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Microglial Scavenger Receptors and Their Roles in the Pathogenesis of Alzheimer's Disease

Kim Wilkinson, Joseph El Khoury

International Journal of Alzheimer's Disease · 2012 · Review

doi:10.1155/2012/489456

Abstract

Alzheimer’s disease (AD) is increasing in prevalence with the aging population. Deposition of amyloid- β (A β ) in the brain of AD patients is a hallmark of the disease and is associated with increased microglial numbers and activation state. The interaction of microglia with A β appears to play a dichotomous role in AD pathogenesis. On one hand, microglia can phagocytose and clear A β , but binding of microglia to A β also increases their ability to produce inflammatory cytokines, chemokines, and neurotoxic reactive oxygen species (ROS). Scavenger receptors, a group of evolutionally conserved proteins expressed on the surface of microglia act as receptors for A β . Of particular interest are SCARA-1 (scavenger receptor A-1), CD36, and RAGE (receptor for advanced glycation end products). SCARA-1 appears to be involved in the clearance of A β , while CD36 and RAGE are involved in activation of microglia by A β . In this review, we discuss the roles of various scavenger receptors in the interaction of microglia with A β and propose that these receptors play complementary, nonredundant functions in the development of AD pathology. We also discuss potential therapeutic applications for these receptors in AD.

Full text

From PubMed Central, U.S. National Library of Medicine, as current on Oct 24, 2026. Paragraph numbers are ours, so an answer can point at one.

1. Microglia and Alzheimer's Disease Pathology

Alzheimer's disease (AD) is a devastating neurological condition characterized by increasing memory loss, inability to perform daily tasks, and eventually dementia. This fatal condition currently has no cure, and by 2050, 13 million people in the United States are projected to be affected by the disease. AD brains show deposition of the protein amyloid-β (Aβ) in senile plaques, this protein is produced by cleavage of APP (amyloid precursor protein), by the enzymes β-secretase and γ-secretase. Aβ accumulates in soluble form and also undergoes conformational changes to become fibrillar, microglia interact with both soluble and fibrillar forms of Aβ.

In addition to Aβ accumulation during the development of AD, tau protein also accumulates in neurofibrillary tangles (NFT) in cell bodies of neurons and apical dendrites. Tau is a microtubule-associated protein that segregates into axons and stabilizes their microtubules. In AD, tau dissociates from the microtubules and begins to accumulate in the somatodendritic compartment of the axon, a process which is not fully understood. Tau contains a high number of phosphorylation sites and upon phosphorylation dissociates from the microtubules, as observed in AD. Tau protein then undergoes conformational changes which form fibrils. NFT could possibly activate microglia which may prove deleterious for the surrounding neurons and contribute to disease progression, however, little is known about the NFT mechanism of action.

Microglia are the major phagocytic cell of the brain and become activated upon encountering Aβ and can release chemokines and cytokines into their environment. Microglia are believed to initially clear Aβ deposits, but as the disease progresses, they produce proinflammatory cytokines, chemokines, and reactive oxygen species (ROS) and lose their ability to clear Aβ, and despite increased numbers of microglia in the AD brain, the plaques continue to increase in size and number. This inflammatory environment ultimately becomes toxic to the surrounding neurons, resulting in neuronal degeneration and disease progression.

Scavenger receptors bind many ligands with high affinity, including Aβ, and have been shown to be expressed on microglia surrounding Aβ plaques in the brain. This review will focus on the role of scavenger receptors in AD development and discuss efforts to examine scavenger receptors as targets for therapy.

2. What Are Scavenger Receptors (SRs)?

Several families of pattern recognition receptors (PRR) have been identified including the well-defined and extensively studied Toll-like and Nod-like receptors (TLR and NLRs). In addition to these proteins, the scavenger receptor (SR) family represents another major class of PRR. SRs were first described in 1979 by Brown and Goldstein as macrophage receptors that mediate endocytosis of modified low-density lipoprotein (LDL) leading to foam cell formation and were shown to play a role in the pathogenesis of atherosclerosis. Since then, the definition of SRs has been broadened: SRs are defined as a family of molecules that share the ability to bind polyanionic ligands. This simple definition belies the importance of SRs as PRRs-SRs are archetypal multifunctional receptors, often able to bind ligands of both pathogen and self-origin. These receptors are teleologically ancient pathogen receptors, emphasizing their important role in host defense. However, while the critical roles SRs play in atherosclerosis and host defense against a variety of pathogens is well characterized, the exact role of these receptors in the pathogenesis of neurodegenerative disorders including AD is not clearly understood.

3. Classification of SRs

SRs are structurally unrelated membrane receptors that are highly expressed by phagocytes such as macrophages, dendritic cells, and microglia, and also found on selected endothelial cells (Figure 1). To date, the SRs family has been classified into 6 classes but additional members of this family, like CD163, RAGE, and SR-PSOX (scavenger receptor that binds phosphatidylserine and oxidized lipoprotein) remain unclassified. SRs are defined by their common ability to bind polyanionic ligands with high affinity and have broad specificity. SRs cooperate with the other innate immune PRRs like the TLRs to define pathogen-specific responses. However, unlike the TLRs and NLRs, SRs facilitate ligand uptake by phagocytosis and endocytosis.

