Skip to content
naulon
Get started

No retraction, correction or concern found when last checked on Oct 23, 2026.

Podocytes

Jochen Reiser, Mehmet M. Altintas

F1000Research · 2016 · Review

doi:10.12688/f1000research.7255.1

Abstract

Podocytes are highly specialized cells of the kidney glomerulus that wrap around capillaries and that neighbor cells of the Bowman’s capsule. When it comes to glomerular filtration, podocytes play an active role in preventing plasma proteins from entering the urinary ultrafiltrate by providing a barrier comprising filtration slits between foot processes, which in aggregate represent a dynamic network of cellular extensions. Foot processes interdigitate with foot processes from adjacent podocytes and form a network of narrow and rather uniform gaps. The fenestrated endothelial cells retain blood cells but permit passage of small solutes and an overlying basement membrane less permeable to macromolecules, in particular to albumin. The cytoskeletal dynamics and structural plasticity of podocytes as well as the signaling between each of these distinct layers are essential for an efficient glomerular filtration and thus for proper renal function. The genetic or acquired impairment of podocytes may lead to foot process effacement (podocyte fusion or retraction), a morphological hallmark of proteinuric renal diseases. Here, we briefly discuss aspects of a contemporary view of podocytes in glomerular filtration, the patterns of structural changes in podocytes associated with common glomerular diseases, and the current state of basic and clinical research.

Full text

From PubMed Central, U.S. National Library of Medicine, as current on Oct 23, 2026. Paragraph numbers are ours, so an answer can point at one.

Podocytes and glomerular filtration

Podocytes (or visceral epithelial cells) are terminally differentiated cells lining the outer surface of the glomerular capillaries. As a major component of the ultrafiltration apparatus, podocytes have a complex cellular architecture consisting of cell body, major processes that extend outward from their cell body, forming interdigitated foot processes (FPs) that enwrap the glomerular capillaries. Major processes are tethered by microtubules and intermediate filaments while FPs contain actin-based cytoskeleton –. Podocyte FPs comprise a functioning slit diaphragm (SD) in between,, a meshwork of proteins actively participating in podocyte signaling –. In addition, FPs have a thick, negatively charged coat (glycocalyx) facing the urinary space; this accounts for negative surface charges throughout the glomerular filtration barrier, which generates an electrostatic repel between the neighboring FPs and helps maintain the unique cytoarchitecture of podocytes by enhancing the physical separation. Podocytes form the glomerular filtration barrier together with the opposing monolayers of fenestrated endothelium in the vascular space and glomerular basement membrane (GBM) in between,. This three-layer filtration barrier serves as a size-selective and charge-dependent molecular sieve facilitating the filtration of cationic molecules, electrolytes, and small and midsized solutes but restricting the passage of anionic molecules and macromolecules,. It is important to bear in mind that those layers should be arranged with decreasing selectivity, with the SD being the least selective filter; otherwise, retained plasma proteins would routinely accumulate behind the filtration slits of podocytes. This elegant structure has to oppose hydrostatic pressure in the glomerular capillary, which is the natural driving force behind macromolecular filtration.

If podocytes are injured, mutated, or lost, the elaborate structure of podocytes is physically altered—a process termed ‘foot process effacement’, which is found in many proteinuric kidney diseases. In some cases, once FPs are effaced (flattened down and fused), the glomerular filtration barrier is no longer intact as evidently indicated by the massive leak of proteins out of the vasculature into the urine, known as proteinuria. Proteinuria (also referred to as ‘albuminuria’ or ‘microalbuminuria’) is a clinically important sign of early renal dysfunction. In the following sections, we outline the response of podocytes to various stimuli or injury (or both) to better understand the mechanisms underlying podocyte FP effacement, proteinuria, and glomerular disease progression.

Major causes of podocyte injury

Podocyte function depends on a highly ordered cellular arrangement of filtration compartments and the correct signaling within this microenvironment. Therefore, podocytes are uniquely sensitive to a variety of agents interfering with their actin cytoskeleton, their apical membrane domain (i.e., the negative surface charge), SD complex that regulates podocyte actin reorganization, and GBM structure to which podocytes adhere –. The mechanisms leading to podocytopathies at the molecular level include genetic events (genetic mutations and deletions) associated with common complex diseases,.

The core structural component of podocyte FPs is a highly regulated actin cytoskeletal network, which was represented either by a dense bundle of actin filaments that extends along the length of FPs or by a relatively short and branched cortical network, which is located at the cell periphery and anchors elements of the SD. The initial response of podocytes to injury is the disruption of these structures and actin dysregulation, where actin and actin-binding proteins accumulate.

In experimental models aiming to study various aspects of cell and molecular biology of podocytes, it has been demonstrated that podocytes are the major targets of various soluble and cellular products, including toxins, reactive oxygen species (ROS), complements, and antibodies, as outlined in Table 1.

A commonly used experimental model to induce glomerular proteinuria is puromycin aminonucleoside (PAN) injection into rats. Upon PAN treatment, podocytes undergo significant alterations ranging from FP effacement and cytoskeletal rearrangement to diminished levels of actin cytoskeleton- and SD-associated proteins –. Abnormal distribution of SD proteins and increasing levels of tight junction proteins,, are also reported. Rats develop proteinuria after 4 or 5 days. The early phase of proteinuria is related to the secretion of hyposialylated angiopoietin-like 4 (ANGPTL4) from podocytes, which binds avidly to the GBM and is sensitive to glucocorticoids. Later stages may be mediated by direct oxidative mechanisms. Many pharmacological agents, including dexamethasone,, fluvastatin, erythropoietin analog darbepoetin, mizoribine, sialic acid, and nuclear factor kappa B (NF-κB) inhibitor dehydroxymethylepoxyquinomicin (DHMEQ), have been shown to possess the ability to reverse the reorganized stress fiber and cortical actin fiber phenotype observed after PAN treatment.

Similar structural and functional abnormalities are observed in a rat model of adriamycin (ADR) –. However, podocyte cytoskeleton returns to almost normal appearance by day 20 in PAN-treated rats, whereas pathological and functional changes progress and proteinuria sustains during a similar period of time in ADR-induced nephropathy. Of note, most mouse strains are not susceptible to either of these reagents except BALB/c and BALB/cJ mice, which develop severe proteinuria and progressive renal failure following ADR administration,. Recently, a nuclear DNA repair protein Prkdc (protein kinase, DNA-activated, catalytic peptide) was discovered to participate in the maintenance of the mitochondrial genome and prevent ADR-induced nephropathy. Simvastatin and thiazolidinedione also confer renoprotective phenotype in response to ADR.

Other toxins, which act on podocytes and have been used experimentally, include diphtheria toxin (DT) – secreted by Corynebacterium diphtheria, which causes acute loss of podocytes in inducible diphtheria toxin receptor (iDTR) mice; uremic toxin indoxyl sulfate, which decreases the expression of podocyte differentiation and functional marker proteins; and hemolytic uremic Shiga toxin –, which mediates the release of inflammatory cytokines and vasoactive mediators while potently inhibiting protein synthesis.

These models represent irreversible glomerular damage with major (20% and above in vivo) podocyte depletion, which leads to progressive renal failure. If podocyte loss is less than this threshold, then podocytes have the capacity to recover the normal structure of a healthy glomerulus. Administration of lipopolysaccharides (LPS) is an example of such a reversible model –. LPS trigger podocyte FP effacement and transient proteinuria within 24 hours, which return to baseline after 3 days. Podocytes sense LPS by Toll-like receptor 4 (TLR-4) and this pro-inflammatory response upregulates expression of the co-stimulatory molecule B7-1 and the urokinase-type plasminogen activator receptor (uPAR). LPS also induces the cytosolic variant of cathepsin L (CatL) enzyme, indicating that CatL upregulation in podocytes is associated with the development of proteinuria in mice through a mechanism that involves the cleavage of large GTPase dynamin, synaptopodin, and CD2-associated protein (CD2AP). In a recent study, we reported that the modification of intracellular pH by glutamine uptake was a protective mechanism of cultured mouse podocytes against cytosolic CatL activity, which was markedly elevated under the disease state. Treatment of cultured human podocytes with TLR-3 immunostimulant polyinosinic-polycytidylic acid (polyIC) induces CatL mRNA and simultaneously downregulates podocyte marker protein synaptopodin, suggesting that polyIC may follow an injury pathway similar to that of LPS.

Another means of podocyte injury are subepithelial immune complexes developing as a result of circulating antibodies, which damage or activate podocytes through complement-dependent processes. A number of signaling pathways have been implicated in complement-mediated podocyte injury –, in which sublethal concentrations of complement produce a pronounced but reversible disruption of the actin cytoskeleton and associated focal contacts. Other intracellular events include endoplasmic reticulum (ER) stress, production of ROS, and proteases. Focusing on immunologically induced glomerular injury, podocytes also respond to immunologic processes particularly targeting GBM. Passive administration of heterologous sera containing cross-reacting antibodies against the GBM results in vacuolization of podocytes, focal detachment of podocytes from GBM, and immediate onset of glomerulosclerosis with crescent formation – consistent with a crosstalk between podocytes and the immune system.

Distortion of glomerular charge selectivity by neutralization of the negative charges on podocytes and SDs with polycation protamine sulfate (PS) causes FPs to broaden in vivo, – and stress fibers to disintegrate in vitro in a calcium-dependent manner,. These physiological changes happen within 15 minutes following PS treatment and can be reversed by reperfusion with heparin for another 15 minutes,,. PS is also responsible for the phosphorylation of SD protein nephrin, and focal adhesion complex protein Cas. On the other hand, protamine had little or no effect on the sieving coefficient (also referred to as fractional clearance) of bovine serum albumin once added to neutralize GBM polyanions, a finding that downplays the contribution of GBM to the charge selectivity exhibited by the glomerular filtration barrier. A similar structural alteration can be induced by polycation poly-L-lysine, by removal of the sialic acid,, or by mutation in glucosamine (UDP- N-acetyl)-2-epimerase/ N-acetylmannosamine kinase ( GNE), the rate-limiting enzyme of sialic acid biosynthesis. Patients with mutations in GNE, however, develop the rare muscle disease HIBM (hereditary inclusion body myopathy) and never get kidney disease, highlighting the differences between mice and humans in this pathway in the kidney.

Mutations, abnormalities, or genetic overexpression or deletion in genes encoding podocyte proteins, which are the regulators of actin cytoskeleton such as synaptopodin ( SYNPO) –, α-actinin 4 ( ACTN4) –, dynamin ( DYN),,, aarF domain-containing kinase 4 ( ADCK4), anillin ( ANLN), apolipoprotein L1 ( APOL1), RhoA-activated Rac1 GTPase-activating protein 24 ( ARHGAP24), Rho guanine nucleotide dissociation inhibitor-α ( ARHGDIA) –, claudin-1 ( CLDN1), chloride intracellular channel 5A ( CLIC5A), cofilin-1 ( CFL1),, ezrin ( EZR), inverted formin 2 ( INF2) –, kidney ankyrin repeat-containing protein ( KANK1, KANK2, KANK4), neuronal Wiskott-Aldrich syndrome protein (N-WASP), class II phosphoinositide 3-kinase C2 α ( PI3KC2α), phospholipase C ε1 ( PLCE1), Rho family small GTP-binding protein Rac1 ( RAC1),, rhophilin 1 ( RHPN1), schwannomin interacting protein 1 ( SCHIP1), and WT1-interacting protein ( WTIP), and the ones that are associated with SD complex, including nephrin ( NPHS1) –, podocin ( NPHS2) –, CD2-associated protein ( CD2AP),,,, Nck adaptor protein 1/2 ( NCK1, NCK2),,, transient receptor potential cation channel 6 ( TRPC6) –, cysteine-rich motor neuron 1 ( CRIM1), FAT atypical cadherin 1 ( FAT1), Fyn proto-oncogene ( FYN),,, IQ domain GTPase-activating protein 1 ( IQGAP1),, MAGUK Inverted 2 ( MAGI-2), myosin 1c ( MYO1C), myosin 1e ( MYO1E) –, kin of IRRE like 1 ( NEPH1),, and zonula occludens 1 ( ZO-1), leads to proteinuric diseases owing to the disruption of filtration barrier and rearrangement of actin cytoskeleton.

Likewise, glomerular filtration barrier is impaired if the podocyte apical membrane domain proteins maintaining the negative surface charge are lost or transferred including podocalyxin ( PC),, protein-tyrosine phosphatase receptor o/glomerular epithelial protein 1 ( PTPRO/GLEPP1),, cdc42 ( CDC42),, atypical protein kinase Clambda/iota ( aPKCλ/ι) –, glucosamine uridine diphospho– N-acetylglucosamine-2-epimerase/ N-acetylmannosamine kinase ( GNE), and Van Gogh-like (planar cell polarity) protein 2 ( VANGL2) –. Highlighting the importance of glomerular capillary wall assembly, manipulating or deleting the genes implicated in the adhesion of podocytes to GBM components such as integrin α3 ( ITGA3),, integrin β1 ( ITGB1),, integrin β4 ( ITGB4), CD9 ( CD9), CD151 ( CD151) –, type IV collagen α3/α4/α5 ( COL4A3, COL4A4, COL4A5) –, discoidin domain receptor 1 ( DDR1), glypican 5 ( GPC5), integrin-linked kinase ( ILK),,, laminin β2 ( LAMB2) –, N-deacetylase/N-sulfotransferase ( NDST1), RAP1 GTPase-activating protein ( RAP1GAP), and talin 1 ( TLN1) causes disorganization of podocyte cytoskeletal architecture, leading to deformation in glomerular filtration.

The involvement of lysosome membrane protein 2 ( SCARB2/LIMP2) in the maintenance of podocyte structure and mitochondrial proteins coenzyme Q 2 ( COQ2), coenzyme Q 6 ( COQ6), Mpv17 ( MPV17), mitochondrial tRNA leucine 1 ( MTTL1), and prohibitin ring complex subunit prohibitin-2 ( PHB2) in the redox state of podocyte is reported in genetic studies. Podocyte-specific deletion of autophagy-related 5 ( ATG5), mammalian target of rapamycin ( MTOR), prorenin receptor ( PRR) –, and class III phosphoinositide 3-kinase/vacuolar protein sorting 34 ( PIK3C3/VPS34), disrupts intracellular vesicle trafficking and impairs autophagic flux. Ablation of dendrin ( DDN) improves renal survival in progressive glomerulosclerosis, whereas knockdown of survivin ( BIRC5), a member of the inhibitor of apoptosis protein family, and Yes-associated protein ( YAP),, a downstream target of Hippo kinases, induces podocyte apoptosis. Podocyte-specific knockout mice for vascular endothelial growth factor A ( VEGF-A) demonstrated a key role for VEGF-A signaling for the establishment and maintenance of a normal glomerular filtration barrier as well as mesangial cell survival and differentiation.

