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At least 739 records · Page 41Linked to original sources
PubMed2006

Synaptopodin orchestrates actin organization and cell motility via regulation of RhoA signalling.

The Rho family of small GTPases (RhoA, Rac1 and Cdc42) controls signal-transduction pathways that influence many aspects of cell behaviour, including cytoskeletal dynamics. At the leading edge, Rac1 and Cdc42 promote cell motility through the formation of lamellipodia and filopodia, respectively. On the contrary, RhoA promotes the formation of contractile actin-myosin-containing stress fibres in the cell body and at the rear. Here, we identify synaptopodin, an actin-associated protein, as a novel regulator of RhoA signalling and cell migration in kidney podocytes. We show that synaptopodin induces stress fibres by competitive blocking of Smurf1-mediated ubiquitination of RhoA, thereby preventing the targeting of RhoA for proteasomal degradation. Gene silencing of synaptopodin in kidney podocytes causes the loss of stress fibres and the formation of aberrant non-polarized filopodia and impairment of cell migration. Together, these data show that synaptopodin is essential for the integrity of the podocyte actin cytoskeleton and for the regulation of podocyte cell migration.

Actins↗
PubMed2006

Glomerular clusterin is associated with PKC-alpha/beta regulation and good outcome of membranous glomerulonephritis in humans.

Mechanisms for human membranous glomerulonephritis (MGN) remain elusive. Most up-to-date concepts still rely on the rat model of Passive Heymann Nephritis that derives from an autoimmune response to glomerular megalin, with complement activation and membrane attack complex assembly. Clusterin has been reported as a megalin ligand in immunodeposits, although its role has not been clarified. We studied renal biopsies of 60 MGN patients by immunohistochemistry utilizing antibodies against clusterin, C5b-9, and phosphorylated-protien kinase C (PKC) isoforms (pPKC). In vitro experiments were performed to investigate the role of clusterin during podocyte damage by MGN serum and define clusterin binding to human podocytes, where megalin is known to be absent. Clusterin, C5b-9, and pPKC-alpha/beta showed highly variable glomerular staining, where high clusterin profiles were inversely correlated to C5b-9 and PKC-alpha/beta expression (P=0.029), and co-localized with the low-density lipoprotein receptor (LDL-R). Glomerular clusterin emerged as the single factor influencing proteinuria at multivariate analysis and was associated with a reduction of proteinuria after a follow-up of 1.5 years (-88.1%, P=0.027). Incubation of podocytes with MGN sera determined strong upregulation of pPKC-alpha/beta that was reverted by pre-incubation with clusterin, serum de-complementation, or protein-A treatment. Preliminary in vitro experiments showed podocyte binding of biotinilated clusterin, co-localization with LDL-R and specific binding inhibition with anti-LDL-R antibodies and with specific ligands. These data suggest a central role for glomerular clusterin in MGN as a modulator of inflammation that potentially influences the clinical outcome. Binding of clusterin to the LDL-R might offer an interpretative key for the pathogenesis of MGN in humans.

Adult↗
PubMed2005

The parietal epithelial cell is crucially involved in human idiopathic focal segmental glomerulosclerosis.

BACKGROUND: Focal segmental glomerulosclerosis (FSGS) is one of the most common patterns of glomerular injury encountered in human renal biopsies. Epithelial hyperplasia, which can be prominent in FSGS, has been attributed to dedifferentiation and proliferation of podocytes. Based on observations in a mouse model of FSGS, we pointed to the role of parietal epithelial cells (PECs). In the present study we investigated the relative role of PECs and podocytes in human idiopathic FSGS. METHODS: We performed a detailed study of lesions from a patient with recurrent idiopathic FSGS by serial sectioning, marker analysis and three-dimensional reconstruction of glomeruli. We have studied the expression of markers for podocytes, PECs, mesangial cells, endothelium, and myofibroblasts. We also looked at proliferation and composition of the deposited extracellular matrix (ECM). RESULTS: We found that proliferating epithelial cells in FSGS lesions are negative for podocyte and macrophage markers, but stain for PEC markers. The composition of the matrix deposited by these cells is identical to Bowman's capsule. CONCLUSION: Our study demonstrates that PECs are crucially involved in the pathogenesis of FSGS lesions.