4. Class A Scavenger Receptors (SCARA)

SCARA are required for host defense against several bacterial and viral pathogens: SCARA-1 is an arrangement of three coiled extracellular regions with cysteine-rich domains connected to the plasma membrane by a long fibrous stalk composed of an alpha-helical coiled coil and a collagen rich triple helix which is believed to bind ligands through the collagen-like domain (Figure 1). SCARA-1 exemplify this family of multiligand receptors, in addition to binding to modified lipoproteins, lipopolysaccharide (LPS), and lipoteichoic acid (LTA), we and others have shown that SCARA-1/2 also bind fibrillar β-amyloid and advanced glycosylation end products (AGEs). SCARA-1/2 mediate phagocytosis of infectious organisms like Staphylococcus aureus and Neisseria meningitides and also mediate clearance of apoptotic thymocytes. Because of their broad ligand specificity, SCARA-1/2 contribute to resistance to gram-positive and gram-negative microbial infections and some viral infections in vivo, and SCARA-1/2 null mice succumb to S. aureus, and Herpes simplex infections faster than normal mice. In addition, SCARA-1/2 null mice also demonstrate increased susceptibility to LPS-induced shock, suggesting a potential role in regulating the endotoxin response.

4.1. SCARA Role in Alzheimer's Disease

Murine microglia bind and phagocytose Aβ via SCARA1. Studies using a transgenic mouse model of AD expressing the human form of Aβ, and developing Aβ plaques in the brain over time showed an increased level of SCARA-1 on microglia around Aβ plaques. Microglia isolated from human brains were also able to bind to and ingest Aβ via SCARA-1. Additional evidence that SCARA-1 is an important phagocytic receptor for Aβ comes from studies using microglia from SCARA-1 knock-out mice. SCARA-1 knock-out microglia isolated from these animals showed a 60% decrease in the ability to take up amyloid-β compared with wild-type cells. These results suggest that in addition to SCARA-1, other receptors may be involved in clearance of Aβ by microglia. Since SCARA-1 is involved in clearance of Aβ, from a therapeutic standpoint, it may be beneficial to upregulate expression of this receptor on microglia thereby increasing the ability of these cells to clear Aβ.

Another SCARA that has been shown to interact with Aβ is the macrophage scavenger receptor with collagenous structure (MARCO). MARCO is a SCARA family member but is encoded by a distinct gene from SCARA-1/2. Importantly, MARCO and SCARA1/2 have both common and distinct ligands. MARCO is expressed on cultured neonatal rat microglia and is also a receptor for Aβ. It is not known if MARCO is expressed in microglia in the AD brain. By coimmunoprecipitation, MARCO has been shown to form a complex with formyl peptide-receptor-like 1 (FPRL1) upon encountering Aβ. Intracellular signaling via ERK 1/2 and inhibition of cAMP is then initiated through FPRL1 which may play a part in decreasing the inflammatory response mediated through MARCO in microglia.

5. Class B Scavenger Receptors (SCARB)

SCARB are also important in the innate host response to bacterial and fungal pathogens. The B class receptors are characterized by the presence of membrane-spanning N and C termini and a large extracellular loop (Figure 1). CD36 (SCARB-2), the first classified SCARB was initially identified as a receptor for thrombospondin and for malaria parasitized erythrocytes. Endemann and colleagues subsequently identified CD36 as the “second” modified lipoprotein receptor, the first receptor being SCARA-1/2. By virtue of their ability to bind HDL and act as fatty acid transporters, CD36 and SCARB-1 play major roles in cholesterol metabolism. CD36 also binds and internalizes S. aureus and is required for protection against this pathogen. Recently, we have uncovered a novel role for CD36 as a receptor for β-glucan. We also found that CD36 and its C. elegans ortholog play a major role in host defense to opportunistic infections with pathogenic yeast such as Candida albicans and Cryptococcus neoformans. Interestingly, SCARB-1 act as a coreceptor for the hepatitis C virus and may play a role in viral pathogenesis of hepatitis C. In addition to binding to microbial ligands, CD36 binds several modified “self” antigens including AGE-modified proteins involved in the pathogenesis of vascular complications of diabetes.

5.1. SCARB Role in Alzheimer's Disease

Scavenger receptor B1 (SCARB-1) is a receptor for Aβ on microglia. A study by Husemann et al. proposed that SCARB-1 is developmentally regulated and was not found on microglia in adult human brain and was only expressed on astrocytes. In a mouse model of AD, a reduction in SCARB-1 protein expression increased Aβ plaque deposition had no effect on microglial accumulation around Aβ plaques and in fact worsened cognitive defects in learning and memory.

CD36/SCARB-2 is also expressed on microglia and a receptor for amyloid-β. Intracellular signaling through CD36 is activated upon Aβ binding and activates microglia to produce cytokines and chemokines that induce microglial migration. CD36 knock-out microglia have less Aβ-mediated activation and reduced chemokines and cytokine production compared with wild-type cells. Injection of Aβ into CD36 knock-out mouse brains induced less accumulation of microglia compared with wild-type brains, demonstrating an important role for CD36 in the inflammatory response to Aβ. Microglial CD36 signals upon Aβ engagement via the Src family members Fyn and Lyn and by activation of mitogen-activated protein kinase (MAPK) and subsequent chemokine and ROS production.

Further investigation of the signaling properties of CD36 has recently been shown to be intimately involved with two toll-like receptors TLR-4 and TLR-6. Upon Aβ engagement, CD36 forms a heterodimeric complex with TLR-4 and TLR-6 on microglia resulting in ROS production, and an increase in IL-β mRNA, indicative of inflammasome activation.

From a therapeutic standpoint, it may be advantageous to inhibit the ability of CD36 to signal when bound to Aβ, and thus prevent the release of chemokines and ROS by microglia that are deleterious to the surrounding neurons. We recently undertook a high-content screen to identify small molecule inhibitors of CD36. Screening of an FDA-approved compound library discovered ursolic acid to be an inhibitor of CD36 binding to Aβ. In addition, ursolic acid also inhibited Aβ-mediated ROS production in microglia without effecting microglial ability to phagocytose Aβ.

