol. 2014;71:429.
Not in our library10.1001/jamaneurol.2013.6222
463.
Lou F., Li M., Liu N., Li X., Ren Y., Luo X. The Polymorphism of SREBF1 Gene rs11868035 G/A Is Associated with susceptibility to Parkinson’s disease in a Chinese Population. Int. J. Neurosci. 2018;1-18.
Not in our library10.1080/00207454.2018.1526796
464.
Yuan X., Cao B., Wu Y., Chen Y., Wei Q., Ou R., Yang J., Chen X., Zhao B., Song W., et al. Association analysis of SNP rs11868035 in SREBF1 with sporadic Parkinson’s disease, sporadic amyotrophic lateral sclerosis and multiple system atrophy in a Chinese population. Neurosci. Lett. 2018;664:128-132.
Not in our library10.1016/j.neulet.2017.11.015
465.
Hasson S.A., Fogel A.I., Wang C., MacArthur R., Guha R., Heman-Ackah S., Martin S., Youle R.J., Inglese J. Chemogenomic profiling of endogenous PARK2 expression using a genome-edited coincidence reporter. ACS Chem. Biol. 2015;10:1188-1197.
Not in our library10.1021/cb5010417
466.
Kim K.Y., Stevens M.V., Akter M.H., Rusk S.E., Huang R.J., Cohen A., Noguchi A., Springer D., Bocharov A.V., Eggerman T.L., et al. Parkin is a lipid-responsive regulator of fat uptake in mice and mutant human cells. J. Clin. Investig. 2011;121:3701-3712.
Not in our library10.1172/jci44736
467.
Yamaguchi S., Yamane T., Takahashi-Niki K., Kato I., Niki T., Goldberg M.S., Shen J., Ishimoto K., Doi T., Iguchi-Ariga S.M. Transcriptional activation of low-density lipoprotein receptor gene by DJ-1 and effect of DJ-1 on cholesterol homeostasis. PLoS ONE. 2012;7:e38144.
Not in our library10.1371/journal.pone.0038144
468.
Kim J.M., Cha S.H., Choi Y.R., Jou I., Joe E.H., Park S.M. DJ-1 deficiency impairs glutamate uptake into astrocytes via the regulation of flotillin-1 and caveolin-1 expression. Sci. Rep. 2016;6:28823.
Not in our library10.1038/srep28823
469.
Kyung J.W., Kim J.M., Lee W., Ha T.Y., Cha S.H., Chung K.H., Choi D.J., Joi I., Song W.K., Joe E.H., et al. DJ-1 deficiency impairs synaptic vesicle endocytosis and reavailability at nerve terminals. Proc. Natl. Acad. Sci. USA. 2018;115:1629-1634.
Not in our library10.1073/pnas.1708754115
470.
Autophagic lysosome reformation dysfunction in glucocerebrosidase deficient cells: relevance to Parkinson disease · 2016
No notice
471.
Cha S.H., Choi Y.R., Heo C.H., Kang S.J., Joe E.H., Jou I., Kim H.M., Park S.M. Loss of parkin promotes lipid rafts-dependent endocytosis through accumulating caveolin-1: Implications for Parkinson’s disease. Mol. Neurodegener. 2015;10:63.
Not in our library10.1186/s13024-015-0060-5
472.
García-Sanz P., Orgaz L., Bueno-Gil G., Espadas I., Rodríguez-Traver E., Kulisevsky J., Gutierrez A., Dávila J.C., González-Polo R.A., Fuentes J.M., et al. N370S-GBA1 mutation causes lysosomal cholesterol accumulation in Parkinson’s disease. Mov. Disord. 2017;32:1409-1422.
Not in our library10.1002/mds.27119
473.
Loss of Leucine-Rich Repeat Kinase 2 (LRRK2) in Rats Leads to Progressive Abnormal Phenotypes in Peripheral Organs · 2013
No notice
474.
Eriksson I., Nath S., Bornefall P., Giraldo A.M.V., Öllinger K. Impact of high cholesterol in a Parkinson’s disease model: Prevention of lysosomal leakage versus stimulation of α-synuclein aggregation. Eur. J. Cell Biol. 2017;96:99-109.
Not in our library10.1016/j.ejcb.2017.01.002
475.
Schmitt M., Dehay B., Bezard E., Garcia-Ladona F.J. U18666A, an activator of sterol regulatory element binding protein pathway, modulates presynaptic dopaminergic phenotype of SH-SY5Y neuroblastoma cells. Synapse. 2017;71:e21980.