A tremendous number of genetic studies were carried out to reveal the biological role of various pathways in podocytes. Regulatory genes, including β-catenin ( CTNNB1), Notch intracellular domain 1 ( ICN1), ILK –, negative factor ( NEF),, Notch’s intracellular domain ( NOTCH-IC), septin ( SEPT7), transforming growth factor-β ( TGF-β), tuberous sclerosis complex 1 ( TSC1), vpr-binding protein ( VPR), and wingless-type MMTV integration site family 1 ( WNT1), are used as genetic switches to turn on (activate) a specific signaling pathway. There are also studies aiming to shut down (repress) a particular pathway targeting the genes such as Akt2 ( AKT2), PINCH-1–binding ankyrin repeat domain of ILK ( ANK), angiotensin II receptor 2 ( AT2), CTNNB1,,, diaphanous interacting protein ( DIP), dickkopf WNT signaling pathway inhibitor 1 ( DKK1),,, insulin-like growth factor-I receptor ( IGF-IR), –, insulin receptor ( INSR),,, NF-κB essential modulator ( NEMO),, Notch-1 ( NOTCH1), Notch-3 ( NOTCH3), 3-phosphoinositide-dependent kinase-1 ( PDK1), rapamycin-sensitive adaptor protein of mTOR ( RAPTOR), and rapamycin-insensitive subunit of mTOR ( RICTOR),, recombining binding protein suppressor of hairless ( RBPSUH), SH2-domain-containing inositol polyphosphate 5-phosphatase 2 ( SHIP2), SMAD family member 2/3 ( SMAD2, SMAD3), and signal transducer and activator of transcription 3 ( STAT3) –.

Currently, there is great interest in research into transcriptional regulation of gene expression patterns during development and differentiation of podocytes. Genetic studies and analysis of mutations in genes encoding transcription factors provide a comprehensive approach in characterizing the functional role of transcription factors. Alterations in c-Maf-inducing protein ( CMIP),, forkhead box C2 ( FOXC2), hypoxia-inducible factor 1 α ( HIF1A) –, Krüppel-like factor 6 ( KLF6), LIM homeobox transcription factor 1 β ( LMX1B) –, v-Maf avian musculoaponeurotic fibrosarcoma oncogene homolog B ( MAFB),, nuclear factor of activated T cells (NFAT),, paired box gene 2 ( PAX2), podocyte-expressed 1/transcription factor 21 ( POD1/TCF21), peroxisome proliferator-activated receptor-α ( PPARA), Snail family zinc finger 1 ( SNAI1),, Wilm’s tumor 1 ( WT-1) –, zinc finger E-box-binding homeobox 2 ( ZEB2), and zinc fingers and homeoboxes 1/2/3 ( ZHX1, ZHX2, and ZHX3) were studied to enforce a particular cell fate by stimulating or suppressing the related genes.

In addition to these molecules, factors, and genes implicating various means of podocyte injury, there are proteins or agents such as angiopoietin-like 3 (ANGPTL3), B7-1 (CD80),, cytosolic CatL –, glucose –, glutamine, insulin, integrin β3 (ITGB3),, tumor necrosis factor-α (TNF-α) –, transient receptor potential cation channel 5/6 (TRPC5 and TRPC6), and uPAR that are involved in the regulation of podocyte cytoskeleton. In some cases, this cytoskeletal disaggregation and the associated activation of certain pathways (including tumor suppressor protein p53 and caspases) lead to podocyte loss ( in vitro) and detachment from GBM ( in vivo). Seminal studies have shown that apoptotic stimuli are mediated by albumin –, aldosterone –, angiopoietin-like3 (ANGPTL3), angiotensin II –, fatty acids –, glucose,,, IGF-binding protein-3 (IGFBP-3), oxidized low-density lipoprotein (LDL), and TGF-β1, –. Angiotensin II and glucose might also induce podocyte autophagic processes as evidenced by the presence of the increased number of autophagosomes and autophagic genes such as LC3-2 and beclin-1. Under specific conditions, podocyte injury leads to a phenotypic conversion, where podocytes lose their epithelial features such as nephrin, P-cadherin, and ZO-1 while acquiring mesenchymal markers such as desmin, fibroblast-specific protein-1 (FSP-1), α-smooth muscle actin (α-SMA), vimentin, type I collagen, and fibronectin. This process is referred to as podocyte’s epithelial-mesenchymal transition (EMT) and is driven in some cases by endothelin-1 (ET-1), ILK, PAN, and TGF-β1. When infected by human immunodeficiency virus 1 (HIV-1) NEF protein, or treated by TNF-α, the podocyte gives a proliferative response marked by the loss of differentiation markers such as synaptopodin, WT-1, and GLEPP-1 and the subsequent expression of the proliferation markers such as podocyte G 1 cyclin, cyclin A, cyclin D1, and Ki-67. There is evidence that non-cytokine-soluble factors such as soluble urokinase-type plasminogen activator receptor (suPAR) cause podocyte FP effacement and proteinuria via a β3 integrin-dependent mechanism but that circulating sialylated ANGPTL4 reduces proteinuria via an endothelial β5 integrin-dependent mechanism. By contrast, podocyte-secreted hypo-sialylated ANGPTL4 causes proteinuria via interactions with the GBM.

Although these complex regulatory mechanisms imply the vulnerability of podocytes, a variety of factors support podocyte differentiation and survival, including activated protein C (APC),, bone morphogenetic protein-7 (BMP7),,, insulin-like growth factor-II (IGF-II), VEGF-A –, and vascular endothelial growth factor C (VEGF-C),.

Podocytes in glomerular disease pathology

Although the podocyte injury is not the only cause of major glomerular diseases, a stable podocyte architecture with interdigitating FPs connected by highly specialized filtration slits is essential for the maintenance and proper function of the glomerular filtration barrier. Both experimental and clinical studies have indicated a pivotal role of podocyte injury in the development and progression of glomerular diseases.

A number of different conditions and health risk factors can result in glomerular disease. Nephrotic syndrome or glomerulonephritis (i.e., malfunction of glomerular filter) may be a direct result of an infection or accumulation of toxic agents in kidneys, or (podocyte- and GBM-associated) genetic defects, or may be due to a secondary insult such as a pre-existing disease occurring in the body –. This represents the conventional approach to classification of glomerular diseases, which generally meets the needs of nephrologists.

The most common cause of primary glomerular disease in adults is focal segmental glomerulosclerosis (FSGS), which is defined by the scarring (sclerosis) of some but not all of the glomeruli (focal) that involves only a section of the affected glomeruli (segmental) by light microscopy of a renal biopsy specimen. In most cases, distinguishing primary (idiopathic) FSGS from the genetic form of FSGS associated with mutations in essential podocyte proteins, or secondary FSGS (linked to a variety of conditions, including viral infections, drug toxicity, or previous glomerular injury) is challenging; however, it has been proven that this heterogeneous lesion results from podocyte injury,,,. Once the integrity of podocyte FPs is lost, podocytes start to detach from underlying GBM at certain sites revealing bare areas of glomerular capillary surface. Later, these bare areas of GBM contact the Bowman’s capsule and form synechia, which represents the earliest committed FSGS lesion. This sequence of pathological events eventually leads to the development of more lesions and progression to glomerulosclerosis. Recurrence of FSGS in renal transplant recipients has given rise to the existence of permeability or circulating factor(s) acting on podocytes as the cause of primary FSGS. To date, a few plasma factors have been proposed but most of these have been found to be non-specific to FSGS serum/plasma. Recently, suPAR was found to be associated with FSGS; for example, two thirds of patients with primary FSGS exhibited high levels of suPAR and those with the highest levels had a greater chance of recurrence after transplantation. In support of this, our group found that higher suPAR levels at baseline are independently associated with faster decline in eGFR and suPAR in plasma can predict risk of developing chronic kidney disease (CKD) in healthy people up to five years before its onset.

Contrary to FSGS, in which podocytes are lost in the areas of sclerosis, minimal change disease (MCD) is a reversible disorder with normal histology and does not cause podocyte depletion. Diffuse effacement of podocyte FPs (accompanied by condensation of the actin-based cytoskeleton but not associated with reduction of any key podocyte-specific protein except podocyte alpha-dystroglycan ) and loss of GBM charge are among the classic features of MCD. All of these changes, and the development of selective proteinuria, are attributed to the secretion from podocytes of a form of ANGPTL4 that lacks sialic acid residues,.

An FSGS-related but morphologically distinct phenotype was observed when podocytes are infected with HIV, or induced by infections, drugs, autoimmune diseases, or organ transplants –. This phenotype is described as collapsing glomerulopathy (CG) and is characterized by extensive loss of mature podocyte markers, severe FP effacement, and focal detachment together with the collapse of the capillary loops. Importantly, podocytes re-enter the cell cycle, become capable of proliferating, and lead to the formation of crescents filling the Bowman’s space, making CG structurally distinct from other forms of FSGS,,. If left untreated, HIV-1-associated nephropathy progresses to end-stage renal disease within weeks to months, whereas the combined antiretroviral therapy, which blocks HIV-1 replication, limits podocyte hyperplasia and hypertrophy and brings podocytes back to differentiation state. Studies using animal models have demonstrated that CG can be ameliorated by using cell-cycle inhibitors or by activating transcription factors involved in podocyte differentiation; however, full recovery from CG is scarce.

The immunoglobulin A (IgA) nephropathy (IgAN), which is the most prevalent primary chronic glomerular disease worldwide, exhibits significant heterogeneity in terms of histopathologic features and clinical outcomes. Emerging data suggest that mesangial deposition of IgA1 immune complexes leads to podocyte necrosis and detachment from the GBM, with the subsequent reduction in nephrin mRNA.

Obesity-related hypertension and diabetes have become epidemic health problems worldwide and major risk factors for the development of CKD. High glucose altered podocyte actin assembly in vitro, high blood glucose (hyperglycemia) induced podocyte apoptosis via the ROS-dependent pathway in obese rodents, and podocyte density and number decreased in patients with obesity-related glomerulopathy.

Targeting podocytes as renal-specific therapy

Human kidney has been considered a terminally differentiated organ with minimal cellular turnover and limited capacity for repair, suggesting that kidney injuries carrying severe consequences have limited treatment options. The goal of clinical nephrologists and renal researchers should be to identify the renal protection mechanism and to develop strategies for the treatment of kidney or various renal compartments of which kidney is composed. Podocytes are probably the most likely candidate cell population to be analyzed on a molecular level since these intricate cells are the most vulnerable component of the glomerular filtration network even during early stages of injury and serve as hallmarks of a state of glomerular disease. Owing to their post-mitotic nature, podocytes have a limited capacity for cell division and do not regenerate in response to injury and loss. This leads to rapid progression of glomerular diseases unless treated. Regardless of the diverse origins of glomerular diseases, podocytes are critical determinants of outcome for all glomerular diseases, which makes podocytes a unique model for monitoring and investigating disease progression.

Therefore, there has been a pronounced shift toward podocyte proteins as therapeutic targets in the last decade. Sialic acid and its precursors show efficacy in MCD and diabetic nephropathy. Mutant forms of human ANGPTL4 reduce proteinuria without causing hypertriglyceridemia in FSGS and diabetic nephropathy,. Calcineurin inhibitor cyclosporine A (CsA) stabilizes of the actin cytoskeleton and stress fibers in podocytes by blocking the calcineurin-mediated phosphorylation and CatL-facilitated degradation of synaptopodin. As mentioned earlier, suPAR, which activates integrin αvβ3 independent of uPAR, has been suggested as an FSGS factor. A specific inhibitor of integrin αvβ3, cyclo-RGDfV, ameliorates proteinuria in mouse models of nephrotic syndrome by directly targeting the upregulated integrin αvβ3 on podocytes. CD20 antibody rituximab binds to sphingomyelin phosphodiesterase acid-like 3b (SMPDL-3b) and stabilizes the structure and function of podocytes treated with the sera of patients with recurrent FSGS. Abatacept blocks the interaction of B7-1 (CD80) with cytoskeletal protein talin and thereby stabilizes β1-integrin activity and prevents podocyte motility. However, these results have been subjected to criticism since uncertainties still remain, preventing us from being too optimistic about the general efficacy of abatacept –. The GTPase dynamin, which promotes endocytosis and regulates actin cytoskeleton,, is induced by small-molecule Bis-T-23 as a potential therapeutic approach. Bis-T-23 effectively promotes dynamin assembly into higher-order structures and increases actin polymerization in injured podocytes.

Molecular analysis of podocytes will lead to a better understanding of disease mechanisms and therefore may enable the identification of targets for early-onset diagnostics and disease treatment. In this context, cell-based high-throughput drug screening assays quantifying the phenotypic changes in podocytes (specifically changes in morphology, F-actin cytoskeleton, focal adhesions, cell volume, and so on) offer great value for the discovery of chemotherapeutic agents. Recently, a podocyte cell-based phenotypic assay was developed and applied to identify novel podocyte-protective small molecules and establish specific drug delivery strategies.

The possibilities of targeting podocytes and thereby affecting kidney disease and progression early in the course set high expectations and hopefully will provide a significant benefit to human health in the future.

References 364

  1. 1.

    Pavenstädt H Kriz W Kretzler M: Cell biology of the glomerular podocyte. Physiol Rev. 2003;83(1):253–307.

    Not in our library10.1152/physrev.00020.2002

  2. 2.

    Andrews PM: Investigations of cytoplasmic contractile and cytoskeletal elements in the kidney glomerulus. Kidney Int. 1981;20(5):549–62.

    Not in our library10.1038/ki.1981.176

  3. 3.

    Kriz W Hackenthal E Nobiling R: A role for podocytes to counteract capillary wall distension. Kidney Int. 1994;45(2):369–76.

    Not in our library10.1038/ki.1994.47

  4. 4.

    Ichimura K Kurihara H Sakai T: Actin filament organization of foot processes in rat podocytes. J Histochem Cytochem. 2003;51(12):1589–600.

    Not in our library10.1177/002215540305101203

  5. 5.

    Reiser J Kriz W Kretzler M: The glomerular slit diaphragm is a modified adherens junction. J Am Soc Nephrol. 2000;11(1):1–8.

    Not in our library10.1681/asn.v1111

  6. 6.

    Fukasawa H Bornheimer S Kudlicka K: Slit diaphragms contain tight junction proteins. J Am Soc Nephrol. 2009;20(7):1491–503.

    Not in our library10.1681/asn.2008101117

  7. 7.

    Huber TB Benzing T: The slit diaphragm: a signaling platform to regulate podocyte function. Curr Opin Nephrol Hypertens. 2005;14(3):211–6.

    Not in our library10.1097/01.mnh.0000165885.85803.a8

  8. 8.

    George B Holzman LB: Signaling from the podocyte intercellular junction to the actin cytoskeleton. Semin Nephrol. 2012;32(4):307–18.

    Not in our library10.1016/j.semnephrol.2012.06.002

  9. 9.

    Grahammer F Schell C Huber TB: The podocyte slit diaphragm--from a thin grey line to a complex signalling hub. Nat Rev Nephrol. 2013;9(10):587–98.

    Not in our library10.1038/nrneph.2013.169

  10. 10.

    Kerjaschki D Sharkey DJ Farquhar MG: Identification and characterization of podocalyxin--the major sialoprotein of the renal glomerular epithelial cell. J Cell Biol. 1984;98(4):1591–6.

    Not in our library10.1083/jcb.98.4.1591

  11. 11.

    Gelberg H Healy L Whiteley H: In vivo enzymatic removal of alpha 2-->6-linked sialic acid from the glomerular filtration barrier results in podocyte charge alteration and glomerular injury. Lab Invest. 1996;74(5):907–20.