6. Class C Scavenger Receptors (SCARC)

SCARC-1 was identified in Drosophila but no mammalian ortholog for this receptor has yet been discovered. SCARC-1 is involved in phagocytosis of Gram-negative and Gram-positive bacteria but not yeast. Intriguingly, SCARC-1 also mediates uptake of dsRNA. Since no mammalian ortholog for SCARC has been identified, it remains to be determined if this class of SR plays any role(s) in mammalian physiology or disease pathogenesis.

7. Class D Scavenger Receptors (SCARD)

The class D SRs are characterized by the presence of a mucin-like extracellular domain (Figure 1). The best characterized SCARD is CD68 (also known as macrosialin), which is expressed by macrophages, dendritic cells microglia, and osteoclasts For this reason, CD68 has been used for many years as a histological marker for these cells. It is found mainly intracellularly in late endosomes but cell surface expression increases following activation. CD68/macrosialin plays a minor role in the binding and uptake of oxidized lipoproteins and apoptotic cells by macrophages.

7.1. Role of SCARD in Alzheimer's Disease

Studies investigating a role of SCARD in AD have been mostly descriptive. Immunizing human subjects with AD with Aβ 1–42 caused a reduction in plaques and an upregulation of CD68 expressed on microglia. However in two longer surviving subjects, even though Aβ plaques were cleared, the expression of CD68 was found to be lower than in nonimmunized AD brains. No studies to date investigated whether this class of SRs is mechanistically involved in CNS disorders including AD.

8. Class E Scavenger Receptors (SCARE)

Lectin-like oxidized LDL receptor (LOX-1) was the first scavenger receptor with a C-type lectin-like domain (Figure 1) to be identified. LOX-1 was initially cloned from endothelial cells and appears to play a role in atherosclerosis. LOX-1 is expressed on freshly isolated human monocytes, LOX-1 decreases with monocyte differentiation into macrophages. LOX-1 binds oxidized LDL and has also been implicated in the transport of β-amyloid across the blood brain barrier. In addition, LOX-1 binds gram positive and gram negative bacteria, although its exact role in the innate immune response to these pathogens is unknown. It is not known if LOX-1 is expressed on microglia.

9. Class F Scavenger Receptors-SCARF

SCARFs are characterized by the presence of multiple extracellular epidermal growth factor-like repeats (Figure 1). The first SCARF was identified as an endothelial receptor for modified LDL, termed SREC. In addition to binding modified LDL, SCARFs are receptors for heat shock proteins and calreticulin which is involved in trafficking associated peptides into the major histocompatibility complex class I cross-presentation pathway of antigen-presenting cells. We found that SCARF-1 is expressed on macrophages, and that SCARF-1 plays an important role in binding of the pathogenic yeasts Candida albicans and Cryptococcus neoformans. SCARF appears to be conserved through evolution. CED-1, a C. elegans ortholog of SCARF also appears to play a major role in the innate worm immune response to pathogenic yeast, and CED-1-deficient mutant worms have a dramatic increase in their susceptibility to these infections. Interestingly, CED-1 also binds to cell corpses. Similarly, related families of molecules have been identified in Drosophila melanogaster where they also contribute to host defense.

9.1. Role of SCARF in Alzheimer's Disease

It is not known if SCARF1 is expressed in the brain and/or involved in AD pathogenesis. MEGF10 (multiple EGF-like domains-10), also a member of the SCARF family, has recently been shown to be a receptor for Aβ. MEGF10 is a type 1 transmembrane protein containing 17 EGF-like domains in the extracellular portion (Figure 1). MEGF10 is expressed in the brain of a transgenic mouse model of AD in the hippocampus and cortex region of the brain where Aβ plaques are also found, but it is unknown whether MEGF10 is expressed on microglia.

10.1. RAGE

RAGE (receptor for advanced glycation end products) is a member of the immunoglobulin superfamily of receptors expressed on endothelial cells and microglia which is capable of binding many ligands including Aβ, AGEs (advanced glycation end products) and S100 protein. Ligand binding to RAGE induces many intracellular signaling pathways such as Ras-extracellular signal-regulated kinase 1/2 (ERK1/2), Cdc42/Race stress-activated protein kinase/c-Jun-NH2-terminal kinase (SAPK/JNK), and p38 mitogen-activated protein (MAP) kinase pathways that activate transcription factors, for example, NFκB, cAMP response element-binding (CREB) protein, or (STAT3), a member of the signal transducers and activators of transcription family. RAGE activation through ligand binding induces a positive signaling feedback loop causing sustained activation of NFκB and a chronic state of inflammation.

10.1.1. Role of RAGE in Alzheimer's Disease

RAGE expressed on endothelial cells has previously been shown to play a role transporting Aβ into the brain, and also increasing the diapedesis of monocytes across the blood- brain barrier through RAGE-mediated signaling.

RAGE is expressed in higher levels on neurons and vasculature in AD brains compared with undiseased brains. Soluble Aβ bound to RAGE induces microglial activation and chemotaxis along a concentration gradient, which may lead to microglial accumulation around Aβ plaques..

In a double-transgenic mouse model of AD (both expressing mutated human APP and increased levels of RAGE), Aβ deposition, and microglial activation through NFκB were observed, providing evidence that RAGE also functions as a signaling receptor. Studies using transgenic mice expressing human Aβ and a dominant negative form of RAGE showed microglial RAGE to be an essential signaling receptor, signaling through p38 MAPK and JNK, which leads to synaptic dysfunction through JNK-mediated IL-β release.