Not in our library10.1002/syn.21980
476.
Morissette M., Morin N., Rouillard C., Di Paolo T. Membrane cholesterol removal and replenishment affect rat and monkey brain monoamine transporters. Neuropharmacology. 2018;133:289-306.
Not in our library10.1016/j.neuropharm.2018.01.039
477.
Paul R., Choudhury A., Kumar S., Giri A., Sandhir R., Borah A. Cholesterol contributes to dopamine-neuronal loss in MPTP mouse model of Parkinson’s disease: Involvement of mitochondrial dysfunctions and oxidative stress. PLoS ONE. 2017;12:e0171285.
Not in our library10.1371/journal.pone.0171285
478.
Paul R., Choudhury A., Chandra Boruah D., Devi R., Bhattacharya P., Choudhury M.D., Borach A. Hypercholesterolemia causes psychomotor abnormalities in mice and alterations in cortico-striatal biogenic amine neurotransmitters: Relevance to Parkinson’s disease. Neurochem. Int. 2017;108:15-26.
Not in our library10.1016/j.neuint.2017.01.021
479.
Paul R., Dutta A., Phukan B.C., Mazumder M.K., Justin-Thenmozhi A., Manivasagam T., Bhattacharya P., Borah A. Accumulation of Cholesterol and Homocysteine in the Nigrostriatal Pathway of Brain Contributes to the Dopaminergic Neurodegeneration in Mice. Neuroscience. 2018;388:347-356.
Not in our library10.1016/j.neuroscience.2018.07.041
480.
Raju A., Jaisankar P., Borah A., Mohanakumar K.P. 1-Methyl-4-Phenylpyridinium-Induced Death of Differentiated SH-SY5Y Neurons Is Potentiated by Cholesterol. Ann. Neurosci. 2018;24:243-251.
Not in our library10.1159/000481551
481.
Fantini J., Carlus D., Yahi N. The fusogenic tilted peptide (67-78) of α-synuclein is a cholesterol binding domain. Biochim. Biophys. Acta. 2011;1808:2343-2351.
Not in our library10.1016/j.bbamem.2011.06.017
482.
Kamp F., Beyer K. Binding of alpha-synuclein affects the lipid packing in bilayers of small vesicles. J. Biol. Chem. 2006;281:9251-9259.
Not in our library10.1074/jbc.m512292200
483.
Van Maarschalkerweerd A., Vetri V., Vestergaard B. Cholesterol facilitates interactions between α-synuclein oligomers and charge-neutral membranes. FEBS Lett. 2015;589:2661-2667.
Not in our library10.1016/j.febslet.2015.08.013
484.
Shvadchak V.V., Falomir-Lockhart L.J., Yushchenko D.A., Jovin T.M. Specificity and kinetics of alpha-synuclein binding to model membranes determined with fluorescent excited state intramolecular proton transfer (ESIPT) probe. J. Biol. Chem. 2011;286:13023-13032.
Not in our library10.1074/jbc.m110.204776
485.
Murphy K.E., Gysbers A.M., Abbott S.K., Spiro A.S., Furuta A., Cooper A., Garner B., Kabuta T., Halliday G.M. Lysosomal-associated membrane protein 2 isoforms are differentially affected in early Parkinson’s disease. Mov. Disord. 2015;30:1639-1647.
Not in our library10.1002/mds.26141
486.
Bar-On P., Crews L., Koob A.O., Mizuno H., Adame A., Spencer B., Masliah E. Statins reduce neuronal alpha-synuclein aggregation in in vitro models of Parkinson’s disease. J. Neurochem. 2008;105:1656-1667.
Not in our library10.1111/j.1471-4159.2008.05254.x
487.
Common molecular mechanism of amyloid pore formation by Alzheimer’s β-amyloid peptide and α-synuclein · 2016
No notice
488.
Fantini J., Yahi N. The driving force of alpha-synuclein insertion and amyloid channel formation in the plasma membrane of neural cells: Key role of ganglioside- and cholesterol-binding domains. Adv. Exp. Med. Biol. 2013;991:15-26.
Not in our library10.1007/978-94-007-6331-9_2
489.
Bate C., Williams A. α-Synuclein-induced synapse damage in cultured neurons is mediated by cholesterol-sensitive activation of cytoplasmic phospholipase A2. Biomolecules. 2015;5:178-193.
Not in our library10.3390/biom5010178
490.