Biopsy↗
PubMed2006

Ezrin--a useful factor in the prognosis of nephrotic syndrome in children: an immunohistochemical approach.

BACKGROUND: Minimal change disease (MCD) and diffuse mesangial proliferation (DMP) are the most common pathomorphological forms of nephrotic syndrome glomerulopathies in children. The clinical course of DMP can be characterised by either DMP-sensitivity (DMP-S) or DMP-resistance (DMP-R) to steroids, resulting in an unfavourable course of the glomerulopathy. Although the clinical processes of DMP-S and DMP-R are initially identical, resistance to steroids may be foreseen by the immunohistochemical expression of cytoskeleton-associated proteins in podocytes. AIMS: To estimate the immunohistochemical expression of ezrin in children with MCD, DMP and focal segmental glomerulosclerosis (FSGS) and to evaluate its usefulness in predicting resistance to steroids. MATERIALS AND METHODS: Renal biopsy specimens of patients with MCD (n = 15), DMP (n = 16) and FSGS (n = 6) were taken. The control tissue consisted of normal-appearing cortex taken from kidneys resected for localised neoplasms (n = 6). The indirect immunohistochemical protocol for the use of a monoclonal antibody directed against ezrin was used. RESULTS: The immunohistochemical expression of ezrin in cases progressively reduced from MCD to DMP-S to DMP-R to FSGS. Except for DMP-R and FSGS (p>0.05), the difference in ezrin expression in podocytes was significant. CONCLUSION: Ezrin can be a potent marker of podocyte injury (podocytopathy) and may help in the histological qualification of MCD, DMP and FSGS. The increased permeability of the filtration barrier in steroid-resistant and proteinuric glomerulopathies may be a consequence of subcellular changes in podocyte-associated proteins following decreased expression of ezrin.

Adolescent↗
PubMed2006

Nephrin ectodomain engagement results in Src kinase activation, nephrin phosphorylation, Nck recruitment, and actin polymerization.

A properly established and maintained podocyte intercellular junction, or slit diaphragm, is a necessary component of the selective permeability barrier of the kidney glomerulus. The observation that mutation or deletion of the slit diaphragm transmembrane protein nephrin results in failure of podocyte foot process morphogenesis and concomitant proteinuria first suggested the hypothesis that nephrin serves as a component of a signaling complex that directly integrates podocyte junctional integrity with cytoskeletal dynamics. The observations made herein provide the first direct evidence to our knowledge for a phosphorylation-mediated signaling mechanism by which this integrative function is derived. Our data support the model that during podocyte intercellular junction formation, engagement of the nephrin ectodomain induces transient Fyn catalytic activity that results in nephrin phosphorylation on specific nephrin cytoplasmic domain tyrosine residues. We found that this nephrin phosphorylation event resulted in recruitment of the SH2-SH3 domain-containing adapter protein Nck and assembly of actin filaments in an Nck-dependent fashion. Considered in the context of the role of nephrin family proteins in other organisms and the integral relationship of actin dynamics and junction formation, these observations establish a function for nephrin in regulating actin cytoskeletal dynamics.

Actins↗
PubMed2024

Deciphering the molecular nexus of BTG2 in periodontitis and diabetic kidney disease.