    Not in our library

  12. 12.

    Satchell SC Braet F: Glomerular endothelial cell fenestrations: an integral component of the glomerular filtration barrier. Am J Physiol Renal Physiol. 2009;296(5):F947–56.

    Not in our library10.1152/ajprenal.90601.2008

  13. 13.

    Kretzler M: Regulation of adhesive interaction between podocytes and glomerular basement membrane. Microsc Res Tech. 2002;57(4):247–53.

    Not in our library10.1002/jemt.10083

  14. 14.

    Farquhar MG: The glomerular basement membrane: not gone, just forgotten. J Clin Invest. 2006;116(8):2090–3.

    Not in our library10.1172/jci29488

  15. 15.

    Tryggvason K Wartiovaara J: How does the kidney filter plasma? Physiology (Bethesda). 2005;20(2):96–101.

    Not in our library10.1152/physiol.00045.2004

  16. 16.

    Menon MC Chuang PY He CJ: The glomerular filtration barrier: components and crosstalk. Int J Nephrol. 2012;2012: 749010.

    Not in our library10.1155/2012/749010

  17. 17.

    Haraldsson B Nyström J Deen WM: Properties of the glomerular barrier and mechanisms of proteinuria. Physiol Rev. 2008;88(2):451–87.

    Not in our library10.1152/physrev.00055.2006

  18. 18.

    Mundel P Reiser J: Proteinuria: an enzymatic disease of the podocyte? Kidney Int. 2010;77(7):571–80.

    Not in our library10.1038/ki.2009.424

  19. 19.

    Endlich K Kriz W Witzgall R: Update in podocyte biology. Curr Opin Nephrol Hypertens. 2001;10(3):331–40.

    Not in our library10.1097/00041552-200105000-00006

  20. 20.

    Asanuma K Mundel P: The role of podocytes in glomerular pathobiology. Clin Exp Nephrol. 2003;7(4):255–9.

    Not in our library10.1007/s10157-003-0259-6

  21. 21.

    Garg P Holzman LB: Podocytes: gaining a foothold. Exp Cell Res. 2012;318(9):955–63.

    Not in our library10.1016/j.yexcr.2012.02.030

  22. 22.

    Barisoni L Schnaper HW Kopp JB: Advances in the biology and genetics of the podocytopathies: implications for diagnosis and therapy. Arch Pathol Lab Med. 2009;133(2):201–16.

    Not in our library10.1043/1543-2165-133.2.201

  23. 23.

    Bierzynska A Soderquest K Koziell A: Genes and podocytes - new insights into mechanisms of podocytopathy. Front Endocrinol (Lausanne). 2015;5:226.

    Not in our library10.3389/fendo.2014.00226

  24. 24.

    Bertram JF Messina A Ryan GB: In vitro effects of puromycin aminonucleoside on the ultrastructure of rat glomerular podocytes. Cell Tissue Res. 1990;260(3):555–63.

    Not in our library10.1007/bf00297236

  25. 25.

    Whiteside CI Cameron R Munk S: Podocytic cytoskeletal disaggregation and basement-membrane detachment in puromycin aminonucleoside nephrosis. Am J Pathol. 1993;142(5):1641–53.

    Not in our library

  26. 26.

    Kim YH Goyal M Kurnit D: Podocyte depletion and glomerulosclerosis have a direct relationship in the PAN-treated rat. Kidney Int. 2001;60(3):957–68.

    Not in our library10.1046/j.1523-1755.2001.060003957.x

  27. 27.

    Reiser J Oh J Shirato I: Podocyte migration during nephrotic syndrome requires a coordinated interplay between cathepsin L and alpha3 integrin. J Biol Chem. 2004;279(33):34827–32.

    Not in our library10.1074/jbc.m401973200

  28. 28.

    Marshall CB Pippin JW Krofft RD: Puromycin aminonucleoside induces oxidant-dependent DNA damage in podocytes in vitro and in vivo. Kidney Int. 2006;70(11):1962–73.

    Not in our library10.1038/sj.ki.5001965

  29. 29.

    Fukuda H Hidaka T Takagi-Akiba M: Podocin is translocated to cytoplasm in puromycin aminonucleoside nephrosis rats and in poor-prognosis patients with IgA nephropathy. Cell Tissue Res. 2015;360(2):391–400.

    Not in our library10.1007/s00441-014-2100-9

  30. 30.

    Kurihara H Anderson JM Kerjaschki D: The altered glomerular filtration slits seen in puromycin aminonucleoside nephrosis and protamine sulfate-treated rats contain the tight junction protein ZO-1. Am J Pathol. 1992;141(4):805–16.

    Not in our library

  31. 31.

    Zhao L Yaoita E Nameta M: Claudin-6 localized in tight junctions of rat podocytes. Am J Physiol Regul Integr Comp Physiol. 2008;294(6):R1856–62.

    Not in our library10.1152/ajpregu.00862.2007

  32. 32.

    Clement LC Avila-Casado C Macé C: Podocyte-secreted angiopoietin-like-4 mediates proteinuria in glucocorticoid-sensitive nephrotic syndrome. Nat Med. 2011;17(1):117–22.

    Not in our library10.1038/nm.2261

  33. 33.

    Wada T Pippin JW Marshall CB: Dexamethasone prevents podocyte apoptosis induced by puromycin aminonucleoside: role of p53 and Bcl-2-related family proteins. J Am Soc Nephrol. 2005;16(9):2615–25.

    Not in our library10.1681/asn.2005020142

  34. 34.

    Wada T Pippin JW Nangaku M: Dexamethasone's prosurvival benefits in podocytes require extracellular signal-regulated kinase phosphorylation. Nephron Exp Nephrol. 2008;109(1):e8–19.

    Not in our library10.1159/000131892

  35. 35.

    Shibata S Nagase M Fujita T: Fluvastatin ameliorates podocyte injury in proteinuric rats via modulation of excessive Rho signaling. J Am Soc Nephrol. 2006;17(3):754–64.

    Not in our library10.1681/asn.2005050571

  36. 36.

    Eto N Wada T Inagi R: Podocyte protection by darbepoetin: preservation of the cytoskeleton and nephrin expression. Kidney Int. 2007;72(4):455–63.

    Not in our library10.1038/sj.ki.5002311

  37. 37.

    Takeuchi S Hiromura K Tomioka M: The immunosuppressive drug mizoribine directly prevents podocyte injury in puromycin aminonucleoside nephrosis. Nephron Exp Nephrol. 2010;116(1):e3–10.

    Not in our library10.1159/000314668

  38. 38.

    Pawluczyk IZ Najafabadi MG Brown JR: Sialic acid supplementation ameliorates puromycin aminonucleoside nephrosis in rats. Lab Invest. 2015;95(9):1019–28.

    Not in our library10.1038/labinvest.2015.78

  39. 39.

    Shimo T Adachi Y Yamanouchi S: A novel nuclear factor κB inhibitor, dehydroxymethylepoxyquinomicin, ameliorates puromycin aminonucleoside-induced nephrosis in mice. Am J Nephrol. 2013;37(4):302–9.

    Not in our library10.1159/000348803

  40. 40.

    Bertani T Poggi A Pozzoni R: Adriamycin-induced nephrotic syndrome in rats: sequence of pathologic events. Lab Invest. 1982;46(1):16–23.

    Not in our library

  41. 41.

    Okuda S Oh Y Tsuruda H: Adriamycin-induced nephropathy as a model of chronic progressive glomerular disease. Kidney Int. 1986;29(2):502–10.

    Not in our library10.1038/ki.1986.28

  42. 42.

    Rossmann P Matousovic K Bohdanecká M: Experimental adriamycin nephropathy. Fine structure, morphometry, glomerular polyanion, and cell membrane antigens. J Pathol. 1993;169(1):99–108.

    Not in our library10.1002/path.1711690115

  43. 43.

    Wang Y Wang YP Tay YC: Progressive adriamycin nephropathy in mice: sequence of histologic and immunohistochemical events. Kidney Int. 2000;58(4):1797–804.

    Not in our library10.1046/j.1523-1755.2000.00342.x

  44. 44.

    Zoja C Garcia PB Rota C: Mesenchymal stem cell therapy promotes renal repair by limiting glomerular podocyte and progenitor cell dysfunction in adriamycin-induced nephropathy. Am J Physiol Renal Physiol. 2012;303(9):F1370–81.

    Not in our library10.1152/ajprenal.00057.2012

  45. 45.

    Chen A Wei CH Sheu LF: Induction of proteinuria by adriamycin or bovine serum albumin in the mouse. Nephron. 1995;69(3):293–300.

    Not in our library10.1159/000188473

  46. 46.

    Chen A Sheu LF Ho YS: Experimental focal segmental glomerulosclerosis in mice. Nephron. 1998;78(4):440–52.

    Not in our library10.1159/000044974

  47. 47.

    Papeta N Zheng Z Schon EA: Prkdc participates in mitochondrial genome maintenance and prevents Adriamycin-induced nephropathy in mice. J Clin Invest. 2010;120(11):4055–64.

    Not in our library10.1172/jci43721

  48. 48.

    Zhang W Li Q Wang L: Simvastatin ameliorates glomerulosclerosis in Adriamycin-induced-nephropathy rats. Pediatr Nephrol. 2008;23(12):2185–94.

    Not in our library10.1007/s00467-008-0933-8

  49. 49.

    Liu HF Guo LQ Huang YY: Thiazolidinedione attenuate proteinuria and glomerulosclerosis in Adriamycin-induced nephropathy rats via slit diaphragm protection. Nephrology (Carlton). 2010;15(1):75–83.

    Not in our library10.1111/j.1440-1797.2009.01146.x

  50. 50.

    Wharram BL Goyal M Wiggins JE: Podocyte depletion causes glomerulosclerosis: diphtheria toxin-induced podocyte depletion in rats expressing human diphtheria toxin receptor transgene. J Am Soc Nephrol. 2005;16(10):2941–52.

    Not in our library10.1681/asn.2005010055

  51. 51.

    Sato Y Wharram BL Lee SK: Urine podocyte mRNAs mark progression of renal disease. J Am Soc Nephrol. 2009;20(5):1041–52.

    Not in our library10.1681/asn.2007121328

  52. 52.

    Goldwich A Steinkasserer A Gessner A: Impairment of podocyte function by diphtheria toxin--a new reversible proteinuria model in mice. Lab Invest. 2012;92(12):1674–85.

    Not in our library10.1038/labinvest.2012.133

  53. 53.

    Ichii O Otsuka-Kanazawa S Nakamura T: Podocyte injury caused by indoxyl sulfate, a uremic toxin and aryl-hydrocarbon receptor ligand. PLoS One. 2014;9(9):e108448.

    Not in our library10.1371/journal.pone.0108448

  54. 54.

    Hughes AK Stricklett PK Schmid D: Cytotoxic effect of Shiga toxin-1 on human glomerular epithelial cells. Kidney Int. 2000;57(6):2350–9.

    Not in our library10.1046/j.1523-1755.2000.00095.x

  55. 55.

    Morigi M Buelli S Zanchi C: Shigatoxin-induced endothelin-1 expression in cultured podocytes autocrinally mediates actin remodeling. Am J Pathol. 2006;169(6):1965–75.

    Not in our library10.2353/ajpath.2006.051331

  56. 56.

    Locatelli M Buelli S Pezzotta A: Shiga toxin promotes podocyte injury in experimental hemolytic uremic syndrome via activation of the alternative pathway of complement. J Am Soc Nephrol. 2014;25(8):1786–98.

    Not in our library10.1681/asn.2013050450

  57. 57.

    Reiser J von Gersdorff G Loos M: Induction of B7-1 in podocytes is associated with nephrotic syndrome. J Clin Invest. 2004;113(10):1390–7.

    Not in our library10.1172/jci200420402

  58. 58.

    Sun Y He L Takemoto M: Glomerular transcriptome changes associated with lipopolysaccharide-induced proteinuria. Am J Nephrol. 2009;29(6):558–70.

    Not in our library10.1159/000191469

  59. 59.

    Srivastava T Sharma M Yew KH: LPS and PAN-induced podocyte injury in an in vitro model of minimal change disease: changes in TLR profile. J Cell Commun Signal. 2013;7(1):49–60.

    Not in our library10.1007/s12079-012-0184-0

  60. 60.

    Wei C Möller CC Altintas MM: Modification of kidney barrier function by the urokinase receptor. Nat Med. 2008;14(1):55–63.

    Not in our library10.1038/nm1696

  61. 61.

    Sever S Altintas MM Nankoe SR: Proteolytic processing of dynamin by cytoplasmic cathepsin L is a mechanism for proteinuric kidney disease. J Clin Invest. 2007;117(8):2095–104.

    Not in our library10.1172/jci32022

  62. 62.

    Faul C Donnelly M Merscher-Gomez S: The actin cytoskeleton of kidney podocytes is a direct target of the antiproteinuric effect of cyclosporine A. Nat Med. 2008;14(9):931–8.

    Not in our library10.1038/nm.1857

  63. 63.

    Yaddanapudi S Altintas MM Kistler AD: CD2AP in mouse and human podocytes controls a proteolytic program that regulates cytoskeletal structure and cellular survival. J Clin Invest. 2011;121(10):3965–80.

    Not in our library10.1172/jci58552

  64. 64.

    Altintas MM Moriwaki K Wei C: Reduction of proteinuria through podocyte alkalinization. J Biol Chem. 2014;289(25):17454–67.

    Not in our library10.1074/jbc.m114.568998

  65. 65.

    Shimada M Ishimoto T Lee PY: Toll-like receptor 3 ligands induce CD80 expression in human podocytes via an NF-κB-dependent pathway. Nephrol Dial Transplant. 2012;27(1):81–9.

    Not in our library10.1093/ndt/gfr271

  66. 66.

    Cybulsky AV Quigg RJ Salant DJ: Experimental membranous nephropathy redux. Am J Physiol Renal Physiol. 2005;289(4):F660–71.

    Not in our library10.1152/ajprenal.00437.2004

  67. 67.

    Berger SP Daha MR: Complement in glomerular injury. Semin Immunopathol. 2007;29(4):375–84.

    Not in our library10.1007/s00281-007-0090-3

  68. 68.

    Noris M Remuzzi G: Overview of complement activation and regulation. Semin Nephrol. 2013;33(6):479–92.

    Not in our library10.1016/j.semnephrol.2013.08.001

  69. 69.

    Takano T Elimam H Cybulsky AV: Complement-mediated cellular injury. Semin Nephrol. 2013;33(6):586–601.

    Not in our library10.1016/j.semnephrol.2013.08.009

  70. 70.

    Topham PS Haydar SA Kuphal R: Complement-mediated injury reversibly disrupts glomerular epithelial cell actin microfilaments and focal adhesions. Kidney Int. 1999;55(5):1763–75.

    Not in our library10.1046/j.1523-1755.1999.00407.x

  71. 71.

    Le Hir M Haas C Marino M: Prevention of crescentic glomerulonephritis induced by anti-glomerular membrane antibody in tumor necrosis factor-deficient mice. Lab Invest. 1998;78(12):1625–31.

    Not in our library

  72. 72.