Bar-On P., Rockenstein E., Adame A., Ho G., Hashimoto M., Masliah E. Effects of the cholesterol-lowering compound methyl-beta-cyclodextrin in models of alpha-synucleinopathy. J. Neurochem. 2006;98:1032-1045.
Not in our library10.1111/j.1471-4159.2006.04017.x
491.
Fortin D.L., Troyer M.D., Nakamura K., Kubo S., Anthony M.D., Edwards R.H. Lipid rafts mediate the synaptic localization of alpha-synuclein. J. Neurosci. 2004;24:6715-6723.
Not in our library10.1523/jneurosci.1594-04.2004
492.
Hsiao J.H.T., Halliday G.M., Kim W.S. α-Synuclein Regulates Neuronal Cholesterol Efflux. Molecules. 2017;22:1769.
Not in our library10.3390/molecules22101769
493.
Leftin A., Job C., Beyer K., Brown M.F. Solid-state 13C NMR reveals annealing of raft-like membranes containing cholesterol by the intrinsically disordered protein α-Synuclein. J. Mol. Biol. 2013;425:2973-2987.
Not in our library10.1016/j.jmb.2013.04.002
494.
Bosco D.A., Fowler D.M., Zhang Q., Nieva J., Powers E.T., Wentworth P., Lerner R.A., Kelly J.W. Elevated levels of oxidized cholesterol metabolites in Lewy body disease brains accelerate alpha-synuclein fibrilization. Nat. Chem. Biol. 2006;2:249-253.
Not in our library10.1038/nchembio782
495.
Chesselet M.F., Fleming S., Mortazavi F., Meurers B. Strengths and limitations of genetic mouse models of Parkinson’s disease. Park. Relat. Disord. 2008;14(Suppl. 2):S84-S87.
Not in our library10.1016/j.parkreldis.2008.04.004
496.
Sheng Z., Jia X., Kang M. Statin use and risk of Parkinson’s disease: A meta-analysis. Behav. Brain Res. 2016;309:29-34.
Not in our library10.1016/j.bbr.2016.04.046
497.
Friedman B., Lahad A., Dresner Y., Vinker S. Long-term statin use and the risk of Parkinson’s disease. Am. J. Manag. Care. 2013;19:626-632.
Not in our library
498.
Gao X., Simon K.C., Schwarzschild M.A., Ascherio A. Prospective study of statin use and risk of Parkinson disease. Arch. Neurol. 2012;69:380-384.
Not in our library10.1001/archneurol.2011.1060
499.
Simvastatin is associated with a reduced incidence of dementia and Parkinson's disease · 2007
No notice
500.
Huang X., Chen H., Miller W.C., Mailman R.B., Woodard J.L., Chen P.C., Xiang D., Murrow R.M., Wand Y.Z., Poole C. Lower low-density lipoprotein cholesterol levels are associated with Parkinson’s disease. Mov. Disord. 2007;22:22.
Not in our library10.1002/mds.21290
501.
Wahner A.D., Bronstein J.M., Bordelon Y.M., Ritz B. Statin use and the risk of Parkinson disease. Neurology. 2008;70:1418-1422.
Not in our library10.1212/01.wnl.0000286942.14552.51
502.
Rozani V., Giladi N., El-Ad B., Gurevich T., Tsamir J., Hemo B., Peretz C. Statin adherence and the risk of Parkinson’s disease: A population-based cohort study. PLoS ONE. 2017;12:e0175054.
Not in our library10.1371/journal.pone.0175054
503.
Ritz B., Manthripragada A.D., Qian L., Schernhammer E., Wermuth L., Olsen J., Friss S. Statin use and Parkinson’s disease in Denmark. Mov. Disord. 2010;25:1210-1216.
Not in our library10.1002/mds.23102
504.
Becker C., Jick S.S., Meier C.R. Use of statins and the risk of Parkinson’s disease: A retrospective case-control study in the UK. Drug Saf. 2008;31:399-407.
Not in our library10.2165/00002018-200831050-00004
505.
Liu G., Sterling N.W., Kong L., Lewis N.M., Mailman R.B., Chen H., Leslie D., Huang X. Statins may facilitate Parkinson’s disease: Insight gained from a large, national claims database. Mov Disord. 2017;32:913-917.
Not in our library10.1002/mds.27006
506.
Bykov K., Yoshida K., Weisskopf M.G., Gagne J.J. Confounding of the association between statins and Parkinson disease: Systematic review and meta-analysis. Pharmacoepidemiol. Drug Saf. 2017;26:294-300.