However, more recent evidence shows that transgenic mice expressing both the Swedish and Arctic forms of human APP, and deficient in RAGE have a decrease in Aβ deposition and an increase in insulin degrading enzyme (IDE), an enzyme known to cleave Aβ when compared to mice expressing RAGE. Such decrease in Aβ was found at 6 months of age. No improvement in cognitive function or difference in microglial recruitment to plaques was seen in 12 months old mice. This suggests RAGE may not be essential for microglial recruitment but could be involved in Aβ processing in the early disease state.

10.2. CD163

CD163 contains nine scavenger receptor cysteine-rich (SRCR) domains, an ancient and highly conserved protein motif, belonging to the SRCR superfamily. CD163 is expressed on mature tissue macrophages and has previously been shown to be involved in the clearance of hemoglobin-haptoglobin from the circulation. Engagement of macrophage CD163-induced nitric oxide, IL-1β, and TNFα production, suggesting CD163 may be involved in activation of macrophages at sites of inflammation. CD163 is also involved in host defense against both gram-positive and gram-negative bacteria, acting as an immune sensor and mediator of inflammation. In the brains of patients with HIV-associated dementia, CD163 was found to be expressed on microglia, and on perivascular macrophages near the blood-brain barrier, and CD163 is considered a marker for perivascular macrophages. However it is unknown whether CD163 is involved in the pathogenesis of AD.

10.3. SR-PSOX

Scavenger receptor that binds phosphatidylserine and oxidized lipids (SR-PSOX), also known as CXCL16, is a class H SR that can be both a membrane-bound and soluble protein. SR-PSOX is expressed on dendritic cells, and on monocyte-derived macrophages surrounding atherosclerotic plaques but not on smooth muscle cells or endothelial cells. The membrane-bound form is composed of type I transmembrane glycoprotein, consisting of CXC chemokine, mucin stalk, transmembrane, and cytoplasmic domains. Treatment of human peripheral blood mononuclear cells (PBMCs) with IFNγ induced increased uptake of oxLDL and increased levels of SR-PSOX. The soluble form of SR-PSOX has been shown to ligate the T-cell receptor CXCR6 and attracts IFNγ-producing T cells to lymph nodes. It is not known if this receptor binds Aβ or whether it plays a role in AD pathogenesis.

11. SR and Innate Immune Signaling

A common emerging theme is that SRs are not only innate immune recognition and phagocytic receptors but also act as critical regulators of inflammatory signaling and function as sensors for the innate immune response. The mechanism(s) by which SRs regulate the outcome of ligand engagement is currently unknown.

Two potential and not mutually exclusive possibilities exist. First, SRs may facilitate ligand delivery to other PRRs, particularly to the TLRs, which have not been shown to be sufficient for cellular binding to their targets. Pertinent to this, recent work has demonstrated that many TLRs do not interact with their ligands on the cell surface but within intracellular compartments such as endosomes or phagosomes. However, the mechanisms that deliver TLR ligands to the appropriate compartments are poorly defined. One possibility is that ligand delivery is facilitated by coreceptors such as Dectins and SRs. The second scenario is that signals triggered directly from the SRs combine with those from other PRRs to define the ligand-specific response.

Such dichotomous cooperative role of SRs with other PRRs is nicely illustrated by CD36. We have observed that CD36 knockout macrophages and microglia show a decreased response to bacterial and self-ligands including Aβ but expression of CD36 is not by itself sufficient to initiate such responses. CD36 requires the presence of TLRs to mediate the responses to its ligands. This reflects two roles for CD36 which contributes to response by both binding the ligand and also by synergistic and cooperative signaling with other PRRS such as TLRs. This cooperation may define the specificity of the response to a particular ligand. Indeed, we found that CD36/TLR2/6 respond to pathogens whereas CD36/TLR4/6 respond to endogenous ligands such as β-amyloid and oxLDL. These roles for CD36 have been mostly described in vitro. It remains to be determined if such sophisticated ligand-receptor specificity of interaction also occurs in vivo and whether it affects diseases processes such as AD.

12. Diverse Roles of SRs in AD

Promising evidence has shown the diversity of SRs with regards to their functions during the development of AD. SCARA-1 and CD36 play complementary nonredundant roles in the interactions of microglia with Aβ. SCARA-1-Aβ interactions are beneficial and promote phagocytosis and clearance of Aβ, whereas CD36-Aβ interactions are harmful and together with TLR-4 and TLR-6 lead to production of neurotoxins and proinflammatory molecules. This is reminiscent of the role CD36 plays in the interaction between macrophages and oxidized low-density lipoproteins in atherosclerosis. Indeed, we have shown in the past that while SCARA-1 mediates adhesion to oxidized LDL coated surfaces, CD36 mediates macrophage activation by oxidized LDL to produce reactive oxygen species. Such differential roles of SCARA-1 and CD36 may have therapeutic implications for AD. Indeed, because of the role of SCARA-1 in Aβ clearance, drugs that upregulate SCARA-1 expression or functions may be helpful for treatment of AD. In contrast, drugs that block CD36 interactions with Aβ or reduce its surface expression may be helpful to stop or delay progression of AD. Similarly, since RAGE expressed on endothelium facilitates the transport of circulating Aβ from the blood across the blood-brain barrier into the brain, compounds that block Aβ-RAGE interactions may be beneficial. In addition to SCARA-1, CD36 and RAGE, and other SRs such as MARCO, LOX-1, and MEGF-10 are also emerging as receptors that bind Aβ and/or may have a role in the pathogenesis of disease (Figure 2). Dissecting the complex roles of various scavenger receptors in microglia-Aβ interactions, is therefore, important to understand the role of microglia in this disease and has therapeutic implications for treatment of this devastating disorder.