    Le Hir M Keller C Eschmann V: Podocyte bridges between the tuft and Bowman's capsule: an early event in experimental crescentic glomerulonephritis. J Am Soc Nephrol. 2001;12(10):2060–71.

    Not in our library10.1681/asn.v12102060

  73. 73.

    Moeller MJ Soofi A Hartmann I: Podocytes populate cellular crescents in a murine model of inflammatory glomerulonephritis. J Am Soc Nephrol. 2004;15(1):61–7.

    Not in our library10.1097/01.asn.0000102468.37809.c6

  74. 74.

    Wheeler J Morley AR Appleton DR: Anti-glomerular basement membrane (GBM) glomerulonephritis in the mouse: development of disease and cell proliferation. J Exp Pathol (Oxford). 1990;71(3):411–22.

    Not in our library

  75. 75.

    Shirato I Hosser H Kimura K: The development of focal segmental glomerulosclerosis in masugi nephritis is based on progressive podocyte damage. Virchows Arch. 1996;429(4–5):255–73.

    Not in our library10.1007/bf00198342

  76. 76.

    Shirato I Sakai T Kimura K: Cytoskeletal changes in podocytes associated with foot process effacement in Masugi nephritis. Am J Pathol. 1996;148(4):1283–96.

    Not in our library

  77. 77.

    Ophascharoensuk V Pippin JW Gordon KL: Role of intrinsic renal cells versus infiltrating cells in glomerular crescent formation. Kidney Int. 1998;54(2):416–25.

    Not in our library10.1046/j.1523-1755.1998.00003.x

  78. 78.

    Kim YG Alpers CE Brugarolas J: The cyclin kinase inhibitor p21 CIP1/WAF1 limits glomerular epithelial cell proliferation in experimental glomerulonephritis. Kidney Int. 1999;55(6):2349–61.

    Not in our library10.1046/j.1523-1755.1999.00504.x

  79. 79.

    Seiler MW Venkatachalam MA Cotran RS: Glomerular epithelium: structural alterations induced by polycations. Science. 1975;189(4200):390–3.

    Not in our library10.1126/science.1145209

  80. 80.

    Kerjaschki D: Polycation-induced dislocation of slit diaphragms and formation of cell junctions in rat kidney glomeruli: the effects of low temperature, divalent cations, colchicine, and cytochalasin B. Lab Invest. 1978;39(5):430–40.

    Not in our library

  81. 81.

    George B Verma R Soofi AA: Crk1/2-dependent signaling is necessary for podocyte foot process spreading in mouse models of glomerular disease. J Clin Invest. 2012;122(2):674–92.

    Not in our library10.1172/jci60070

  82. 82.

    Reiser J Pixley FJ Hug A: Regulation of mouse podocyte process dynamics by protein tyrosine phosphatases rapid communication. Kidney Int. 2000;57(5):2035–42.

    Not in our library10.1046/j.1523-1755.2000.00070.x

  83. 83.

    Rüdiger F Greger R Nitschke R: Polycations induce calcium signaling in glomerular podocytes. Kidney Int. 1999;56(5):1700–9.

    Not in our library10.1046/j.1523-1755.1999.00729.x

  84. 84.

    Schaldecker T Kim S Tarabanis C: Inhibition of the TRPC5 ion channel protects the kidney filter. J Clin Invest. 2013;123(12):5298–309.

    Not in our library10.1172/jci71165

  85. 85.

    Seiler MW Rennke HG Venkatachalam MA: Pathogenesis of polycation-induced alterations ("fusion") of glomerular epithelium. Lab Invest. 1977;36(1):48–61.

    Not in our library

  86. 86.

    Verma R Kovari I Soofi A: Nephrin ectodomain engagement results in Src kinase activation, nephrin phosphorylation, Nck recruitment, and actin polymerization. J Clin Invest. 2006;116(5):1346–59.

    Not in our library10.1172/jci27414

  87. 87.

    Daniels BS: Increased albumin permeability in vitro following alterations of glomerular charge is mediated by the cells of the filtration barrier. J Lab Clin Med. 1994;124(2):224–30.

    Not in our library

  88. 88.

    Andrews PM: Glomerular epithelial alterations resulting from sialic acid surface coat removal. Kidney Int. 1979;15(4):376–85.

    Not in our library10.1038/ki.1979.49

  89. 89.

    Galeano B Klootwijk R Manoli I: Mutation in the key enzyme of sialic acid biosynthesis causes severe glomerular proteinuria and is rescued by N-acetylmannosamine. J Clin Invest. 2007;117(6):1585–94.

    Not in our library10.1172/jci30954

  90. 90.

    Asanuma K Kim K Oh J: Synaptopodin regulates the actin-bundling activity of alpha-actinin in an isoform-specific manner. J Clin Invest. 2005;115(5):1188–98.

    Not in our library10.1172/jci200523371

  91. 91.

    Asanuma K Yanagida-Asanuma E Faul C: Synaptopodin orchestrates actin organization and cell motility via regulation of RhoA signalling. Nat Cell Biol. 2006;8(5):485–91.

    Not in our library10.1038/ncb1400

  92. 92.

    Huber TB Kwoh C Wu H: Bigenic mouse models of focal segmental glomerulosclerosis involving pairwise interaction of CD2AP, Fyn, and synaptopodin. J Clin Invest. 2006;116(5):1337–45.

    Not in our library10.1172/jci27400

  93. 93.

    Kaplan JM Kim SH North KN: Mutations in ACTN4, encoding alpha-actinin-4, cause familial focal segmental glomerulosclerosis. Nat Genet. 2000;24(3):251–6.

    Not in our library10.1038/73456

  94. 94.

    Kos CH Le TC Sinha S: Mice deficient in alpha-actinin-4 have severe glomerular disease. J Clin Invest. 2003;111(11):1683–90.

    Not in our library10.1172/jci200317988

  95. 95.

    Michaud J Lemieux LI Dubé M: Focal and segmental glomerulosclerosis in mice with podocyte-specific expression of mutant alpha-actinin-4. J Am Soc Nephrol. 2003;14(5):1200–11.

    Not in our library10.1097/01.asn.0000059864.88610.5e

  96. 96.

    Michaud JL Chaisson KM Parks RJ: FSGS-associated alpha-actinin-4 (K256E) impairs cytoskeletal dynamics in podocytes. Kidney Int. 2006;70(6):1054–61.

    Not in our library10.1038/sj.ki.5001665

  97. 97.

    Gu C Yaddanapudi S Weins A: Direct dynamin-actin interactions regulate the actin cytoskeleton. EMBO J. 2010;29(21):3593–606.

    Not in our library10.1038/emboj.2010.249

  98. 98.

    Soda K Balkin DM Ferguson SM: Role of dynamin, synaptojanin, and endophilin in podocyte foot processes. J Clin Invest. 2012;122(12):4401–11.

    Not in our library10.1172/jci65289

  99. 99.

    Ashraf S Gee HY Woerner S: ADCK4 mutations promote steroid-resistant nephrotic syndrome through CoQ 10 biosynthesis disruption. J Clin Invest. 2013;123(12):5179–89.

    Not in our library10.1172/jci69000

  100. 100.

    Gbadegesin RA Hall G Adeyemo A: Mutations in the gene that encodes the F-actin binding protein anillin cause FSGS. J Am Soc Nephrol. 2014;25(9):1991–2002.

    Not in our library10.1681/asn.2013090976

  101. 101.

    Lan X Jhaveri A Cheng K: APOL1 risk variants enhance podocyte necrosis through compromising lysosomal membrane permeability. Am J Physiol Renal Physiol. 2014;307(3):F326–36.

    Not in our library10.1152/ajprenal.00647.2013

  102. 102.

    Akilesh S Suleiman H Yu H: Arhgap24 inactivates Rac1 in mouse podocytes, and a mutant form is associated with familial focal segmental glomerulosclerosis. J Clin Invest. 2011;121(10):4127–37.

    Not in our library10.1172/jci46458

  103. 103.

    Togawa A Miyoshi J Ishizaki H: Progressive impairment of kidneys and reproductive organs in mice lacking Rho GDIalpha. Oncogene. 1999;18(39):5373–80.

    Not in our library10.1038/sj.onc.1202921

  104. 104.

    Gee HY Saisawat P Ashraf S: ARHGDIA mutations cause nephrotic syndrome via defective RHO GTPase signaling. J Clin Invest. 2013;123(8):3243–53.

    Not in our library10.1172/jci69134

  105. 105.

    Gupta IR Baldwin C Auguste D: ARHGDIA: a novel gene implicated in nephrotic syndrome. J Med Genet. 2013;50(5):330–8.

    Not in our library10.1136/jmedgenet-2012-101442

  106. 106.

    Hasegawa K Wakino S Simic P: Renal tubular Sirt1 attenuates diabetic albuminuria by epigenetically suppressing Claudin-1 overexpression in podocytes. Nat Med. 2013;19(11):1496–504.

    Not in our library10.1038/nm.3363

  107. 107.

    Wegner B Al-Momany A Kulak SC: CLIC5A, a component of the ezrin-podocalyxin complex in glomeruli, is a determinant of podocyte integrity. Am J Physiol Renal Physiol. 2010;298(6):F1492–503.

    Not in our library10.1152/ajprenal.00030.2010

  108. 108.

    Garg P Verma R Cook L: Actin-depolymerizing factor cofilin-1 is necessary in maintaining mature podocyte architecture. J Biol Chem. 2010;285(29):22676–88.

    Not in our library10.1074/jbc.m110.122929

  109. 109.

    Ashworth S Teng B Kaufeld J: Cofilin-1 inactivation leads to proteinuria--studies in zebrafish, mice and humans. PLoS One. 2010;5(9):e12626.

    Not in our library10.1371/journal.pone.0012626

  110. 110.

    Wasik AA Koskelainen S Hyvönen ME: Ezrin is down-regulated in diabetic kidney glomeruli and regulates actin reorganization and glucose uptake via GLUT1 in cultured podocytes. Am J Pathol. 2014;184(6):1727–39.

    Not in our library10.1016/j.ajpath.2014.03.002

  111. 111.

    Brown EJ Schlöndorff JS Becker DJ: Mutations in the formin gene INF2 cause focal segmental glomerulosclerosis. Nat Genet. 2010;42(1):72–6.

    Not in our library10.1038/ng.505

  112. 112.

    Boyer O Benoit G Gribouval O: Mutations in INF2 are a major cause of autosomal dominant focal segmental glomerulosclerosis. J Am Soc Nephrol. 2011;22(2):239–45.

    Not in our library10.1681/asn.2010050518

  113. 113.

    Barua M Brown EJ Charoonratana VT: Mutations in the INF2 gene account for a significant proportion of familial but not sporadic focal and segmental glomerulosclerosis. Kidney Int. 2013;83(2):316–22.

    Not in our library10.1038/ki.2012.349

  114. 114.

    Sun H Al-Romaih KI MacRae CA: Human Kidney Disease-causing INF2 Mutations Perturb Rho/Dia Signaling in the Glomerulus. EBioMedicine. 2014;1(2–3):107–15.

    Not in our library10.1016/j.ebiom.2014.11.009

  115. 115.

    Gee HY Zhang F Ashraf S: KANK deficiency leads to podocyte dysfunction and nephrotic syndrome. J Clin Invest. 2015;125(6):2375–84.

    Not in our library10.1172/jci79504

  116. 116.

    Schell C Baumhakl L Salou S: N-wasp is required for stabilization of podocyte foot processes. J Am Soc Nephrol. 2013;24(5):713–21.

    Not in our library10.1681/asn.2012080844

  117. 117.

    Harris DP Vogel P Wims M: Requirement for class II phosphoinositide 3-kinase C2alpha in maintenance of glomerular structure and function. Mol Cell Biol. 2011;31(1):63–80.

    Not in our library10.1128/mcb.00468-10

  118. 118.

    Hinkes B Wiggins RC Gbadegesin R: Positional cloning uncovers mutations in PLCE1 responsible for a nephrotic syndrome variant that may be reversible. Nat Genet. 2006;38(12):1397–405.

    Not in our library10.1038/ng1918

  119. 119.

    Blattner SM Hodgin JB Nishio M: Divergent functions of the Rho GTPases Rac1 and Cdc42 in podocyte injury. Kidney Int. 2013;84(5):920–30.

    Not in our library10.1038/ki.2013.175

  120. 120.

    Ishizaka M Gohda T Takagi M: Podocyte-specific deletion of Rac1 leads to aggravation of renal injury in STZ-induced diabetic mice. Biochem Biophys Res Commun. 2015;467(3):549–55.

    Not in our library10.1016/j.bbrc.2015.09.158

  121. 121.

    Lal MA Andersson AC Katayama K: Rhophilin-1 is a key regulator of the podocyte cytoskeleton and is essential for glomerular filtration. J Am Soc Nephrol. 2015;26(3):647–62.

    Not in our library10.1681/asn.2013111195

  122. 122.

    Perisic L Rodriguez PQ Hultenby K: Schip1 is a novel podocyte foot process protein that mediates actin cytoskeleton rearrangements and forms a complex with Nherf2 and ezrin. PLoS One. 2015;10(3):e0122067.

    Not in our library10.1371/journal.pone.0122067

  123. 123.

    Kim JH Mukherjee A Madhavan SM: WT1-interacting protein (Wtip) regulates podocyte phenotype by cell-cell and cell-matrix contact reorganization. Am J Physiol Renal Physiol. 2012;302(1):F103–15.

    Not in our library10.1152/ajprenal.00419.2011

  124. 124.

    Kestilä M Lenkkeri U Männikkö M: Positionally cloned gene for a novel glomerular protein--nephrin--is mutated in congenital nephrotic syndrome. Mol Cell. 1998;1(4):575–82.

    Not in our library10.1016/s1097-2765(00)80057-x

  125. 125.

    Putaala H Soininen R Kilpeläinen P: The murine nephrin gene is specifically expressed in kidney, brain and pancreas: inactivation of the gene leads to massive proteinuria and neonatal death. Hum Mol Genet. 2001;10(1):1–8.

    Not in our library10.1093/hmg/10.1.1

  126. 126.

    Garg P Verma R Nihalani D: Neph1 cooperates with nephrin to transduce a signal that induces actin polymerization. Mol Cell Biol. 2007;27(24):8698–712.

    Not in our library10.1128/mcb.00948-07

  127. 127.

    Boute N Gribouval O Roselli S: NPHS2, encoding the glomerular protein podocin, is mutated in autosomal recessive steroid-resistant nephrotic syndrome. Nat Genet. 2000;24(4):349–54.

    Not in our library10.1038/74166

  128. 128.

    Huber TB Simons M Hartleben B: Molecular basis of the functional podocin-nephrin complex: mutations in the NPHS2 gene disrupt nephrin targeting to lipid raft microdomains. Hum Mol Genet. 2003;12(24):3397–405.

    Not in our library10.1093/hmg/ddg360

  129. 129.

    Roselli S Heidet L Sich M: Early glomerular filtration defect and severe renal disease in podocin-deficient mice. Mol Cell Biol. 2004;24(2):550–60.

    Not in our library10.1128/mcb.24.2.550-560.2004

  130. 130.

    Shih NY Li J Karpitskii V: Congenital nephrotic syndrome in mice lacking CD2-associated protein. Science. 1999;286(5438):312–5.