Not in our library10.1002/pds.4079
507.
Marques N.F., Castro A.A., Mancini G., Rocha F.L., Santos A.R.S., Prediger R.D., De Bem A.F., Tasca C.I. Atorvastatin Prevents Early Oxidative Events and Modulates Inflammatory Mediators in the Striatum Following Intranasal 1-Methyl-4-phenyl-1, 2, 3, 6-tetrahydropyridine (MPTP) Administration in Rats. Neurotox. Res. 2018;33:549-559.
Not in our library10.1007/s12640-017-9840-8
508.
Yan J.Q., Ma Y.J., Sun J.C., Bai S.F., Huang L.N. Neuroprotective effect of lovastatin by inhibiting NMDA receptor1 in 6-hydroxydopamine treated PC12 cells. Int. J. Clin. Exp. Med. 2014;7:3313-3319.
Not in our library
509.
Jiang P., Gan M., Lin W.L., Yen S.H.C. Nutrient deprivation induces α-synuclein aggregation through endoplasmic reticulum stress response and SREBP2 pathway. Front. Aging Neurosci. 2014;6:268.
Not in our library10.3389/fnagi.2014.00268
510.
Koob A.O., Ubhi K., Paulsson J.F., Kelly J., Rockenstein E., Mante M., Adame A., Masliah E. Lovastatin ameliorates alpha-synuclein accumulation and oxidation in transgenic mouse models of alpha-synucleinopathies. Exp. Neurol. 2010;221:267-274.
Not in our library10.1016/j.expneurol.2009.11.015
511.
Xu Y.Q., Long L., Yan J.Q., Wei L., Pan M.Q., Gao H.M., Zhou P., Liu M., Zhu C.S., Tang B.S., et al. Simvastatin induces neuroprotection in 6-OHDA-lesioned PC12 via the PI3K/AKT/caspase 3 pathway and anti-inflammatory responses. CNS Neurosci. Ther. 2013;19:170-177.
Not in our library10.1111/cns.12053
512.
Kumar A., Sharma N., Gupta A., Kalonia H., Mishra J. Neuroprotective potential of atorvastatin and simvastatin (HMG-CoA reductase inhibitors) against 6-hydroxydopamine (6-OHDA) induced Parkinson-like symptoms. Brain Res. 2012;1471:13-22.
Not in our library10.1016/j.brainres.2012.06.050
513.
Ghosh A., Roy A., Matras J., Brahmachari S., Gendelman H.E., Pahan K. Simvastatin inhibits the activation of p21ras and prevents the loss of dopaminergic neurons in a mouse model of Parkinson’s disease. J. Neurosci. 2009;29:13543-13556.
Not in our library10.1523/jneurosci.4144-09.2009
514.
Selley M.L. Simvastatin prevents 1-methyl-4-phenyl-1, 2, 3, 6-tetrahydropyridine-induced striatal dopamine depletion and protein tyrosine nitration in mice. Brain. Res. 2005;1037:1-6.
Not in our library10.1016/j.brainres.2004.02.083
515.
Wang Q., Tang X.N., Wang L., Yenari M.A., Ying W., Goh B.C., Lee H.S., Wilder-Smith E.P., Wong P.T. Effects of high dose of simvastatin on levels of dopamine and its reuptake in prefrontal cortex and striatum among SD rats. Neurosci. Lett. 2006;408:189-193.
Not in our library10.1016/j.neulet.2006.09.009
516.
Kreisler A., Gelé P., Wiart J.F., Lhermitte M., Destée A., Bordet R. Lipid-lowering drugs in the MPTP mouse model of Parkinson’s disease: Fenofibrate has a neuroprotective effect, whereas bezafibrate and HMG-CoA reductase inhibitors do not. Brain Res. 2007;1135:77-84.
Not in our library10.1016/j.brainres.2006.12.011
517.
Schirris T.J.J., Renkema G.H., Ritschel T., Voermans N.C., Bilos A., van Engelen B.G.M., Brandt U., Koopman W.J., Beyrath J.D., Rodenburg R.J., et al. Statin-Induced Myopathy Is Associated with Mitochondrial Complex III Inhibition. Cell Metab. 2015;22:399-407.
Not in our library10.1016/j.cmet.2015.08.002
518.
Nakamura K., Mori F., Tanji K., Miki Y., Yamada M., Kakita A., Takahasi H., Utsumi J., Sasaki H., Wakabayashi K. Isopentenyl diphosphate isomerase, a cholesterol synthesizing enzyme, is localized in Lewy bodies. Neuropathology. 2015;35:432-440.