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    Not in our library10.1016/s0002-9440(10)64030-8

  36. 36.

    Chung H, Brazil MI, Irizarry MC, Hyman BT, Maxfield FR. Uptake of fibrillar β-amyloid by microglia isolated from MSR-A (type I and type II) knockout mice. Neuroreport. 2001;12(6):1151-1154.

    Not in our library10.1097/00001756-200105080-00020

  37. 37.

    Mukhopadhyay S, Chen Y, Sankala M, et al. Marco, an innate activation marker of macrophages, is a class A scavenger receptor for neisseria meningitidis. European Journal of Immunology. 2006;36(4):940-949.

    Not in our library10.1002/eji.200535389

  38. 38.

    Hamilton RF, Thakur SA, Mayfair JK, Holian A. Marco mediates silica uptake and toxicity in alveolar macrophages from c57bl/6 mice. The Journal of Biological Chemistry. 2006;281(45):34218-34226.

    Not in our library10.1074/jbc.m605229200

  39. 39.

    Alarcón R, Fuenzalida C, Santibáñez M, von Bernhardi R. Expression of scavenger receptors in glial cells: Comparing the adhesion of astrocytes and microglia from neonatal rats to surface-bound β-amyloid. The Journal of Biological Chemistry. 2005;280(34):30406-30415.

    Not in our library10.1074/jbc.m414686200

  40. 40.

    Brandenburg LO, Konrad M, Wruck CJ, Koch T, Lucius R, Pufe T. Functional and physical interactions between formyl-peptide-receptors and scavenger receptor marco and their involvement in amyloid beta 1-42-induced signal transduction in glial cells. Journal of Neurochemistry. 2010;113(3):749-760.

    Not in our library10.1111/j.1471-4159.2010.06637.x

  41. 41.

    Gruarin P, Thorne RF, Dorahy DJ, Burns GF, Sitia R, Alessio M. CD36 is a ditopic glycoprotein with the n-terminal domain implicated in intracellular transport. Biochemical and Biophysical Research Communications. 2000;275(2):446-454.

    Not in our library10.1006/bbrc.2000.3333

  42. 42.

    Asch AS, Barnwell J, Silverstein RL, Nachman RL. Isolation of the thrombospondin membrane receptor. Journal of Clinical Investigation. 1987;79(4):1054-1061.

    Not in our library10.1172/jci112918

  43. 43.

    Ockenhouse CF, Chulay JD. Plasmodium falciparum sequestration: okm5 antigen (CD36) mediates cytoadherence of parasitized erythrocytes to a myelomonocytic cell line. Journal of Infectious Diseases. 1988;157(3):584-588.

    Not in our library10.1093/infdis/157.3.584

  44. 44.

    Endemann G, Stanton LW, Madden KS, Bryant CM, White RT, Protter AA. CD36 is a receptor for oxidized low density lipoprotein. The Journal of Biological Chemistry. 1993;268(16):11811-11816.

    Not in our library

  45. 45.

    Acton S, Rigotti A, Landschulz KT, Xu S, Hobbs HH, Kriegert M. Identification of scavenger receptor SR-BI as a high density lipoprotein receptor. Science. 1996;271(5248):518-520.

    Not in our library10.1126/science.271.5248.518

  46. 46.

    Abumrad NA, El-Maghrabi MR, Amri EZ, Lopez E, Grimaldi PA. Cloning of a rat adipocyte membrane protein implicated in binding or transport of long-chain fatty acids that is induced during preadipocyte differentiation. homology with human CD36. The Journal of Biological Chemistry. 1993;268(24):17665-17668.

    Not in our library

  47. 47.

    Harmon CM, Abumrad NA. Binding of sulfosuccinimidyl fatty acids to adipocyte membrane proteins: isolation and amino-terminal sequence of an 88-kD protein implicated in transport of long-chain fatty acids. Journal of Membrane Biology. 1993;133(1):43-49.

    Not in our library10.1007/bf00231876

  48. 48.

    Means TK, Mylonakis E, Tampakakis E, et al. Evolutionarily conserved recognition and innate immunity to fungal pathogens by the scavenger receptors scarf1 and CD36. Journal of Experimental Medicine. 2009;206(3):637-653.

    Not in our library10.1084/jem.20082109

  49. 49.

    Scarselli E, Ansuini H, Cerino R, et al. The human scavenger receptor class B type I is a novel candidate receptor for the hepatitis c virus. The EMBO Journal. 2002;21(19):5017-5025.

    Not in our library10.1093/emboj/cdf529

  50. 50.

    Zeisel MB, Koutsoudakis G, Schnober EK, et al. Scavenger receptor class B type I is a key host factor for hepatitis c virus infection required for an entry step closely linked to cd81. Hepatology. 2007;46(6):1722-1731.

    Not in our library10.1002/hep.21994

  51. 51.

    Ohgami N, Nagai R, Ikemoto M, et al. CD36, serves as a receptor for advanced glycation endproducts (AGE). Journal of Diabetes and its Complications. 2002;16(1):56-59.

    Not in our library10.1016/s1056-8727(01)00208-2

  52. 52.

    Husemann J, Loike JD, Kodama T, Silverstein SC. Scavenger receptor class B type I (SR-BI) mediates adhesion of neonatal murine microglia to fibrillar β-amyloid. Journal of Neuroimmunology. 2001;114(1-2):142-150.

    Not in our library10.1016/s0165-5728(01)00239-9

  53. 53.