    Not in our library10.1126/science.286.5438.312

  131. 131.

    Kim JM Wu H Green G: CD2-associated protein haploinsufficiency is linked to glomerular disease susceptibility. Science. 2003;300(5623):1298–300.

    Not in our library10.1126/science.1081068

  132. 132.

    Jones N Blasutig IM Eremina V: Nck adaptor proteins link nephrin to the actin cytoskeleton of kidney podocytes. Nature. 2006;440(7085):818–23.

    Not in our library10.1038/nature04662

  133. 133.

    Jones N New LA Fortino MA: Nck proteins maintain the adult glomerular filtration barrier. J Am Soc Nephrol. 2009;20(7):1533–43.

    Not in our library10.1681/asn.2009010056

  134. 134.

    Hofstra JM Lainez S van Kuijk WH: New TRPC6 gain-of-function mutation in a non-consanguineous Dutch family with late-onset focal segmental glomerulosclerosis. Nephrol Dial Transplant. 2013;28(7):1830–8.

    Not in our library10.1093/ndt/gfs572

  135. 135.

    Reiser J Polu KR Möller CC: TRPC6 is a glomerular slit diaphragm-associated channel required for normal renal function. Nat Genet. 2005;37(7):739–44.

    Not in our library10.1038/ng1592

  136. 136.

    Winn MP Conlon PJ Lynn KL: A mutation in the TRPC6 cation channel causes familial focal segmental glomerulosclerosis. Science. 2005;308(5729):1801–4.

    Not in our library10.1126/science.1106215

  137. 137.

    Möller CC Wei C Altintas MM: Induction of TRPC6 channel in acquired forms of proteinuric kidney disease. J Am Soc Nephrol. 2007;18(1):29–36.

    Not in our library10.1681/asn.2006091010

  138. 138.
    A Novel TRPC6 Mutation That Causes Childhood FSGS · 2009
    No notice
  139. 139.

    Schlöndorff J Del Camino D Carrasquillo R: TRPC6 mutations associated with focal segmental glomerulosclerosis cause constitutive activation of NFAT-dependent transcription. Am J Physiol Cell Physiol. 2009;296(3):C558–69.

    Not in our library10.1152/ajpcell.00077.2008

  140. 140.

    Chiluiza D Krishna S Schumacher VA: Gain-of-function mutations in transient receptor potential C6 (TRPC6) activate extracellular signal-regulated kinases 1/2 (ERK1/2). J Biol Chem. 2013;288(25):18407–20.

    Not in our library10.1074/jbc.m113.463059

  141. 141.

    Kistler AD Singh G Altintas MM: Transient receptor potential channel 6 (TRPC6) protects podocytes during complement-mediated glomerular disease. J Biol Chem. 2013;288(51):36598–609.

    Not in our library10.1074/jbc.m113.488122

  142. 142.

    Nyström J Hultenby K Ek S: CRIM1 is localized to the podocyte filtration slit diaphragm of the adult human kidney. Nephrol Dial Transplant. 2009;24(7):2038–44.

    Not in our library10.1093/ndt/gfn743

  143. 143.

    Ciani L Patel A Allen ND: Mice lacking the giant protocadherin mFAT1 exhibit renal slit junction abnormalities and a partially penetrant cyclopia and anophthalmia phenotype. Mol Cell Biol. 2003;23(10):3575–82.

    Not in our library10.1128/mcb.23.10.3575-3582.2003

  144. 144.

    Yu CC Yen TS Lowell CA: Lupus-like kidney disease in mice deficient in the Src family tyrosine kinases Lyn and Fyn. Curr Biol. 2001;11(1):34–8.

    Not in our library10.1016/s0960-9822(00)00024-5

  145. 145.

    Verma R Wharram B Kovari I: Fyn binds to and phosphorylates the kidney slit diaphragm component Nephrin. J Biol Chem. 2003;278(23):20716–23.

    Not in our library10.1074/jbc.m301689200

  146. 146.

    Rigothier C Auguste P Welsh GI: IQGAP1 interacts with components of the slit diaphragm complex in podocytes and is involved in podocyte migration and permeability in vitro. PLoS One. 2012;7(5):e37695.

    Not in our library10.1371/journal.pone.0037695

  147. 147.

    Liu Y Liang W Yang Y: IQGAP1 regulates actin cytoskeleton organization in podocytes through interaction with nephrin. Cell Signal. 2015;27(4):867–77.

    Not in our library10.1016/j.cellsig.2015.01.015

  148. 148.

    Balbas MD Burgess MR Murali R: MAGI-2 scaffold protein is critical for kidney barrier function. Proc Natl Acad Sci U S A. 2014;111(41):14876–81.

    Not in our library10.1073/pnas.1417297111

  149. 149.

    Arif E Wagner MC Johnstone DB: Motor protein Myo1c is a podocyte protein that facilitates the transport of slit diaphragm protein Neph1 to the podocyte membrane. Mol Cell Biol. 2011;31(10):2134–50.

    Not in our library10.1128/mcb.05051-11

  150. 150.

    Krendel M Kim SV Willinger T: Disruption of Myosin 1e promotes podocyte injury. J Am Soc Nephrol. 2009;20(1):86–94.

    Not in our library10.1681/asn.2007111172

  151. 151.

    Mele C Iatropoulos P Donadelli R: MYO1E mutations and childhood familial focal segmental glomerulosclerosis. N Engl J Med. 2011;365(4):295–306.

    Not in our library10.1056/nejmoa1101273

  152. 152.

    Sanna-Cherchi S Burgess KE Nees SN: Exome sequencing identified MYO1E and NEIL1 as candidate genes for human autosomal recessive steroid-resistant nephrotic syndrome. Kidney Int. 2011;80(4):389–96.

    Not in our library10.1038/ki.2011.148

  153. 153.

    Chase SE Encina CV Stolzenburg LR: Podocyte-specific knockout of myosin 1e disrupts glomerular filtration. Am J Physiol Renal Physiol. 2012;303(7):F1099–106.

    Not in our library10.1152/ajprenal.00251.2012

  154. 154.

    Donoviel DB Freed DD Vogel H: Proteinuria and perinatal lethality in mice lacking NEPH1, a novel protein with homology to NEPHRIN. Mol Cell Biol. 2001;21(14):4829–36.

    Not in our library10.1128/mcb.21.14.4829-4836.2001

  155. 155.

    Itoh M Nakadate K Horibata Y: The structural and functional organization of the podocyte filtration slits is regulated by Tjp1/ZO-1. PLoS One. 2014;9(9):e106621.

    Not in our library10.1371/journal.pone.0106621

  156. 156.

    Doyonnas R Kershaw DB Duhme C: Anuria, omphalocele, and perinatal lethality in mice lacking the CD34-related protein podocalyxin. J Exp Med. 2001;194(1):13–27.

    Not in our library10.1084/jem.194.1.13

  157. 157.

    Fukasawa H Obayashi H Schmieder S: Phosphorylation of podocalyxin (Ser415) Prevents RhoA and ezrin activation and disrupts its interaction with the actin cytoskeleton. Am J Pathol. 2011;179(5):2254–65.

    Not in our library10.1016/j.ajpath.2011.07.046

  158. 158.

    Wharram BL Goyal M Gillespie PJ: Altered podocyte structure in GLEPP1 (Ptpro)-deficient mice associated with hypertension and low glomerular filtration rate. J Clin Invest. 2000;106(10):1281–90.

    Not in our library10.1172/jci7236

  159. 159.

    Ozaltin F Ibsirlioglu T Taskiran EZ: Disruption of PTPRO causes childhood-onset nephrotic syndrome. Am J Hum Genet. 2011;89(1):139–47.

    Not in our library10.1016/j.ajhg.2011.05.026

  160. 160.

    Scott RP Hawley SP Ruston J: Podocyte-specific loss of Cdc42 leads to congenital nephropathy. J Am Soc Nephrol. 2012;23(7):1149–54.

    Not in our library10.1681/asn.2011121206

  161. 161.

    Hirose T Satoh D Kurihara H: An essential role of the universal polarity protein, aPKClambda, on the maintenance of podocyte slit diaphragms. PLoS One. 2009;4(1):e4194.

    Not in our library10.1371/journal.pone.0004194

  162. 162.

    Huber TB Hartleben B Winkelmann K: Loss of podocyte aPKClambda/iota causes polarity defects and nephrotic syndrome. J Am Soc Nephrol. 2009;20(4):798–806.

    Not in our library10.1681/asn.2008080871

  163. 163.

    Satoh D Hirose T Harita Y: aPKCλ maintains the integrity of the glomerular slit diaphragm through trafficking of nephrin to the cell surface. J Biochem. 2014;156(2):115–28.

    Not in our library10.1093/jb/mvu022

  164. 164.

    Babayeva S Zilber Y Torban E: Planar cell polarity pathway regulates actin rearrangement, cell shape, motility, and nephrin distribution in podocytes. Am J Physiol Renal Physiol. 2011;300(2):F549–60.

    Not in our library10.1152/ajprenal.00566.2009

  165. 165.

    Babayeva S Rocque B Aoudjit L: Planar cell polarity pathway regulates nephrin endocytosis in developing podocytes. J Biol Chem. 2013;288(33):24035–48.

    Not in our library10.1074/jbc.m113.452904

  166. 166.

    Rocque BL Babayeva S Li J: Deficiency of the planar cell polarity protein Vangl2 in podocytes affects glomerular morphogenesis and increases susceptibility to injury. J Am Soc Nephrol. 2015;26(3):576–86.

    Not in our library10.1681/asn.2014040340

  167. 167.

    Kreidberg JA Donovan MJ Goldstein SL: Alpha 3 beta 1 integrin has a crucial role in kidney and lung organogenesis. Development. 1996;122(11):3537–47.

    Not in our library10.1242/dev.122.11.3537

  168. 168.

    Kanasaki K Kanda Y Palmsten K: Integrin beta1-mediated matrix assembly and signaling are critical for the normal development and function of the kidney glomerulus. Dev Biol. 2008;313(2):584–93.

    Not in our library10.1016/j.ydbio.2007.10.047

  169. 169.

    Pozzi A Jarad G Moeckel GW: Beta1 integrin expression by podocytes is required to maintain glomerular structural integrity. Dev Biol. 2008;316(2):288–301.

    Not in our library10.1016/j.ydbio.2008.01.022

  170. 170.

    Kambham N Tanji N Seigle RL: Congenital focal segmental glomerulosclerosis associated with beta4 integrin mutation and epidermolysis bullosa. Am J Kidney Dis. 2000;36(1):190–6.

    Not in our library10.1053/ajkd.2000.8293

  171. 171.

    Blumenthal A Giebel J Warsow G: Mechanical stress enhances CD9 expression in cultured podocytes. Am J Physiol Renal Physiol. 2015;308(6):F602–13.

    Not in our library10.1152/ajprenal.00190.2014

  172. 172.

    Karamatic Crew V Burton N Kagan A: CD151, the first member of the tetraspanin (TM4) superfamily detected on erythrocytes, is essential for the correct assembly of human basement membranes in kidney and skin. Blood. 2004;104(8):2217–23.

    Not in our library10.1182/blood-2004-04-1512

  173. 173.

    Sachs N Kreft M van den Bergh Weerman MA: Kidney failure in mice lacking the tetraspanin CD151. J Cell Biol. 2006;175(1):33–9.

    Not in our library10.1083/jcb.200603073

  174. 174.

    Baleato RM Guthrie PL Gubler MC: Deletion of CD151 results in a strain-dependent glomerular disease due to severe alterations of the glomerular basement membrane. Am J Pathol. 2008;173(4):927–37.

    Not in our library10.2353/ajpath.2008.071149

  175. 175.

    Blumenthal A Giebel J Ummanni R: Morphology and migration of podocytes are affected by CD151 levels. Am J Physiol Renal Physiol. 2012;302(10):F1265–77.

    Not in our library10.1152/ajprenal.00468.2011

  176. 176.

    Hudson BG Tryggvason K Sundaramoorthy M: Alport's syndrome, Goodpasture's syndrome, and type IV collagen. N Engl J Med. 2003;348(25):2543–56.

    Not in our library10.1056/nejmra022296

  177. 177.

    Hudson BG: The molecular basis of Goodpasture and Alport syndromes: beacons for the discovery of the collagen IV family. J Am Soc Nephrol. 2004;15(10):2514–27.

    Not in our library10.1097/01.asn.0000141462.00630.76

  178. 178.

    Gubler MC: Inherited diseases of the glomerular basement membrane. Nat Clin Pract Nephrol. 2008;4(1):24–37.

    Not in our library10.1038/ncpneph0671

  179. 179.

    Gross O Beirowski B Harvey SJ: DDR1-deficient mice show localized subepithelial GBM thickening with focal loss of slit diaphragms and proteinuria. Kidney Int. 2004;66(1):102–11.

    Not in our library10.1111/j.1523-1755.2004.00712.x

  180. 180.

    Okamoto K Tokunaga K Doi K: Common variation in GPC5 is associated with acquired nephrotic syndrome. Nat Genet. 2011;43(5):459–63.

    Not in our library10.1038/ng.792

  181. 181.

    Dai C Stolz DB Bastacky SI: Essential role of integrin-linked kinase in podocyte biology: Bridging the integrin and slit diaphragm signaling. J Am Soc Nephrol. 2006;17(8):2164–75.

    Not in our library10.1681/asn.2006010033

  182. 182.

    El-Aouni C Herbach N Blattner SM: Podocyte-specific deletion of integrin-linked kinase results in severe glomerular basement membrane alterations and progressive glomerulosclerosis. J Am Soc Nephrol. 2006;17(5):1334–44.

    Not in our library10.1681/asn.2005090921

  183. 183.

    Noakes PG Miner JH Gautam M: The renal glomerulus of mice lacking s-laminin/laminin beta 2: nephrosis despite molecular compensation by laminin beta 1. Nat Genet. 1995;10(4):400–6.

    Not in our library10.1038/ng0895-400

  184. 184.

    Jarad G Cunningham J Shaw AS: Proteinuria precedes podocyte abnormalities in Lamb2 -/- mice, implicating the glomerular basement membrane as an albumin barrier. J Clin Invest. 2006;116(8):2272–9.

    Not in our library10.1172/jci28414

  185. 185.

    Chen YM Kikkawa Y Miner JH: A missense LAMB2 mutation causes congenital nephrotic syndrome by impairing laminin secretion. J Am Soc Nephrol. 2011;22(5):849–58.

    Not in our library10.1681/asn.2010060632

  186. 186.

    Chen YM Zhou Y Go G: Laminin β2 gene missense mutation produces endoplasmic reticulum stress in podocytes. J Am Soc Nephrol. 2013;24(8):1223–33.

    Not in our library10.1681/asn.2012121149

  187. 187.

    Sugar T Wassenhove-McCarthy DJ Esko JD: Podocyte-specific deletion of NDST1, a key enzyme in the sulfation of heparan sulfate glycosaminoglycans, leads to abnormalities in podocyte organization in vivo. Kidney Int. 2014;85(2):307–18.

    Not in our library10.1038/ki.2013.281

  188. 188.