Not in our library10.1111/neup.12204
519.
Kabuto H., Yamanushi T.T., Janjua N., Takayama F., Mankura M. Effects of squalene/squalane on dopamine levels, antioxidant enzyme activity, and fatty acid composition in the striatum of Parkinson’s disease mouse model. J. Oleo Sci. 2013;62:21-28.
Not in our library10.5650/jos.62.21
520.
Lim L., Jackson-Lewis V., Wong L.C., Shui G.H., Goh A.X.H., Kesavapany S., Jenner A.M., Fivaz M., Przedborski S., Wenk M.R. Lanosterol induces mitochondrial uncoupling and protects dopaminergic neurons from cell death in a model for Parkinson’s disease. Cell Death Differ. 2012;19:416-427.
Not in our library10.1038/cdd.2011.105
521.
Sodium Phenylbutyrate Controls Neuroinflammatory and Antioxidant Activities and Protects Dopaminergic Neurons in Mouse Models of Parkinson’s Disease · 2012
No notice
522.
Zhang S., Glukhova S.A., Caldwell K.A., Caldwell G.A. NCEH-1 modulates cholesterol metabolism and protects against α-synuclein toxicity in a C. elegans model of Parkinson’s disease. Hum. Mol. Genet. 2017;26:3823-3836.
Not in our library10.1093/hmg/ddx269
523.
Björkhem I., Lövgren-Sandblom A., Leoni V., Meaney S., Brodin L., Salveson L., Winge K., Pålhagen S., Svenningsson P. Oxysterols and Parkinson’s disease: Evidence that levels of 24S-hydroxycholesterol in cerebrospinal fluid correlates with the duration of the disease. Neurosci. Lett. 2013;555:102-105.
Not in our library10.1016/j.neulet.2013.09.003
524.
Dexter D.T., Holley A.E., Flitter W.D., Slater T.F., Wells F.R., Daniel S.E., Lee A.J., Jenner P., Marsden C.D. Increased levels of lipid hydroperoxides in the parkinsonian substantia nigra: An HPLC and ESR study. Mov. Disord. 1994;9:92-97.
Not in our library10.1002/mds.870090115
525.
Björkhem I., Patra K., Boxer A.L., Svenningsson P. 24S-Hydroxycholesterol Correlates with Tau and Is Increased in Cerebrospinal Fluid in Parkinson’s Disease and Corticobasal Syndrome. Front. Neurol. 2018;9:756.
Not in our library10.3389/fneur.2018.00756
526.
Di Natale C., Monaco A., Pedone C., Tessitore A., De Mase A., Tedeschi G., Netti P.A., Abrescia P. The level of 24-hydroxycholesteryl esters decreases in plasma of patients with Parkinson’s disease. Neurosci. Lett. 2018;672:108-112.
Not in our library10.1016/j.neulet.2018.02.041
527.
Rantham Prabhakara J.P., Feist G., Thomasson S., Thompson A., Schommer E., Ghribi O. Differential effects of 24-hydroxycholesterol and 27-hydroxycholesterol on tyrosine hydroxylase and alpha-synuclein in human neuroblastoma SH-SY5Y cells. J. Neurochem. 2008;107:1722-1729.
Not in our library10.1111/j.1471-4159.2008.05736.x
528.
Marwarha G., Rhen T., Schommer T., Ghribi O. The oxysterol 27-hydroxycholesterol regulates α-synuclein and tyrosine hydroxylase expression levels in human neuroblastoma cells through modulation of liver X receptors and estrogen receptors—Relevance to Parkinson’s disease. J. Neurochem. 2011;119:1119-1136.
Not in our library10.1111/j.1471-4159.2011.07497.x
529.
Cheng D., Kim W.S., Garner B. Regulation of alpha-synuclein expression by liver X receptor ligands in vitro. Neuroreport. 2008;19:1685-1689.
Not in our library10.1097/wnr.0b013e32831578b2
530.
Schommer J., Marwarha G., Schommer T., Flick T., Lund J., Ghribi O. 27-Hydroxycholesterol increases α-synuclein protein levels through proteasomal inhibition in human dopaminergic neurons. BMC Neurosci. 2018;19:17.
Not in our library10.1186/s12868-018-0420-5
531.
Emanuelsson I., Norlin M. Protective effects of 27- and 24-hydroxycholesterol against staurosporine-induced cell death in undifferentiated neuroblastoma SH-SY5Y cells. Neurosci. Lett. 2012;525:44-48.