OBJECTIVE: To investigate the role of BTG2 in periodontitis and diabetic kidney disease (DKD) and its potential underlying mechanism. METHODS: Gene expression data for periodontitis and DKD were acquired from the Gene Expression Omnibus (GEO) database. Differential expression analysis identified co-expressed genes between these conditions. The Nephroseq V5 online nephropathy database validated the role of these genes in DKD. Pearson correlation analysis identified genes associated with our target gene. We employed Gene Set Enrichment Analysis (GSEA) and Protein-Protein Interaction (PPI) networks to elucidate potential mechanisms. Expression levels of BTG2 mRNA were examined using quantitative polymerase Chain Reaction (qPCR) and immunofluorescence assays. Western blotting quantified proteins involved in epithelial-to-mesenchymal transition (EMT), apoptosis, mTORC1 signaling, and autophagy. Additionally, wound healing and flow cytometric apoptosis assays evaluated podocyte migration and apoptosis, respectively. RESULTS: Analysis of GEO database data revealed BTG2 as a commonly differentially expressed gene in both DKD and periodontitis. BTG2 expression was reduced in DKD compared to normal conditions and correlated with proteinuria. GSEA indicated enrichment of BTG2 in the EMT and mTORC1 signaling pathways. The PPI network highlighted BTG2's relevance to S100A9, S100A12, and FPR1. Immunofluorescence assays demonstrated significantly lower BTG2 expression in podocytes under high glucose (HG) conditions. Reduced BTG2 expression in HG-treated podocytes led to increased levels of EMT markers (α-SMA, vimentin) and the apoptotic protein Bim, alongside a decrease in nephrin. Lower BTG2 levels were associated with increased podocyte mobility and apoptosis, as well as elevated RPS6KB1 and mTOR levels, but reduced autophagy marker LC3. CONCLUSION: Our findings suggest that BTG2 is a crucial intermediary gene linking DKD and periodontitis. Modulating autophagy via inhibition of the mTORC1 signaling pathway, and consequently suppressing EMT, may be pivotal in the interplay between periodontitis and DKD.

Periodontitis↗
PubMed2006

Induction of TRPC6 channel in acquired forms of proteinuric kidney disease.

Injury to podocytes and their slit diaphragms typically leads to marked proteinuria. Mutations in the TRPC6 gene that codes for a slit diaphragm-associated, cation-permeable ion channel have been shown recently to co-segregate with hereditary forms of progressive kidney failure. Herein is shown that induced expression of wild-type TRPC6 is a common feature of human proteinuric kidney diseases, with highest induction observed in membranous nephropathy. Cultured podocytes that are exposed to complement upregulate TRPC6 protein. Stimulation of receptor-operated channels in puromycin aminonucleoside-treated podocytes leads to increased calcium influx in a time- and dosage-dependent manner. Mechanistically, it is shown that TRPC6 is functionally connected to the podocyte actin cytoskeleton, which is rearranged upon overexpression of TRPC6. Transient in vivo gene delivery of TRPC6 into mice leads to expression of TRPC6 protein at the slit diaphragm and causes proteinuria. These studies suggest the involvement of TRPC6 in the pathology of nongenetic forms of proteinuric disease.

Animals↗
PubMedDate not supplied

Cellular and molecular biology of membranous nephropathy.

There have been dramatic increases in the understanding of the molecular mechanisms involved in membranous nephropathy (MN) over the past 2 decades. Most of these have come directly from studies carried out in the Heymann nephritis models of MN in rats, which closely simulate the clinical and pathologic features of the human disease. Once considered a prototypical example of circulating immune complex trapping in glomeruli, we now recognize that MN develops, in both the rat and man, consequent to an autoimmune process involving antibodies directed to antigens on the foot processes of podocytes that form subepithelial immune deposits. Proteinuria is a consequence of sublytic complement C5b-9 attack on podocytes. The podocyte response to sublytic C5b-9 includes up-regulated expression of genes for production of oxidants, proteases, prostanoids, growth factors, CTGF, transforming growth factor (TGF) and TGF receptors leading to overproduction of extracellular matrix components that result in 'spike' formations. Other podocyte changes including detachment, apoptosis and alterations in cell cycle regulatory proteins favoring hypertrophy over proliferation also contribute to proteinuria and to development of glomerular sclerosis. Finally, progression of chronic proteinuric MN to chronic kidney disease (CKD) and renal failure likely results in part from additional effects of sublytic C5b-9 on proximal tubular epithelial cells, resulting in interstitial inflammation and fibrosis with a fall in glomerular filtration rate (GFR). Expanded understanding of the molecular pathophysiology of MN has important implications for monitoring disease activity, predicting disease course and designing new approaches to therapy for this common glomerular disease.

Animals↗
PubMed1978

Scanning electron microscopy of the kidney glomerular epithelium after treatment with polycations in situ and in vitro.