    Thanopoulou K, Fragkouli A, Stylianopoulou F, Georgopoulos S. Scavenger receptor class B type I (SR-BI) regulates perivascular macrophages and modifies amyloid pathology in an Alzheimer mouse model. Proceedings of the National Academy of Sciences of the United States of America. 2010;107(48):20816-20821.

    Not in our library10.1073/pnas.1005888107

  54. 54.

    El Khoury JB, Moore KJ, Means TK, et al. CD36 mediates the innate host response to β-amyloid. Journal of Experimental Medicine. 2003;197(12):1657-1666.

    Not in our library10.1084/jem.20021546

  55. 55.

    Coraci IS, Husemann J, Berman JW, et al. CD36, a class B scavenger receptor, is expressed on microglia in Alzheimer’s disease brains and can mediate production of reactive oxygen species in response to β-amyloid fibrils. The American Journal of Pathology. 2002;160(1):101-112.

    Not in our library10.1016/s0002-9440(10)64354-4

  56. 56.

    Moore KJ, El Khoury J, Medeiros LA, et al. A CD36-initiated signaling cascade mediates inflammatory effects of β-amyloid. The Journal of Biological Chemistry. 2002;277(49):47373-47379.

    Not in our library10.1074/jbc.m208788200

  57. 57.

    Wilkinson K, Boyd JD, Glicksman M, Moore KJ, El Khoury J. A high content drug screen identifies ursolic acid as an inhibitor of amyloid β protein interactions with its receptor CD36. The Journal of Biological Chemistry. 2011;286(40):34914-34922.

    Not in our library10.1074/jbc.m111.232116

  58. 58.

    Pearson A, Lux A, Krieger M. Expression cloning of dsR-CI, a class C macrophage-specific scavenger receptor from drosophila melanogaster. Proceedings of the National Academy of Sciences of the United States of America. 1995;92(9):4056-4060.

    Not in our library10.1073/pnas.92.9.4056

  59. 59.

    Rämet M, Pearson A, Manfruelli P, et al. Drosophila scavenger receptor CI is a pattern recognition receptor for bacteria. Immunity. 2001;15(6):1027-1038.

    Not in our library10.1016/s1074-7613(01)00249-7

  60. 60.

    Martinez-Pomares L, Platt N, Mcknight AJ, Da Silva RP, Gordon S. Macrophage membrane molecules: markers of tissue differentiation and heterogeneity. Immunobiology. 1996;195(4-5):407-416.

    Not in our library10.1016/s0171-2985(96)80012-x

  61. 61.

    Greaves DR, Gordon S. Macrophage-specific gene expression: current paradigms and future challenges. International Journal of Hematology. 2002;76(1):6-15.

    Not in our library10.1007/bf02982713

  62. 62.

    Gordon S. Macrophage-restricted molecules: role in differentiation and activation. Immunology Letters. 1999;65(1-2):5-8.

    Not in our library10.1016/s0165-2478(98)00116-3

  63. 63.

    Yamada Y, Doi T, Hamakubo T, Kodama T. Scavenger receptor family proteins: roles for atherosclerosis, host defence and disorders of the central nervous system. Cellular and Molecular Life Sciences. 1998;54(7):628-640.

    Not in our library10.1007/s000180050191

  64. 64.

    Argiles A, Mourad G, Kerr PG, Garcia M, Collins B, Demaille JG. Cells surrounding haemodialysis-associated amyloid deposits are mainly macrophages. Nephrology Dialysis Transplantation. 1994;9(6):662-667.

    Not in our library10.1093/ndt/9.6.662

  65. 65.

    Zotova E, Holmes C, Johnston D, Neal JW, Nicoll JAR, Boche D. Microglial alterations in human Alzheimer’s disease following aβ42 immunization. Neuropathology and Applied Neurobiology. 2011;37(5):513-524.

    Not in our library10.1111/j.1365-2990.2010.01156.x

  66. 66.

    Sawamura T, Kume N, Aoyama T, et al. An endothelial receptor for oxidized low-density lipoprotein. Nature. 1997;386(6620):73-77.

    Not in our library10.1038/386073a0

  67. 67.

    Yoshida H, Kondratenko N, Green S, Steinberg D, Quehenberger O. Identification of the lectin-like receptor for oxidized low-density lipoprotein in human macrophages and its potential role as a scavenger receptor. Biochemical Journal. 1998;334(1):9-13.

    Not in our library10.1042/bj3340009

  68. 68.

    Luedecking-Zimmer E, DeKosky ST, Chen Q, Barmada MM, Kamboh MI. Investigation of oxidized IDI-receptor 1 (ORI1) as the candidate gene for Alzheimer’s disease on chromosome 12. Human Genetics. 2002;111(4-5):443-451.

    Not in our library10.1007/s00439-002-0802-7

  69. 69.

    Shi J, Tian J, Pritchard A, et al. A 3′-UTR polymorphism in the oxidized ldl receptor 1 gene increases Aβ40 load as cerebral amyloid angiopathy in Alzheimer’s disease. Acta Neuropathologica. 2006;111(1):15-20.

    Not in our library10.1007/s00401-005-1108-3

  70. 70.

    Shimaoka T, Kume N, Minami M, et al. LOX-1 supports adhesion of gram-positive and gram-negative bacteria. Journal of Immunology. 2001;166(8):5108-5114.

    Not in our library10.4049/jimmunol.166.8.5108

  71. 71.

    Adachi H, Tsujimoto M, Arai H, Inouel K. Expression cloning of a novel scavenger receptor from human endothelial cells. The Journal of Biological Chemistry. 1997;272(50):31217-31220.