Not in our library10.1016/j.neulet.2012.07.057
532.
Theofilopoulos S., Wang Y., Kitambi S.S., Sacchetti P., Sousa K.M., Bodin K., Kirk J., Saltó C., Gustafsson M., Toledo E.M., et al. Brain endogenous liver X receptor ligands selectively promote midbrain neurogenesis. Nat. Chem. Biol. 2013;9:126-133.
Not in our library10.1038/nchembio.1156
533.
Sacchetti P., Sousa K.M., Hall A.C., Liste I., Steffensen K.R., Theofilopoulos S., Parish C.L., Hazenber C., Richter L.A., Hovatta O., et al. Liver X receptors and oxysterols promote ventral midbrain neurogenesis in vivo and in human embryonic stem cells. Cell Stem Cell. 2009;5:409-419.
Not in our library10.1016/j.stem.2009.08.019
534.
Ramasamy I. Recent advances in physiological lipoprotein metabolism. Clin. Chem. Lab. Med. 2014;52:1695-1727.
Not in our library10.1515/cclm-2013-0358
535.
Kuai R., Li D., Chen Y.E., Moon J.J., Schwendeman A. High-Density Lipoproteins: Nature’s Multifunctional Nanoparticles. ACS Nano. 2016;10:3015-3041.
Not in our library10.1021/acsnano.5b07522
536.
Swanson C.R., Berlyand Y., Xie S.X., Alcalay R.N., Chahine L.M., Chen-Plotkin A.S. Plasma apolipoprotein A1 associates with age at onset and motor severity in early Parkinson’s disease patients. Mov. Disord. 2015;30:1648-1656.
Not in our library10.1002/mds.26290
537.
Swanson C.R., Li K., Unger T.L., Gallagher M.D., Van Deerlin V.M., Agarwal P., Leverenz J., Roberts J., Samii A., Gross R.G., et al. Lower plasma apolipoprotein A1 levels are found in Parkinson’s disease and associate with apolipoprotein A1 genotype. Mov. Disord. 2015;30:805-812.
Not in our library10.1002/mds.26022
538.
Lu W., Wan X., Liu B., Rong X., Zhu L., Li P., Li J., Wang L., Cui L., Wang X. Specific changes of serum proteins in Parkinson’s disease patients. PLoS ONE. 2014;9:e95684.
Not in our library10.1371/journal.pone.0095684
539.
Qiang J.K., Wong Y.C., Siderowf A., Hurtig H.I., Xie S.X., Lee V.M.Y., Trojanowski J.Q., Yearout D., Leverenz J., Montine T.J., et al. Plasma apolipoprotein A1 as a biomarker for Parkinson disease. Ann. Neurol. 2013;74:119-127.
Not in our library10.1002/ana.23872
540.
Cassani E., Cereda E., Barichella M., Madio C., Cancello R., Caccialanza R., Zini M., Cilia R., Pezzoli G. Cardiometabolic factors and disease duration in patients with Parkinson’s disease. Nutrition. 2013;29:1331-1335.
Not in our library10.1016/j.nut.2013.04.013
541.
Kawata M., Nemoto Y., Asahina M., Moroo I., Shinomiya M., Yamada T. Risk factors for cerebral arteriosclerosis in Parkinson’s disease. Park. Relat. Disord. 1996;2:75-79.
Not in our library10.1016/1353-8020(95)00025-9
542.
Du G., Lewis M.M., Shaffer M.L., Chen H., Yang Q.X., Mailman R.B., Huang X. Serum cholesterol and nigrostriatal R2* values in Parkinson’s disease. PLoS ONE. 2012;7:e35397.
Not in our library10.1371/journal.pone.0035397
543.
Huang X., Abbott R.D., Petrovitch H., Mailman R.B., Ross G.W. Low LDL cholesterol and increased risk of Parkinson’s disease: Prospective results from Honolulu-Asia Aging Study. Mov. Disord. 2008;23:1013-1018.
Not in our library10.1002/mds.22013
544.
Benn M., Nordestgaard B.G., Frikke-Schmidt R., Tybjærg-Hansen A. Low LDL cholesterol, PCSK9 and HMGCR genetic variation, and risk of Alzheimer’s disease and Parkinson’s disease: Mendelian randomisation study. BMJ. 2017;357:j1648.
Not in our library10.1136/bmj.j1648
545.