Changes in fine structure of glomerular epithelial cells (podocytes) were examined after treatment in situ and in vitro with polycations (i.e., protamine sulfate and poly-1-lysine). Scanning and transmission electron microscopic observations indicate that polycation-induced alterations of the glomerular epithelium are similar in many respects to those resulting from puromycin aminonucleoside nephrosis. These alterations include the formation of junctional complexes between adjacent podocyte processes, flattening and retraction of podocyte processes, extensive folding of the slit diaphragms, formation of interpedicular microbridges, and development of irregular knobby surface-microprojections. Prolonged treatment in vitro with high concentrations of polycations results in nearly complete loss of podocyte processes and the transformation of these once elaborate cells into simple polyhedral cells. The foregoing observations support the view that pedicel loss in puromycin aminonucleoside nephrosis may be due to a reduction in the glomerular epithelial polyanionic sialic acid surface coat.

Animals↗
PubMed1979

Ultrastructure of the renal corpuscle of the garter snake Thamnophis sirtalis.

The renal corpuscle of the garter snake was examined using scanning and transmission electron microscopy, freeze-fracture and tracer experiments. The renal corpuscle was small and glomerular architecture simple. The visceral epithelium was composed of irregular, highly branched podocytes with broad, interdigitating foot processes. Numerous cell junctions, including fasciae occludentes and adhaerentes, occurred between podocytes. The podocytes bore numerous microvilli which projected into the urinary space and contained large bundles of microfilaments. The podocytes lay on a basal lamina which appeared to act as a primary filtration barrier.

Animals↗
PubMed1981

Cationized ferritin binding to anionic surfaces in normal and aminonucleoside nephrotic kidneys.

The distribution and effects of polycationized ferritin (PCF) bound ot anionic sites on living plasmalemmas and basal laminae of normal and puromycin aminonucleoside nephrotic (PAN) kidneys were studied using an in vitro model system. Immersion of normal glomeruli in physiological saline solutions containing low concentrations of PCF (0.01 to 0.1 mg/ml) for 10 seconds results in preferential binding of PCF to microvillous projections on the glomerular epithelium (i.e., podocytes). Exposure to higher concentrations of PCF (1.0 mg/ml) for 10 seconds results in several layers of PCF distributed evenly over the urinary aspect of epithelial podocytes. In these short treatment times, the thin slit diaphragms which span the filtration slits appear to be impermeable to PCF. Within several minutes after PCF treatment, ferritin is found within caveolae on the surface of epithelial podocytes and within numerous pinosomes and larger endocytic vesicles within these cells. Longer treatment with PCF results in the narrowing of filtration slit spaces and the formation of junctions between adjacent podocyte foot processes. Occurringg coincident with these structural changes is a gradual accumulation of PCF in regular patches along the lamina rara externa (LRE) of the glomerular basement membrane. Loss of foot processes and accumulation of PCF in the LRE are prevented by treatment with either cytochalasin B (25 micro g/ml), D (2 micro g/ml) or incubation at low temperatures (0-4 degrees C). When PCF-coated glomeruli are incubated in PCF-free media, the ferritin coat is shed form the free surfaces within 1/2 to 1 hour except at the tips and sides of microvillous projections. Pretreatment of normal glomeruli with neuraminidase or protamine sulfate results in a dramatic reduction in the binding of PCF to the glomerular epithelial free surface. Treatment of PAN glomeruli with PCF often results in patchlike distributions of PCF over the glomerular epithelial free surface. High concentrations of PCF (1.0 mg/ml) bind preferentially to microvillous projections on the parietal epithelial luminal surface and in distinct patchlike patterns along the basal laminae of parietal and tubular epithelial cells.

Animals↗
PubMedDate not supplied

Influence of C-peptide on early glomerular changes in diabetic mice.