    Not in our library10.1074/jbc.272.50.31217

  72. 72.

    Facciponte JG, Wang XY, Subjeck JR. Hsp110 and Grp170, members of the Hsp70 superfamily, bind to scavenger receptor-A and scavenger receptor expressed by endothelial cell-I. European Journal of Immunology. 2007;37(8):2268-2279.

    Not in our library10.1002/eji.200737127

  73. 73.

    Berwin B, Delneste Y, Lovingood RV, Post SR, Pizzo SV. SREC-I, a type F scavenger receptor, is an endocytic receptor for calreticulin. The Journal of Biological Chemistry. 2004;279(49):51250-51257.

    Not in our library10.1074/jbc.m406202200

  74. 74.

    Zhou Z, Hartwieg E, Horvitz HR. CED-1 is a transmembrane receptor that mediates cell corpse engulfment in C. elegans. Cell. 2001;104(1):43-56.

    Not in our library10.1016/s0092-8674(01)00190-8

  75. 75.

    Kocks C, Cho JH, Nehme N, et al. Eater, a transmembrane protein mediating phagocytosis of bacterial pathogens in drosophila. Cell. 2005;123(2):335-346.

    Not in our library10.1016/j.cell.2005.08.034

  76. 76.

    Singh TD, Park SY, Bae JS, et al. Megf10 functions as a receptor for the uptake of amyloid-β. FEBS Letters. 2010;584(18):3936-3942.

    Not in our library10.1016/j.febslet.2010.08.050

  77. 77.

    Suzuki E, Nakayama M. The mammalian CED-1 ortholog MEGF10/KIAA1780 displays a novel adhesion pattern. Experimental Cell Research. 2007;313(11):2451-2464.

    Not in our library10.1016/j.yexcr.2007.03.041

  78. 78.

    Neeper M, Schmidt AM, Brett J, et al. Cloning and expression of a cell surface receptor for advanced glycosylation end products of proteins. The Journal of Biological Chemistry. 1992;267(21):14998-15004.

    Not in our library

  79. 79.

    Brett J, Schmidt AM, Yan SD, et al. Survey of the distribution of a newly characterized receptor for advanced glycation end products in tissues. The American Journal of Pathology. 1993;143(6):1699-1712.

    Not in our library

  80. 80.

    Yan SD, Chen X, Fu J, et al. RAGE and amyloid-β peptide neurotoxicity in Alzheimer’s disease. Nature. 1996;382(6593):685-691.

    Not in our library10.1038/382685a0

  81. 81.

    Leclerc E, Fritz G, Vetter SW, Heizmann CW. Binding of S100 proteins to RAGE: an update. Biochimica Et Biophysica Acta. 2009;1793(6):993-1007.

    Not in our library10.1016/j.bbamcr.2008.11.016

  82. 82.

    Huttunen HJ, Kuja-Panula J, Rauvala H. Receptor for advanced glycation end products (RAGE) signaling induces creb-dependent chromogranin expression during neuronal differentiation. The Journal of Biological Chemistry. 2002;277(41):38635-38646.

    Not in our library10.1074/jbc.m202515200

  83. 83.

    Huttunen HJ, Fages C, Rauvala H. Receptor for advanced glycation end products (RAGE)-mediated neurite outgrowth and activation of NF-κB require the cytoplasmic domain of the receptor but different downstream signaling pathways. The Journal of Biological Chemistry. 1999;274(28):19919-19924.

    Not in our library10.1074/jbc.274.28.19919

  84. 84.

    Taguchi A, Blood DC, Del Toro G, et al. Blockade of RAGE-amphoterin signalling suppresses tumour growth and metastases. Nature. 2000;405(6784):354-360.

    Not in our library10.1038/35012626

  85. 85.

    Shi Du Yan, Schmidt AM, Anderson GM, et al. EnhanCED cellular oxidant stress by the interaction of advanced glycation end products with their receptors/binding proteins. The Journal of Biological Chemistry. 1994;269(13):9889-9897.

    Not in our library

  86. 86.

    Ariyoshi H, Yoshikawa N, Aono Y, et al. Role of receptor for advanced glycation end-product (RAGE) and the JAK/STAT-signaling pathway in AGE-induced collagen production in NRK-49F cells. Journal of Cellular Biochemistry. 2001;81(1):102-113.

    Not in our library10.1002/1097-4644(20010401)81:1<102::aid-jcb1027>3.0.co;2-y

  87. 87.

    Andrassy M, Igwe J, Autschbach F, et al. Posttranslationally modified proteins as mediators of sustained intestinal inflammation. The American Journal of Pathology. 2006;169(4):1223-1237.

    Not in our library10.2353/ajpath.2006.050713

  88. 88.

    Mackic JB, Stins M, McComb JG, et al. Human blood-brain barrier receptors for Alzheimer’s amyloid-β 1-40. asymmetrical binding, endocytosis, and transcytosis at the apical side of brain microvascular endothelial cell monolayer. Journal of Clinical Investigation. 1998;102(4):734-743.

    Not in our library10.1172/jci2029

  89. 89.

    Giri R, Shen Y, Stins M, et al. β-amyloid-induced migration of monocytes across human brain endothelial cells involves RAGE and PECAM-1. American Journal of Physiology. 2000;279(6):C1772-C1781.

    Not in our library10.1152/ajpcell.2000.279.6.c1772

  90. 90.

    Arancio O, Zhang HP, Chen X, et al. RAGE potentiates aβ-induced perturbation of neuronal function in transgenic mice. The EMBO Journal. 2004;23(20):4096-4105.