Andican G., Konukoglu D., Bozluolcay M., Bayülkem K., Firtiına S., Burcak G. Plasma oxidative and inflammatory markers in patients with idiopathic Parkinson’s disease. Acta Neurol. Belg. 2012;112:155-159.
Not in our library10.1007/s13760-012-0015-3
546.
Schroeter H., Williams R.J., Matin R., Iversen L., Rice-Evans C.A. Phenolic antioxidants attenuate neuronal cell death following uptake of oxidized low-density lipoprotein. Free Radic. Biol. Med. 2000;29:1222-1233.
Not in our library10.1016/s0891-5849(00)00415-9
547.
Van Meer G., Voelker D.R., Feigenson G.W. Membrane lipids: Where they are and how they behave. Nat. Rev. Mol. Cell Biol. 2008;9:112-124.
Not in our library10.1038/nrm2330
548.
Tumanov S., Kamphorst J.J. Recent advances in expanding the coverage of the lipidome. Curr. Opin. Biotechnol. 2017;43:127-133.
Not in our library10.1016/j.copbio.2016.11.008
549.
Neuronal Lipid Metabolism: Multiple Pathways Driving Functional Outcomes in Health and Disease · 2018
No notice
550.
Piomelli D., Astarita G., Rapaka R. A neuroscientist’s guide to lipidomics. Nat. Rev. Neurosci. 2007;8:743-754.
Not in our library10.1038/nrn2233
551.
Andersen O.S., Koeppe R.E. Bilayer thickness and membrane protein function: An energetic perspective. Annu. Rev. Biophys. Biomol. Struct. 2007;36:107-130.
Not in our library10.1146/annurev.biophys.36.040306.132643
552.
Rohrbough J., Broadie K. Lipid regulation of the synaptic vesicle cycle. Nat. Rev. Neurosci. 2005;6:139-150.
Not in our library10.1038/nrn1608
553.
Galvagnion C., Brown J.W.P., Ouberai M.M., Flagmeier P., Vendruscolo M., Buell A.K., Sparr E., Dobson C.M. Chemical properties of lipids strongly affect the kinetics of the membrane-induced aggregation of α-synuclein. Proc. Natl. Acad. Sci. USA. 2016;113:7065-7070.
Not in our library10.1073/pnas.1601899113
554.
Esposito G., Ana Clara F., Verstreken P. Synaptic vesicle trafficking and Parkinson’s disease. Dev. Neurobiol. 2012;72:134-144.
Not in our library10.1002/dneu.20916
555.
Evidence for Immune Response, Axonal Dysfunction and Reduced Endocytosis in the Substantia Nigra in Early Stage Parkinson’s Disease · 2015
No notice
556.
Spillantini M.G., Crowther R.A., Jakes R., Hasegawa M., Goedert M. alpha-Synuclein in filamentous inclusions of Lewy bodies from Parkinson’s disease and dementia with lewy bodies. Proc. Natl. Acad. Sci. USA. 1998;95:6469-6473.
Not in our library10.1073/pnas.95.11.6469
557.
Castillo P.E., Younts T.J., Chávez A.E., Hashimotodani Y. Endocannabinoid signaling and synaptic function. Neuron. 2012;76:70-81.
Not in our library10.1016/j.neuron.2012.09.020
558.
Fatty Acids in Energy Metabolism of the Central Nervous System · 2014
No notice
559.
Ebert D., Haller R.G., Walton M.E. Energy contribution of octanoate to intact rat brain metabolism measured by 13C nuclear magnetic resonance spectroscopy. J. Neurosci. 2003;23:5928-5935.
Not in our library10.1523/jneurosci.23-13-05928.2003
560.
Rustam Y.H., Reid G.E. Analytical Challenges and Recent Advances in Mass Spectrometry Based Lipidomics. Anal. Chem. 2018;90:374-397.
Not in our library10.1021/acs.analchem.7b04836
561.
Bou Khalil M., Hou W., Zhou H., Elisma F., Swayne L.A., Blanchard A.P., Yao Z., Bennett S.A., Figeys D. Lipidomics era: Accomplishments and challenges. Mass Spectrom. Rev. 2010;29:877-929.
Not in our library10.1002/mas.20294
562.
Hu P., Fabyanic E., Kwon D.Y., Tang S., Zhou Z., Wu H. Dissecting Cell-Type Composition and Activity-Dependent Transcriptional State in Mammalian Brains by Massively Parallel Single-Nucleus RNA-Seq. Mol. Cell. 2017;68:1006-1015.e7.
Not in our library10.1016/j.molcel.2017.11.017
563.