    Potla U Ni J Vadaparampil J: Podocyte-specific RAP1GAP expression contributes to focal segmental glomerulosclerosis-associated glomerular injury. J Clin Invest. 2014;124(4):1757–69.

    Not in our library10.1172/jci67846

  189. 189.

    Tian X Kim JJ Monkley SM: Podocyte-associated talin1 is critical for glomerular filtration barrier maintenance. J Clin Invest. 2014;124(3):1098–113.

    Not in our library10.1172/jci69778

  190. 190.

    Berkovic SF Dibbens LM Oshlack A: Array-based gene discovery with three unrelated subjects shows SCARB2/LIMP-2 deficiency causes myoclonus epilepsy and glomerulosclerosis. Am J Hum Genet. 2008;82(3):673–84.

    Not in our library10.1016/j.ajhg.2007.12.019

  191. 191.

    Diomedi-Camassei F Di Giandomenico S Santorelli FM: COQ2 nephropathy: a newly described inherited mitochondriopathy with primary renal involvement. J Am Soc Nephrol. 2007;18(10):2773–80.

    Not in our library10.1681/asn.2006080833

  192. 192.

    Heeringa SF Chernin G Chaki M: COQ6 mutations in human patients produce nephrotic syndrome with sensorineural deafness. J Clin Invest. 2011;121(5):2013–24.

    Not in our library10.1172/jci45693

  193. 193.

    Casalena G Krick S Daehn I: Mpv17 in mitochondria protects podocytes against mitochondrial dysfunction and apoptosis in vivo and in vitro. Am J Physiol Renal Physiol. 2014;306(11):F1372–80.

    Not in our library10.1152/ajprenal.00608.2013

  194. 194.

    Löwik MM Hol FA Steenbergen EJ: Mitochondrial tRNA Leu(UUR) mutation in a patient with steroid-resistant nephrotic syndrome and focal segmental glomerulosclerosis. Nephrol Dial Transplant. 2005;20(2):336–41.

    Not in our library10.1093/ndt/gfh546

  195. 195.
    Inhibition of insulin/IGF‐1 receptor signaling protects from mitochondria‐mediated kidney failure · 2015
    Not checked
  196. 196.

    Hartleben B Gödel M Meyer-Schwesinger C: Autophagy influences glomerular disease susceptibility and maintains podocyte homeostasis in aging mice. J Clin Invest. 2010;120(4):1084–96.

    Not in our library10.1172/jci39492

  197. 197.

    Cinà DP Onay T Paltoo A: Inhibition of MTOR disrupts autophagic flux in podocytes. J Am Soc Nephrol. 2012;23(3):412–20.

    Not in our library10.1681/asn.2011070690

  198. 198.

    Riediger F Quack I Qadri F: Prorenin receptor is essential for podocyte autophagy and survival. J Am Soc Nephrol. 2011;22(12):2193–202.

    Not in our library10.1681/asn.2011020200

  199. 199.

    Oshima Y Kinouchi K Ichihara A: Prorenin receptor is essential for normal podocyte structure and function. J Am Soc Nephrol. 2011;22(12):2203–12.

    Not in our library10.1681/asn.2011020202

  200. 200.

    Li C Siragy HM: (Pro)renin receptor regulates autophagy and apoptosis in podocytes exposed to high glucose. Am J Physiol Endocrinol Metab. 2015;309(3):E302–10.

    Not in our library10.1152/ajpendo.00603.2014

  201. 201.

    Chen J Chen MX Fogo AB: mVps34 deletion in podocytes causes glomerulosclerosis by disrupting intracellular vesicle trafficking. J Am Soc Nephrol. 2013;24(2):198–207.

    Not in our library10.1681/asn.2012010101

  202. 202.

    Bechtel W Helmstädter M Balica J: Vps34 deficiency reveals the importance of endocytosis for podocyte homeostasis. J Am Soc Nephrol. 2013;24(5):727–43.

    Not in our library10.1681/asn.2012070700

  203. 203.

    Weins A Wong JS Basgen JM: Dendrin ablation prolongs life span by delaying kidney failure. Am J Pathol. 2015;185(8):2143–57.

    Not in our library10.1016/j.ajpath.2015.04.011

  204. 204.

    Li X Zhang X Li X: The role of survivin in podocyte injury induced by puromycin aminonucleoside. Int J Mol Sci. 2014;15(4):6657–73.

    Not in our library10.3390/ijms15046657

  205. 205.

    Campbell KN Wong JS Gupta R: Yes-associated protein (YAP) promotes cell survival by inhibiting proapoptotic dendrin signaling. J Biol Chem. 2013;288(24):17057–62.

    Not in our library10.1074/jbc.c113.457390

  206. 206.

    Schwartzman M Reginensi A Wong JS: Podocyte-Specific Deletion of Yes-Associated Protein Causes FSGS and Progressive Renal Failure. J Am Soc Nephrol. 2016;27(1):216–26.

    Not in our library10.1681/asn.2014090916

  207. 207.

    Eremina V Sood M Haigh J: Glomerular-specific alterations of VEGF-A expression lead to distinct congenital and acquired renal diseases. J Clin Invest. 2003;111(5):707–16.

    Not in our library10.1172/jci17423

  208. 208.

    Eremina V Cui S Gerber H: Vascular endothelial growth factor a signaling in the podocyte-endothelial compartment is required for mesangial cell migration and survival. J Am Soc Nephrol. 2006;17(3):724–35.

    Not in our library10.1681/asn.2005080810

  209. 209.

    Kato H Gruenwald A Suh JH: Wnt/β-catenin pathway in podocytes integrates cell adhesion, differentiation, and survival. J Biol Chem. 2011;286(29):26003–15.

    Not in our library10.1074/jbc.m111.223164

  210. 210.

    Niranjan T Bielesz B Gruenwald A: The Notch pathway in podocytes plays a role in the development of glomerular disease. Nat Med. 2008;14(3):290–8.

    Not in our library10.1038/nm1731

  211. 211.

    Kretzler M Teixeira VP Unschuld PG: Integrin-linked kinase as a candidate downstream effector in proteinuria. FASEB J. 2001;15(10):1843–5.

    Not in our library10.1096/fj.00-0832fje

  212. 212.

    Teixeira Vde P Blattner SM Li M: Functional consequences of integrin-linked kinase activation in podocyte damage. Kidney Int. 2005;67(2):514–23.

    Not in our library10.1111/j.1523-1755.2005.67108.x

  213. 213.

    Kang YS Li Y Dai C: Inhibition of integrin-linked kinase blocks podocyte epithelial-mesenchymal transition and ameliorates proteinuria. Kidney Int. 2010;78(4):363–73.

    Not in our library10.1038/ki.2010.137

  214. 214.

    He JC Husain M Sunamoto M: Nef stimulates proliferation of glomerular podocytes through activation of Src-dependent Stat3 and MAPK1,2 pathways. J Clin Invest. 2004;114(5):643–51.

    Not in our library10.1172/jci21004

  215. 215.

    Zuo Y Matsusaka T Zhong J: HIV-1 genes vpr and nef synergistically damage podocytes, leading to glomerulosclerosis. J Am Soc Nephrol. 2006;17(10):2832–43.

    Not in our library10.1681/asn.2005080878

  216. 216.

    Waters AM Wu MY Onay T: Ectopic notch activation in developing podocytes causes glomerulosclerosis. J Am Soc Nephrol. 2008;19(6):1139–57.

    Not in our library10.1681/asn.2007050596

  217. 217.

    Wasik AA Polianskyte-Prause Z Dong MQ: Septin 7 forms a complex with CD2AP and nephrin and regulates glucose transporter trafficking. Mol Biol Cell. 2012;23(17):3370–9.

    Not in our library10.1091/mbc.e11-12-1010

  218. 218.

    Schiffer M Bitzer M Roberts IS: Apoptosis in podocytes induced by TGF-beta and Smad7. J Clin Invest. 2001;108(8):807–16.

    Not in our library10.1172/jci12367

  219. 219.

    Inoki K Mori H Wang J: mTORC1 activation in podocytes is a critical step in the development of diabetic nephropathy in mice. J Clin Invest. 2011;121(6):2181–96.

    Not in our library10.1172/jci44771

  220. 220.

    Dai C Stolz DB Kiss LP: Wnt/beta-catenin signaling promotes podocyte dysfunction and albuminuria. J Am Soc Nephrol. 2009;20(9):1997–2008.

    Not in our library10.1681/asn.2009010019

  221. 221.

    Canaud G Bienaimé F Viau A: AKT2 is essential to maintain podocyte viability and function during chronic kidney disease. Nat Med. 2013;19(10):1288–96.

    Not in our library10.1038/nm.3313

  222. 222.

    Yang Y Guo L Blattner SM: Formation and phosphorylation of the PINCH-1-integrin linked kinase-alpha-parvin complex are important for regulation of renal glomerular podocyte adhesion, architecture, and survival. J Am Soc Nephrol. 2005;16(7):1966–76.

    Not in our library10.1681/asn.2004121112

  223. 223.

    Rüster C Franke S Wenzel U: Podocytes of AT2 receptor knockout mice are protected from angiotensin II-mediated RAGE induction. Am J Nephrol. 2011;34(4):309–17.

    Not in our library10.1159/000329321

  224. 224.

    Heikkilä E Juhila J Lassila M: beta-Catenin mediates adriamycin-induced albuminuria and podocyte injury in adult mouse kidneys. Nephrol Dial Transplant. 2010;25(8):2437–46.

    Not in our library10.1093/ndt/gfq076

  225. 225.

    Jiang L Xu L Song Y: Calmodulin-dependent protein kinase II/cAMP response element-binding protein/Wnt/β-catenin signaling cascade regulates angiotensin II-induced podocyte injury and albuminuria. J Biol Chem. 2013;288(32):23368–79.

    Not in our library10.1074/jbc.m113.460394

  226. 226.

    Lu T He JC Wang ZH: HIV-1 Nef disrupts the podocyte actin cytoskeleton by interacting with diaphanous interacting protein. J Biol Chem. 2008;283(13):8173–82.

    Not in our library10.1074/jbc.m708920200

  227. 227.

    Welsh GI Hale LJ Eremina V: Insulin signaling to the glomerular podocyte is critical for normal kidney function. Cell Metab. 2010;12(4):329–40.

    Not in our library10.1016/j.cmet.2010.08.015

  228. 228.

    Hale LJ Welsh GI Perks CM: Insulin-like growth factor-II is produced by, signals to and is an important survival factor for the mature podocyte in man and mouse. J Pathol. 2013;230(1):95–106.

    Not in our library10.1002/path.4165

  229. 229.

    Hale LJ Hurcombe J Lay A: Insulin directly stimulates VEGF-A production in the glomerular podocyte. Am J Physiol Renal Physiol. 2013;305(2):F182–8.

    Not in our library10.1152/ajprenal.00548.2012

  230. 230.

    Brähler S Ising C Hagmann H: Intrinsic proinflammatory signaling in podocytes contributes to podocyte damage and prolonged proteinuria. Am J Physiol Renal Physiol. 2012;303(10):F1473–85.

    Not in our library10.1152/ajprenal.00031.2012

  231. 231.

    Brähler S Ising C Barrera Aranda B: The NF-κB essential modulator (NEMO) controls podocyte cytoskeletal dynamics independently of NF-κB. Am J Physiol Renal Physiol. 2015;309(7):F617–26.

    Not in our library10.1152/ajprenal.00059.2015

  232. 232.

    Lin CL Wang FS Hsu YC: Modulation of notch-1 signaling alleviates vascular endothelial growth factor-mediated diabetic nephropathy. Diabetes. 2010;59(8):1915–25.

    Not in our library10.2337/db09-0663

  233. 233.

    El Machhour F Keuylian Z Kavvadas P: Activation of Notch3 in Glomeruli Promotes the Development of Rapidly Progressive Renal Disease. J Am Soc Nephrol. 2015;26(7):1561–75.

    Not in our library10.1681/asn.2013090968

  234. 234.

    Saurus P Kuusela S Lehtonen E: Podocyte apoptosis is prevented by blocking the Toll-like receptor pathway. Cell Death Dis. 2015;6:e1752.

    Not in our library10.1038/cddis.2015.125

  235. 235.

    Gödel M Hartleben B Herbach N: Role of mTOR in podocyte function and diabetic nephropathy in humans and mice. J Clin Invest. 2011;121(6):2197–209.

    Not in our library10.1172/jci44774

  236. 236.

    Hyvönen ME Saurus P Wasik A: Lipid phosphatase SHIP2 downregulates insulin signalling in podocytes. Mol Cell Endocrinol. 2010;328(1–2):70–9.

    Not in our library10.1016/j.mce.2010.07.016

  237. 237.

    Das R Xu S Quan X: Upregulation of mitochondrial Nox4 mediates TGF-β-induced apoptosis in cultured mouse podocytes. Am J Physiol Renal Physiol. 2014;306(2):F155–67.

    Not in our library10.1152/ajprenal.00438.2013

  238. 238.

    Feng X Lu TC Chuang PY: Reduction of Stat3 activity attenuates HIV-induced kidney injury. J Am Soc Nephrol. 2009;20(10):2138–46.

    Not in our library10.1681/asn.2008080879

  239. 239.

    Dai Y Gu L Yuan W: Podocyte-specific deletion of signal transducer and activator of transcription 3 attenuates nephrotoxic serum-induced glomerulonephritis. Kidney Int. 2013;84(5):950–61.

    Not in our library10.1038/ki.2013.197

  240. 240.

    Abkhezr M Dryer SE: STAT3 regulates steady-state expression of synaptopodin in cultured mouse podocytes. Mol Pharmacol. 2015;87(2):231–9.

    Not in our library10.1124/mol.114.094508

  241. 241.

    Chugh SS: Transcriptional regulation of podocyte disease. Transl Res. 2007;149(5):237–42.

    Not in our library10.1016/j.trsl.2007.01.002

  242. 242.

    Zhang SY Kamal M Dahan K: c-mip impairs podocyte proximal signaling and induces heavy proteinuria. Sci Signal. 2010;3(122):ra39.

    Not in our library10.1126/scisignal.2000678

  243. 243.

    Sendeyo K Audard V Zhang SY: Upregulation of c-mip is closely related to podocyte dysfunction in membranous nephropathy. Kidney Int. 2013;83(3):414–25.

    Not in our library10.1038/ki.2012.426

  244. 244.

    Takemoto M He L Norlin J: Large-scale identification of genes implicated in kidney glomerulus development and function. EMBO J. 2006;25(5):1160–74.

    Not in our library10.1038/sj.emboj.7601014

  245. 245.

    Brukamp K Jim B Moeller MJ: Hypoxia and podocyte-specific Vhlh deletion confer risk of glomerular disease. Am J Physiol Renal Physiol. 2007;293(4):F1397–407.

    Not in our library10.1152/ajprenal.00133.2007

  246. 246.

    Steenhard BM Isom K Stroganova L: Deletion of von Hippel-Lindau in glomerular podocytes results in glomerular basement membrane thickening, ectopic subepithelial deposition of collagen {alpha}1{alpha}2{alpha}1(IV), expression of neuroglobin, and proteinuria. Am J Pathol. 2010;177(1):84–96.

    Not in our library10.2353/ajpath.2010.090767

  247. 247.