    Not in our library10.1038/sj.emboj.7600415

  91. 91.

    Arancio O, Zhang HP, Chen X, et al. RAGE potentiates aβ-induced perturbation of neuronal function in transgenic mice. The EMBO Journal. 2004;23(20):4096-4105.

    Not in our library10.1038/sj.emboj.7600415

  92. 92.

    Origlia N, Bonadonna C, Rosellini A, et al. Microglial receptor for advanced glycation end product-dependent signal pathway drives β-amyloid-induced synaptic depression and long-term depression impairment in entorhinal cortex. Journal of Neuroscience. 2010;30(34):11414-11425.

    Not in our library10.1523/jneurosci.2127-10.2010

  93. 93.

    Himeno E, Ohyagi Y, Ma L, et al. Apomorphine treatment in Alzheimer mice promoting amyloid-β degradation. Annals of Neurology. 2011;69(2):248-256.

    Not in our library10.1002/ana.22319

  94. 94.

    Vodopivec I, Galichet A, Knobloch M, Bierhaus A, Heizmann CW, Nitsch RM. RAGE does not affect amyloid pathology in transgenic ArcAβ mice. Neurodegenerative Diseases. 2009;6(5-6):270-280.

    Not in our library10.1159/000261723

  95. 95.

    Fabriek BO, Dijkstra CD, van den Berg TK. The macrophage scavenger receptor CD163. Immunobiology. 2005;210(2-4):153-160.

    Not in our library10.1016/j.imbio.2005.05.010

  96. 96.

    Polfliet MMJ, Fabriek BO, Daniëls WP, Dijkstra CD, van den Berg TK. The rat macrophage scavenger receptor CD163: expression, regulation and role in inflammatory mediator production. Immunobiology. 2006;211(6-8):419-425.

    Not in our library10.1016/j.imbio.2006.05.015

  97. 97.

    Fabriek BO, Bruggen RV, Deng DM, et al. The macrophage scavenger receptor CD163 functions as an innate immune sensor for bacteria. Blood. 2009;113(4):887-892.

    Not in our library10.1182/blood-2008-07-167064

  98. 98.

    Roberts ES, Masliah E, Fox HS. CD163 identifies a unique population of ramified microglia in HIV encephalitis (HIVE). Journal of Neuropathology and Experimental Neurology. 2004;63(12):1255-1264.

    Not in our library10.1093/jnen/63.12.1255

  99. 99.

    Fabriek BO, Van Haastert ES, Galea I, et al. CD163-positive perivascular macrophages in the human cns express molecules for antigen recognition and presentation. Glia. 2005;51(4):297-305.

    Not in our library10.1002/glia.20208

  100. 100.

    Minami M, Kume N, Shimaoka T, et al. Expression of SR-PSOX, a novel cell-surface scavenger receptor for phosphatidylserine and oxidized LDL in human atherosclerotic lesions. Arteriosclerosis, Thrombosis, and Vascular Biology. 2001;21(11):1796-1800.

    Not in our library10.1161/hq1001.096652

  101. 101.

    Shimaoka T, Kume N, Minami M, et al. Molecular cloning of a novel scavenger receptor for oxidized low density lipoprotein, SR-PSOX, on macrophages. The Journal of Biological Chemistry. 2000;275(52):40663-40666.

    Not in our library10.1074/jbc.c000761200

  102. 102.

    Wuttge DM, Zhou X, Sheikine Y, et al. CXCL16/SR-PSOX Is an Interferon-γ-Regulated Chemokine and Scavenger Receptor Expressed in Atherosclerotic Lesions. Arteriosclerosis, Thrombosis, and Vascular Biology. 2004;24(4):750-755.

    Not in our library10.1161/01.atv.0000124102.11472.36

  103. 103.

    Matloubian M, David A, Engel S, Ryan JE, Cyster JG. A transmembrane CXC chemokine is a ligand for HIV-coreceptor bonzo. Nature Immunology. 2000;1(4):298-304.

    Not in our library10.1038/79738

  104. 104.

    Mukhopadhyay S, Herre J, Brown GD, Gordon S. The potential for toll-like receptors to collaborate with other innate immune receptors. Immunology. 2004;112(4):521-530.

    Not in our library10.1111/j.1365-2567.2004.01941.x

  105. 105.

    Underhill DM. Toll-like receptors: networking for success. European Journal of Immunology. 2003;33(7):1767-1775.

    Not in our library10.1002/eji.200324037

  106. 106.

    Gantner BN, Simmons RM, Canavera SJ, Akira S, Underhill DM. Collaborative induction of inflammatory responses by dectin-1 and toll-like receptor 2. Journal of Experimental Medicine. 2003;197(9):1107-1117.

    Not in our library10.1084/jem.20021787

  107. 107.

    Brown GD, Herre J, Williams DL, Willment JA, Marshall ASJ, Gordon S. Dectin-1 mediates the biological effects of β-glucans. Journal of Experimental Medicine. 2003;197(9):1119-1124.

    Not in our library10.1084/jem.20021890

  108. 108.

    Hoebe K, Georgel P, Rutschmann S, et al. CD36 is a sensor of diacylglycerides. Nature. 2005;433(7025):523-527.

    Not in our library10.1038/nature03253

  109. 109.

    Maxeiner H, Husemann J, Thomas CA, Loike JD, El Khoury J, Silverstein SC. Complementary roles for scavenger receptor a and CD36 of human monocyte-derived macrophages in adhesion to surfaces coated with oxidized low-density lipoproteins and in secretion of H2O2. Journal of Experimental Medicine. 1998;188(12):2257-2265.

    Not in our library10.1084/jem.188.12.2257

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