Rubakhin S.S., Romanova E.V., Nemes P., Sweedler J.V. Profiling metabolites and peptides in single cells. Nat. Methods. 2011;8:S20-S29.
Not in our library10.1038/nmeth.1549
564.
Yang K., Han X. Lipidomics: Techniques, Applications, and Outcomes Related to Biomedical Sciences. Trends Biochem. Sci. 2016;41:954-969.
Not in our library10.1016/j.tibs.2016.08.010
565.
Caesar R., Tremaroli V., Kovatcheva-Datchary P., Cani P.D., Bäckhed F. Crosstalk between Gut Microbiota and Dietary Lipids Aggravates WAT Inflammation through TLR Signaling. Cell Metab. 2015;22:658-668.
Not in our library10.1016/j.cmet.2015.07.026
566.
Den Besten G., Lange K., Havinga R., van Dijk T.H., Gerding A., van Eunen K., Müller M., Groen A.K., Hoovield G.J., Bakker B.M., et al. Gut-derived short-chain fatty acids are vividly assimilated into host carbohydrates and lipids. Am. J. Physiol. Gastrointest. Liver Physiol. 2013;305:G900-G910.
Not in our library10.1152/ajpgi.00265.2013
567.
Caesar R., Nygren H., Orešič M., Bäckhed F. Interaction between dietary lipids and gut microbiota regulates hepatic cholesterol metabolism. J. Lipid Res. 2016;57:474-481.
Not in our library10.1194/jlr.m065847
568.
Petersen C., Round J.L. Defining dysbiosis and its influence on host immunity and disease. Cell. Microbiol. 2014;16:1024-1033.
Not in our library10.1111/cmi.12308
569.
Hill-Burns E.M., Debelius J.W., Morton J.T., Wissemann W.T., Lewis M.R., Wallen Z.D., Peddada S.D., Factor S.A., Molho E., Zabetian C.P., et al. Parkinson’s disease and Parkinson’s disease medications have distinct signatures of the gut microbiome. Mov. Disord. 2017;32:739-749.
Not in our library10.1002/mds.26942
570.
The nasal and gut microbiome in Parkinson's disease and idiopathic rapid eye movement sleep behavior disorder · 2017
No notice
571.
Petrov V.A., Saltykova I.V., Zhukova I.A., Alifirova V.M., Zhukova N.G., Dorofeeva Y.B., Tyakht A.V., Kovarsky B.A., Alekseev D.G., Kostryukova E.S., et al. Analysis of Gut Microbiota in Patients with Parkinson’s Disease. Bull. Exp. Biol. Med. 2017;162:734-737.
Not in our library10.1007/s10517-017-3700-7
572.
Unger M.M., Spiegel J., Dillmann K.U., Grundmann D., Philippeit H., Bürmann J., Faßbender K., Schwiertz A., Schäfer K.H. Short chain fatty acids and gut microbiota differ between patients with Parkinson’s disease and age-matched controls. Park. Relat. Disord. 2016;32:66-72.
Not in our library10.1016/j.parkreldis.2016.08.019
573.
Keshavarzian A., Green S.J., Engen P.A., Voigt R.M., Naqib A., Forsyth C.B., Mutlu E., Shannon K.M. Colonic bacterial composition in Parkinson’s disease. Mov. Disord. 2015;30:1351-1360.
Not in our library10.1002/mds.26307
574.
Progression of Parkinson's disease is associated with gut dysbiosis: Two-year follow-up study · 2017
Expression of concern
575.
Cassani E., Barichella M., Cancello R., Cavanna F., Iorio L., Cereda E., Bolliri C., Zampella Maria P., Bianchi F., Cestaro B., et al. Increased urinary indoxyl sulfate (indican): New insights into gut dysbiosis in Parkinson’s disease. Park. Relat. Disord. 2015;21:389-393.
Not in our library10.1016/j.parkreldis.2015.02.004
576.
Lista S., Khachaturian Z.S., Rujescu D., Garaci F., Dubois B., Hampel H. Application of Systems Theory in Longitudinal Studies on the Origin and Progression of Alzheimer’s Disease. Methods Mol. Biol. 2016;1303:49-67.
Not in our library10.1007/978-1-4939-2627-5_2
577.
Dehairs J., Derua R., Rueda-Rincon N., Swinnen J.V. Lipidomics in drug development. Drug Discov. Today Technol. 2015;13:33-38.
Not in our library10.1016/j.ddtec.2015.03.002

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