    Ding M Cui S Li C: Loss of the tumor suppressor Vhlh leads to upregulation of Cxcr4 and rapidly progressive glomerulonephritis in mice. Nat Med. 2006;12(9):1081–7.

    Not in our library10.1038/nm1460

  248. 248.

    Mallipattu SK Horne SJ D'Agati V: Krüppel-like factor 6 regulates mitochondrial function in the kidney. J Clin Invest. 2015;125(3):1347–61.

    Not in our library10.1172/jci77084

  249. 249.

    Chen H Lun Y Ovchinnikov D: Limb and kidney defects in Lmx1b mutant mice suggest an involvement of LMX1B in human nail patella syndrome. Nat Genet. 1998;19(1):51–5.

    Not in our library10.1038/ng0598-51

  250. 250.

    Morello R Zhou G Dreyer SD: Regulation of glomerular basement membrane collagen expression by LMX1B contributes to renal disease in nail patella syndrome. Nat Genet. 2001;27(2):205–8.

    Not in our library10.1038/84853

  251. 251.

    Miner JH Morello R Andrews KL: Transcriptional induction of slit diaphragm genes by Lmx1b is required in podocyte differentiation. J Clin Invest. 2002;109(8):1065–72.

    Not in our library10.1172/jci13954

  252. 252.

    Rohr C Prestel J Heidet L: The LIM-homeodomain transcription factor Lmx1b plays a crucial role in podocytes. J Clin Invest. 2002;109(8):1073–82.

    Not in our library10.1172/jci13961

  253. 253.

    Suleiman H Heudobler D Raschta AS: The podocyte-specific inactivation of Lmx1b, Ldb1 and E2a yields new insight into a transcriptional network in podocytes. Dev Biol. 2007;304(2):701–12.

    Not in our library10.1016/j.ydbio.2007.01.020

  254. 254.

    Burghardt T Kastner J Suleiman H: LMX1B is essential for the maintenance of differentiated podocytes in adult kidneys. J Am Soc Nephrol. 2013;24(11):1830–48.

    Not in our library10.1681/asn.2012080788

  255. 255.

    Sadl V Jin F Yu J: The mouse Kreisler ( Krml1/MafB) segmentation gene is required for differentiation of glomerular visceral epithelial cells. Dev Biol. 2002;249(1):16–29.

    Not in our library10.1006/dbio.2002.0751

  256. 256.

    Moriguchi T Hamada M Morito N: MafB is essential for renal development and F4/80 expression in macrophages. Mol Cell Biol. 2006;26(15):5715–27.

    Not in our library10.1128/mcb.00001-06

  257. 257.

    Wang Y Jarad G Tripathi P: Activation of NFAT signaling in podocytes causes glomerulosclerosis. J Am Soc Nephrol. 2010;21(10):1657–66.

    Not in our library10.1681/asn.2009121253

  258. 258.

    Nijenhuis T Sloan AJ Hoenderop JG: Angiotensin II contributes to podocyte injury by increasing TRPC6 expression via an NFAT-mediated positive feedback signaling pathway. Am J Pathol. 2011;179(4):1719–32.

    Not in our library10.1016/j.ajpath.2011.06.033

  259. 259.

    Barua M Stellacci E Stella L: Mutations in PAX2 associate with adult-onset FSGS. J Am Soc Nephrol. 2014;25(9):1942–53.

    Not in our library10.1681/asn.2013070686

  260. 260.

    Cui S Li C Ema M: Rapid isolation of glomeruli coupled with gene expression profiling identifies downstream targets in Pod1 knockout mice. J Am Soc Nephrol. 2005;16(11):3247–55.

    Not in our library10.1681/asn.2005030278

  261. 261.

    Zhou Y Kong X Zhao P: Peroxisome proliferator-activated receptor-α is renoprotective in doxorubicin-induced glomerular injury. Kidney Int. 2011;79(12):1302–11.

    Not in our library10.1038/ki.2011.17

  262. 262.

    Matsui I Ito T Kurihara H: Snail, a transcriptional regulator, represses nephrin expression in glomerular epithelial cells of nephrotic rats. Lab Invest. 2007;87(3):273–83.

    Not in our library10.1038/labinvest.3700518

  263. 263.

    Buelli S Rosanò L Gagliardini E: β-arrestin-1 drives endothelin-1-mediated podocyte activation and sustains renal injury. J Am Soc Nephrol. 2014;25(3):523–33.

    Not in our library10.1681/asn.2013040362

  264. 264.

    Ito S Ikeda M Takata A: Nephrotic syndrome and end-stage renal disease with WT1 mutation detected at 3 years. Pediatr Nephrol. 1999;13(9):790–1.

    Not in our library10.1007/s004670050702

  265. 265.

    Guo JK Menke AL Gubler MC: WT1 is a key regulator of podocyte function: reduced expression levels cause crescentic glomerulonephritis and mesangial sclerosis. Hum Mol Genet. 2002;11(6):651–9.

    Not in our library10.1093/hmg/11.6.651

  266. 266.

    Patek CE Fleming S Miles CG: Murine Denys-Drash syndrome: evidence of podocyte de-differentiation and systemic mediation of glomerulosclerosis. Hum Mol Genet. 2003;12(18):2379–94.

    Not in our library10.1093/hmg/ddg240

  267. 267.

    Chau YY Brownstein D Mjoseng H: Acute multiple organ failure in adult mice deleted for the developmental regulator Wt1. PLoS Genet. 2011;7(12):e1002404.

    Not in our library10.1371/journal.pgen.1002404

  268. 268.

    Hall G Gbadegesin RA Lavin P: A novel missense mutation of Wilms' Tumor 1 causes autosomal dominant FSGS. J Am Soc Nephrol. 2015;26(4):831–43.

    Not in our library10.1681/asn.2013101053

  269. 269.

    Kumar PA Kotlyarevska K Dejkhmaron P: Growth hormone (GH)-dependent expression of a natural antisense transcript induces zinc finger E-box-binding homeobox 2 (ZEB2) in the glomerular podocyte: a novel action of gh with implications for the pathogenesis of diabetic nephropathy. J Biol Chem. 2010;285(41):31148–56.

    Not in our library10.1074/jbc.m110.132332

  270. 270.

    Liu G Clement LC Kanwar YS: ZHX proteins regulate podocyte gene expression during the development of nephrotic syndrome. J Biol Chem. 2006;281(51):39681–92.

    Not in our library10.1074/jbc.m606664200

  271. 271.

    Lin Y Rao J Zha XL: Angiopoietin-like 3 induces podocyte F-actin rearrangement through integrin α(V)β₃/FAK/PI3K pathway-mediated Rac1 activation. Biomed Res Int. 2013;2013: 135608.

    Not in our library10.1155/2013/135608

  272. 272.

    Fiorina P Vergani A Bassi R: Role of podocyte B7-1 in diabetic nephropathy. J Am Soc Nephrol. 2014;25(7):1415–29.

    Not in our library10.1681/asn.2013050518

  273. 273.

    Iglesias-de la Cruz MC Ziyadeh FN Isono M: Effects of high glucose and TGF-beta1 on the expression of collagen IV and vascular endothelial growth factor in mouse podocytes. Kidney Int. 2002;62(3):901–13.

    Not in our library10.1046/j.1523-1755.2002.00528.x

  274. 274.

    Han SY Kang YS Jee YH: High glucose and angiotensin II increase beta1 integrin and integrin-linked kinase synthesis in cultured mouse podocytes. Cell Tissue Res. 2006;323(2):321–32.

    Not in our library10.1007/s00441-005-0065-4

  275. 275.

    Ha TS: High glucose and advanced glycosylated end-products affect the expression of alpha-actinin-4 in glomerular epithelial cells. Nephrology (Carlton). 2006;11(5):435–41.

    Not in our library10.1111/j.1440-1797.2006.00668.x

  276. 276.

    Kim NH Rincon-Choles H Bhandari B: Redox dependence of glomerular epithelial cell hypertrophy in response to glucose. Am J Physiol Renal Physiol. 2006;290(3):F741–51.

    Not in our library10.1152/ajprenal.00313.2005

  277. 277.

    De Petris L Hruska KA Chiechio S: Bone morphogenetic protein-7 delays podocyte injury due to high glucose. Nephrol Dial Transplant. 2007;22(12):3442–50.

    Not in our library10.1093/ndt/gfm503

  278. 278.

    Wei C El Hindi S Li J: Circulating urokinase receptor as a cause of focal segmental glomerulosclerosis. Nat Med. 2011;17(8):952–60.

    Not in our library10.1038/nm.2411

  279. 279.

    Koukouritaki SB Vardaki EA Papakonstanti EA: TNF-alpha induces actin cytoskeleton reorganization in glomerular epithelial cells involving tyrosine phosphorylation of paxillin and focal adhesion kinase. Mol Med. 1999;5(6):382–92.

    Not in our library

  280. 280.

    Saito Y Okamura M Nakajima S: Suppression of nephrin expression by TNF-alpha via interfering with the cAMP-retinoic acid receptor pathway. Am J Physiol Renal Physiol. 2010;298(6):F1436–44.

    Not in our library10.1152/ajprenal.00512.2009

  281. 281.

    Bitzan M Babayeva S Vasudevan A: TNFα pathway blockade ameliorates toxic effects of FSGS plasma on podocyte cytoskeleton and β3 integrin activation. Pediatr Nephrol. 2012;27(12):2217–26.

    Not in our library10.1007/s00467-012-2163-3

  282. 282.

    Tian D Jacobo SM Billing D: Antagonistic regulation of actin dynamics and cell motility by TRPC5 and TRPC6 channels. Sci Signal. 2010;3(145):ra77.

    Not in our library10.1126/scisignal.2001200

  283. 283.

    Yoshida S Nagase M Shibata S: Podocyte injury induced by albumin overload in vivo and in vitro: involvement of TGF-beta and p38 MAPK. Nephron Exp Nephrol. 2008;108(3):e57–68.

    Not in our library10.1159/000124236

  284. 284.

    He F Chen S Wang H: Regulation of CD2-associated protein influences podocyte endoplasmic reticulum stress-mediated apoptosis induced by albumin overload. Gene. 2011;484(1–2):18–25.

    Not in our library10.1016/j.gene.2011.05.025

  285. 285.

    Okamura K Dummer P Kopp J: Endocytosis of albumin by podocytes elicits an inflammatory response and induces apoptotic cell death. PLoS One. 2013;8(1):e54817.

    Not in our library10.1371/journal.pone.0054817

  286. 286.

    Shibata S Nagase M Yoshida S: Podocyte as the target for aldosterone: roles of oxidative stress and Sgk1. Hypertension. 2007;49(2):355–64.

    Not in our library10.1161/01.hyp.0000255636.11931.a2

  287. 287.

    Zhu C Huang S Yuan Y: Mitochondrial dysfunction mediates aldosterone-induced podocyte damage: a therapeutic target of PPARγ. Am J Pathol. 2011;178(5):2020–31.

    Not in our library10.1016/j.ajpath.2011.01.029

  288. 288.

    Su M Dhoopun AR Yuan Y: Mitochondrial dysfunction is an early event in aldosterone-induced podocyte injury. Am J Physiol Renal Physiol. 2013;305(4):F520–31.

    Not in our library10.1152/ajprenal.00570.2012

  289. 289.

    Dai R Lin Y Liu H: A vital role for Angptl3 in the PAN-induced podocyte loss by affecting detachment and apoptosis in vitro. BMC Nephrol. 2015;16:38.

    Not in our library10.1186/s12882-015-0034-4

  290. 290.

    Ding G Reddy K Kapasi AA: Angiotensin II induces apoptosis in rat glomerular epithelial cells. Am J Physiol Renal Physiol. 2002;283(1):F173–80.

    Not in our library10.1152/ajprenal.00240.2001

  291. 291.

    Jia J Ding G Zhu J: Angiotensin II infusion induces nephrin expression changes and podocyte apoptosis. Am J Nephrol. 2008;28(3):500–7.

    Not in our library10.1159/000113538

  292. 292.

    Zhang H Ding J Fan Q: TRPC6 up-regulation in Ang II-induced podocyte apoptosis might result from ERK activation and NF-kappaB translocation. Exp Biol Med (Maywood). 2009;234(9):1029–36.

    Not in our library10.3181/0901-rm-11

  293. 293.

    Ren Z Liang W Chen C: Angiotensin II induces nephrin dephosphorylation and podocyte injury: role of caveolin-1. Cell Signal. 2012;24(2):443–50.

    Not in our library10.1016/j.cellsig.2011.09.022

  294. 294.

    Sanchez-Niño MD Sanz AB Sanchez-Lopez E: HSP27/HSPB1 as an adaptive podocyte antiapoptotic protein activated by high glucose and angiotensin II. Lab Invest. 2012;92(1):32–45.

    Not in our library10.1038/labinvest.2011.138

  295. 295.

    Sieber J Lindenmeyer MT Kampe K: Regulation of podocyte survival and endoplasmic reticulum stress by fatty acids. Am J Physiol Renal Physiol. 2010;299(4):F821–9.

    Not in our library10.1152/ajprenal.00196.2010

  296. 296.

    Sieber J Weins A Kampe K: Susceptibility of podocytes to palmitic acid is regulated by stearoyl-CoA desaturases 1 and 2. Am J Pathol. 2013;183(3):735–44.

    Not in our library10.1016/j.ajpath.2013.05.023

  297. 297.

    Kampe K Sieber J Orellana JM: Susceptibility of podocytes to palmitic acid is regulated by fatty acid oxidation and inversely depends on acetyl-CoA carboxylases 1 and 2. Am J Physiol Renal Physiol. 2014;306(4):F401–9.

    Not in our library10.1152/ajprenal.00454.2013

  298. 298.

    Susztak K Raff AC Schiffer M: Glucose-induced reactive oxygen species cause apoptosis of podocytes and podocyte depletion at the onset of diabetic nephropathy. Diabetes. 2006;55(1):225–33.

    Not in our library10.2337/diabetes.55.01.06.db05-0894

  299. 299.

    Peters I Tossidou I Achenbach J: IGF-binding protein-3 modulates TGF-beta/BMP-signaling in glomerular podocytes. J Am Soc Nephrol. 2006;17(6):1644–56.

    Not in our library10.1681/asn.2005111209

  300. 300.

    Bussolati B Deregibus MC Fonsato V: Statins prevent oxidized LDL-induced injury of glomerular podocytes by activating the phosphatidylinositol 3-kinase/AKT-signaling pathway. J Am Soc Nephrol. 2005;16(7):1936–47.

    Not in our library10.1681/asn.2004080629

  301. 301.

    Schiffer M Mundel P Shaw AS: A novel role for the adaptor molecule CD2-associated protein in transforming growth factor-beta-induced apoptosis. J Biol Chem. 2004;279(35):37004–12.

    Not in our library10.1074/jbc.m403534200

  302. 302.

    Wada T Pippin JW Terada Y: The cyclin-dependent kinase inhibitor p21 is required for TGF-beta1-induced podocyte apoptosis. Kidney Int. 2005;68(4):1618–29.

    Not in our library10.1111/j.1523-1755.2005.00574.x

  303. 303.

    Wu DT Bitzer M Ju W: TGF-beta concentration specifies differential signaling profiles of growth arrest/differentiation and apoptosis in podocytes. J Am Soc Nephrol. 2005;16(11):3211–21.

    Not in our library10.1681/asn.2004121055

  304. 304.

    Jung KY Chen K Kretzler M: TGF-beta1 regulates the PINCH-1-integrin-linked kinase-alpha-parvin complex in glomerular cells. J Am Soc Nephrol. 2007;18(1):66–73.

    Not in our library10.1681/asn.2006050421

  305. 305.

    Yadav A Vallabu S Arora S: ANG II promotes autophagy in podocytes. Am J Physiol Cell Physiol. 2010;299(2):C488–96.

    Not in our library10.1152/ajpcell.00424.2009

  306. 306.

    Ma T Zhu J Chen X: High glucose induces autophagy in podocytes. Exp Cell Res. 2013;319(6):779–89.

    Not in our library10.1016/j.yexcr.2013.01.018

  307. 307.

    Liu Y: New insights into epithelial-mesenchymal transition in kidney fibrosis. J Am Soc Nephrol. 2010;21(2):212–22.

    Not in our library10.1681/asn.2008121226

  308. 308.

    Li Y Kang YS Dai C: Epithelial-to-mesenchymal transition is a potential pathway leading to podocyte dysfunction and proteinuria. Am J Pathol. 2008;172(2):299–308.

    Not in our library10.2353/ajpath.2008.070057

  309. 309.

    Husain M Gusella GL Klotman ME: HIV-1 Nef induces proliferation and anchorage-independent growth in podocytes. J Am Soc Nephrol. 2002;13(7):1806–15.

    Not in our library10.1097/01.asn.0000019642.55998.69

  310. 310.

    Sunamoto M Husain M He JC: Critical role for Nef in HIV-1-induced podocyte dedifferentiation. Kidney Int. 2003;64(5):1695–701.

    Not in our library10.1046/j.1523-1755.2003.00283.x

  311. 311.

    Bruggeman LA Drawz PE Kahoud N: TNFR2 interposes the proliferative and NF-κB-mediated inflammatory response by podocytes to TNF-α. Lab Invest. 2011;91(3):413–25.

    Not in our library10.1038/labinvest.2010.199

  312. 312.

    Clement LC Macé C Avila-Casado C: Circulating angiopoietin-like 4 links proteinuria with hypertriglyceridemia in nephrotic syndrome. Nat Med. 2014;20(1):37–46.

    Not in our library10.1038/nm.3396

  313. 313.

    Isermann B Vinnikov IA Madhusudhan T: Activated protein C protects against diabetic nephropathy by inhibiting endothelial and podocyte apoptosis. Nat Med. 2007;13(11):1349–58.

    Not in our library10.1038/nm1667

  314. 314.

    Madhusudhan T Wang H Straub BK: Cytoprotective signaling by activated protein C requires protease-activated receptor-3 in podocytes. Blood. 2012;119(3):874–83.

    Not in our library10.1182/blood-2011-07-365973

  315. 315.

    Mitu GM Wang S Hirschberg R: BMP7 is a podocyte survival factor and rescues podocytes from diabetic injury. Am J Physiol Renal Physiol. 2007;293(5):F1641–8.

    Not in our library10.1152/ajprenal.00179.2007

  316. 316.

    Foster RR Hole R Anderson K: Functional evidence that vascular endothelial growth factor may act as an autocrine factor on human podocytes. Am J Physiol Renal Physiol. 2003;284(6):F1263–73.

    Not in our library10.1152/ajprenal.00276.2002

  317. 317.

    Foster RR Saleem MA Mathieson PW: Vascular endothelial growth factor and nephrin interact and reduce apoptosis in human podocytes. Am J Physiol Renal Physiol. 2005;288(1):F48–57.

    Not in our library10.1152/ajprenal.00146.2004

  318. 318.

    Müller-Deile J Worthmann K Saleem M: The balance of autocrine VEGF-A and VEGF-C determines podocyte survival. Am J Physiol Renal Physiol. 2009;297(6):F1656–67.

    Not in our library10.1152/ajprenal.00275.2009

  319. 319.

    Foster RR Satchell SC Seckley J: VEGF-C promotes survival in podocytes. Am J Physiol Renal Physiol. 2006;291(1):F196–207.

    Not in our library10.1152/ajprenal.00431.2005

  320. 320.

    Barisoni L Schnaper HW Kopp JB: A proposed taxonomy for the podocytopathies: a reassessment of the primary nephrotic diseases. Clin J Am Soc Nephrol. 2007;2(3):529–42.

    Not in our library10.2215/cjn.04121206

  321. 321.

    Chiang C Inagi R: Glomerular diseases: genetic causes and future therapeutics. Nat Rev Nephrol. 2010;6(9):539–54.

    Not in our library10.1038/nrneph.2010.103

  322. 322.

    Smeets B Moeller MJ: Parietal epithelial cells and podocytes in glomerular diseases. Semin Nephrol. 2012;32(4):357–67.

    Not in our library10.1016/j.semnephrol.2012.06.007

  323. 323.

    Pollak MR: The genetic basis of FSGS and steroid-resistant nephrosis. Semin Nephrol. 2003;23(2):141–6.

    Not in our library10.1053/snep.2003.50014

  324. 324.

    Löwik MM Groenen PJ Levtchenko EN: Molecular genetic analysis of podocyte genes in focal segmental glomerulosclerosis--a review. Eur J Pediatr. 2009;168(11):1291–304.

    Not in our library10.1007/s00431-009-1017-x

  325. 325.

    Kuppe C Gröne HJ Ostendorf T: Common histological patterns in glomerular epithelial cells in secondary focal segmental glomerulosclerosis. Kidney Int. 2015;88(5):990–8.

    Not in our library10.1038/ki.2015.116

  326. 326.

    Wiggins RC: The spectrum of podocytopathies: a unifying view of glomerular diseases. Kidney Int. 2007;71(12):1205–14.

    Not in our library10.1038/sj.ki.5002222

  327. 327.

    Fukuda A Chowdhury MA Venkatareddy MP: Growth-dependent podocyte failure causes glomerulosclerosis. J Am Soc Nephrol. 2012;23(8):1351–63.

    Not in our library10.1681/asn.2012030271

  328. 328.

    Kriz W LeHir M: Pathways to nephron loss starting from glomerular diseases-insights from animal models. Kidney Int. 2005;67(2):404–19.

    Not in our library10.1111/j.1523-1755.2005.67097.x

  329. 329.

    Savin VJ Sharma R Sharma M: Circulating factor associated with increased glomerular permeability to albumin in recurrent focal segmental glomerulosclerosis. N Engl J Med. 1996;334(14):878–83.

    Not in our library10.1056/nejm199604043341402

  330. 330.

    McCarthy ET Sharma M Savin VJ: Circulating permeability factors in idiopathic nephrotic syndrome and focal segmental glomerulosclerosis. Clin J Am Soc Nephrol. 2010;5(11):2115–21.

    Not in our library10.2215/cjn.03800609

  331. 331.

    Bose B Cattran D: Glomerular diseases: FSGS. Clin J Am Soc Nephrol. 2014;9(3):626–32.

    Not in our library10.2215/cjn.05810513

  332. 332.

    Hayek SS Sever S Ko YA: Soluble Urokinase Receptor and Chronic Kidney Disease. N Engl J Med. 2015;373(20):1916–25.

    Not in our library10.1056/nejmoa1506362

  333. 333.

    Regele HM Fillipovic E Langer B: Glomerular expression of dystroglycans is reduced in minimal change nephrosis but not in focal segmental glomerulosclerosis. J Am Soc Nephrol. 2000;11(3):403–12.

    Not in our library10.1681/asn.v113403

  334. 334.

    Chugh SS Clement LC Macé C: New insights into human minimal change disease: lessons from animal models. Am J Kidney Dis. 2012;59(2):284–92.

    Not in our library10.1053/j.ajkd.2011.07.024

  335. 335.

    Yang Y Gubler M Beaufils H: Dysregulation of podocyte phenotype in idiopathic collapsing glomerulopathy and HIV-associated nephropathy. Nephron. 2002;91(3):416–23.

    Not in our library10.1159/000064281

  336. 336.

    Medapalli RK He JC Klotman PE: HIV-associated nephropathy: pathogenesis. Curr Opin Nephrol Hypertens. 2011;20(3):306–11.

    Not in our library10.1097/mnh.0b013e328345359a

  337. 337.

    Laurinavicius A Rennke HG: Collapsing glomerulopathy--a new pattern of renal injury. Semin Diagn Pathol. 2002;19(3):106–15.

    Not in our library

  338. 338.

    Barri YM Munshi NC Sukumalchantra S: Podocyte injury associated glomerulopathies induced by pamidronate. Kidney Int. 2004;65(2):634–41.

    Not in our library10.1111/j.1523-1755.2004.00426.x

  339. 339.

    Albaqumi M Soos TJ Barisoni L: Collapsing glomerulopathy. J Am Soc Nephrol. 2006;17(10):2854–63.

    Not in our library10.1681/asn.2006030225

  340. 340.

    Detwiler RK Falk RJ Hogan SL: Collapsing glomerulopathy: a clinically and pathologically distinct variant of focal segmental glomerulosclerosis. Kidney Int. 1994;45(5):1416–24.

    Not in our library10.1038/ki.1994.185

  341. 341.

    Atta MG Gallant JE Rahman MH: Antiretroviral therapy in the treatment of HIV-associated nephropathy. Nephrol Dial Transplant. 2006;21(10):2809–13.

    Not in our library10.1093/ndt/gfl337

  342. 342.

    Gherardi D D'Agati V Chu TH: Reversal of collapsing glomerulopathy in mice with the cyclin-dependent kinase inhibitor CYC202. J Am Soc Nephrol. 2004;15(5):1212–22.

    Not in our library10.1097/01.asn.0000124672.41036.f4

  343. 343.

    Vaughan MR Pippin JW Griffin SV: ATRA induces podocyte differentiation and alters nephrin and podocin expression in vitro and in vivo. Kidney Int. 2005;68(1):133–44.

    Not in our library10.1111/j.1523-1755.2005.00387.x

  344. 344.

    Albaqumi M Barisoni L: Current views on collapsing glomerulopathy. J Am Soc Nephrol. 2008;19(7):1276–81.

    Not in our library10.1681/asn.2007080926

  345. 345.

    D'Amico G: The commonest glomerulonephritis in the world: IgA nephropathy. Q J Med. 1987;64(245):709–27.

    Not in our library

  346. 346.

    Wyatt RJ Julian BA: IgA nephropathy. N Engl J Med. 2013;368(25):2402–14.

    Not in our library10.1056/nejmra1206793

  347. 347.

    Lemley KV Lafayette RA Safai M: Podocytopenia and disease severity in IgA nephropathy. Kidney Int. 2002;61(4):1475–85.

    Not in our library10.1046/j.1523-1755.2002.00269.x

  348. 348.

    Lai KN Leung JC Chan LY: Activation of podocytes by mesangial-derived TNF-alpha: glomerulo-podocytic communication in IgA nephropathy. Am J Physiol Renal Physiol. 2008;294(4):F945–55.

    Not in our library10.1152/ajprenal.00423.2007

  349. 349.

    Gagliardini E Benigni A Tomasoni S: Targeted downregulation of extracellular nephrin in human IgA nephropathy. Am J Nephrol. 2003;23(4):277–86.

    Not in our library10.1159/000072281

  350. 350.

    Kramer H: Obesity and chronic kidney disease. Contrib Nephrol. 2006;151:1–18.

    Not in our library10.1159/000095315

  351. 351.

    Zhou X Hurst RD Templeton D: High glucose alters actin assembly in glomerular mesangial and epithelial cells. Lab Invest. 1995;73(3):372–83.

    Not in our library

  352. 352.

    Chen HM Liu ZH Zeng CH: Podocyte lesions in patients with obesity-related glomerulopathy. Am J Kidney Dis. 2006;48(5):772–9.

    Not in our library10.1053/j.ajkd.2006.07.025

  353. 353.

    Griffin SV Petermann AT Durvasula RV: Podocyte proliferation and differentiation in glomerular disease: role of cell-cycle regulatory proteins. Nephrol Dial Transplant. 2003;18(Suppl 6):vi8–13.

    Not in our library10.1093/ndt/gfg1069

  354. 354.

    Kriz W: Podocyte is the major culprit accounting for the progression of chronic renal disease. Microsc Res Tech. 2002;57(4):189–95.

    Not in our library10.1002/jemt.10072

  355. 355.

    Kikuchi M Wickman L Hodgin JB: Podometrics as a Potential Clinical Tool for Glomerular Disease Management. Semin Nephrol. 2015;35(3):245–55.

    Not in our library10.1016/j.semnephrol.2015.04.004

  356. 356.

    Reiser J Gupta V Kistler AD: Toward the development of podocyte-specific drugs. Kidney Int. 2010;77(8):662–8.

    Not in our library10.1038/ki.2009.559

  357. 357.

    Chugh SS Macé C Clement LC: Angiopoietin-like 4 based therapeutics for proteinuria and kidney disease. Front Pharmacol. 2014;5:23.

    Not in our library10.3389/fphar.2014.00023

  358. 358.

    Fornoni A Sageshima J Wei C: Rituximab targets podocytes in recurrent focal segmental glomerulosclerosis. Sci Transl Med. 2011;3(85):85ra46.

    Not in our library10.1126/scitranslmed.3002231

  359. 359.

    Yu CC Fornoni A Weins A: Abatacept in B7-1-positive proteinuric kidney disease. N Engl J Med. 2013;369(25):2416–23.

    Not in our library10.1056/nejmoa1304572

  360. 360.

    Benigni A Gagliardini E Remuzzi G: Abatacept in B7-1-positive proteinuric kidney disease. N Engl J Med. 2014;370(13):1261–3.

    Not in our library10.1056/nejmc1400502#sa1

  361. 361.

    Alachkar N Carter-Monroe N Reiser J: Abatacept in B7-1-positive proteinuric kidney disease. N Engl J Med. 2014;370(13):1263–4.

    Not in our library10.1056/nejmc1400502#sa2

  362. 362.

    Salant DJ: Podocyte Expression of B7-1/CD80: Is it a Reliable Biomarker for the Treatment of Proteinuric Kidney Diseases with Abatacept? J Am Soc Nephrol. 2015; pii: ASN.2015080947.

    Not in our library10.1681/asn.2015080947

  363. 363.

    Schiffer M Teng B Gu C: Pharmacological targeting of actin-dependent dynamin oligomerization ameliorates chronic kidney disease in diverse animal models. Nat Med. 2015;21(6):601–9.

    Not in our library10.1038/nm.3843

  364. 364.

    Lee HW Khan SQ Faridi MH: A Podocyte-Based Automated Screening Assay Identifies Protective Small Molecules. J Am Soc Nephrol. 2015;26(11):2741–52.

    Not in our library10.1681/asn.2014090859

Cited by papers we hold 5

Reads

Read by people on this page

None yet.

Checked or read by AI through naulon

None yet.

A person counts once a day per paper. We keep no cookie and no address: a reader is a hash that changes every day. Any month under five reads shows no number.

Are you an author?

Is this your paper?

Claim it to add your note and be paid when agents cite it. Free.