BACKGROUND: C-peptide has been shown to ameliorate diabetes-induced functional and structural renal changes in animal models as well as in patients with type 1 diabetes. This study aims to examine the molecular effects of C-peptide on early glomerular changes in a mouse model of type 1 diabetes. METHODS: Fourteen days after induction of diabetes by streptozotocin (STZ), the animals received rat C-peptide for either 24 h or 7 days. Urinary albumin excretion was measured by ELISA. Glomerular mRNA expression of the transforming growth factor (TGF)-beta(1) and type IV collagen was quantified by real-time PCR. The effect of C-peptide on type IV collagen gene expression in cultured murine podocytes was also examined. RESULTS: C-peptide decreased urinary albumin excretion from 0.29 to 0.18 microg/min (-40.7%, P < 0.01). The transcript level of (alpha3)IV collagen in glomeruli was up-regulated 2.2-fold in diabetic mice and was inhibited by 45-70% (P < 0.05) upon C-peptide treatment. C-peptide suppressed glomerular expression of TGF-beta(1) by 36.6% after 7 days (P < 0.05) but not 24 h after injection. In vitro studies using cultured podocytes revealed that C-peptide dose-dependently inhibited TGF-beta-induced up-regulation of type IV collagen. Moreover, both pertussis toxin (PTX) and a specific inhibitor for extracellular signal-regulated kinase (ERK) pathway reversed the inhibitory effect of C-peptide on TGF-beta. Finally, C-peptide was shown to up-regulate the activity of ERK in podocytes. CONCLUSIONS: These findings indicate that C-peptide suppresses specific aspects of early glomerular changes in a mouse model of diabetes and that the effect is at least in part mediated via interaction with the TGF-beta signal in glomerular podocytes.

Albuminuria↗
PubMed1975

Scanning electron microscopy of the nephrotic kidney.

Scanning electron microscopy (SEMy), supplemented with light microscopy and transmission electron microscopy, was used to study aminonucleoside nephrosis in rats. The visceral epithelium undergoes dramatic restructing in response to aminonucleoside nephrosis. Due in part to an accumulation of intracellular vacuoles, kidney podocytes swell in size. Podocyte major processes lose their many pedicles and slit pores and form close junctions (80 A) with adjacent podocytes. Although no prominant pores opening into the urinary space are found in the visceral epithelium, there is evidence that podocyte vacuoles may rupture and thereby release protein into the urinary space. Many parietal cells also increase in size, accumulate intracellular vacuoles and come into very cose proximity to the visceral epithelium. Casts of PAS-positive, electron-dense material fill the lumina of many uriniferous tubules. Although most proximal tubules exhibit an extensive loss of brush border, no significant changes in other kidney microprojections or cilia were noted. Transmission electron and light microscopy of nephrotic kidneys reveal considerable changes in proximal and distal tubules including a reduction in mitochondria, in cell height, in electron density of the cytoplasmic matrix, in lateral and basal plasmalemma infolds, enlarged euchromatic nuclei, dilated lumens, and accumulation of PAS-positive cytoplasmic granules. SEMy of kidney needle biopsies from patients with proteinuria reveal that SEMy is useful for evaluating glomerular changes in man.

Animals↗
PubMed2002

Glomerular differentiation in p27 and p57 double-mutant metanephroi.

The cell cycle inhibitors p27 and p57 are initially concurrently expressed at a critical point of glomerulogenesis and podocyte differentiation. The present study generated mice lacking both p27 and p57, in order to investigate the synergistic roles of these molecules in glomerular differentiation. It appeared that p27 and p57 double-mutant mice died between E16.5 and E18.5, before glomerular differentiation can take place. We harvested E13.5 metanephroi to advance the glomerulogenesis in a metanephric organ culture. Metanephroi of double-mutant and wild-type mice showed no great difference in size and shape at harvest or after 6 days in culture. Histology and morphometry revealed that average glomerular size in metanephroi from double-mutant mice was significantly larger than those in any other mutants. Larger glomeruli in double-mutant metanephroi are composed of an increased number of podocytes. The glomeruli in the double-mutant metanephroi expressed synaptopodin and WT-1 with the same pattern and intensity as those found in wild type. In addition, electron micrography showed the presence of foot processes and slit membrane in podocytes in double mutant. Western blot analysis of metanephroi after 6 days in culture showed an up-regulation of p21 protein in p27 mutant and double-mutant, but not in p57 mutant metanephroi. These findings suggest that p27 and p57 are synergistically involved, in part, to determine the number, but not the differentiation, in podocytes.

Animals↗
PubMed2004

Interaction of the spectrin-like repeats of alpha-actinin-4 with humanin peptide.

BACKGROUND: Podocyte alpha-actinin-4 (actinin-4) is an essential component of the glomerular filtration barrier. We recently reported that the central rod spectrin-like repeats (R1-R4) of actinin-4 have a high affinity to puromycin aminonucleoside (PAN), which can induce nephro-sis in animals. The aim of this study was to identify endogenous molecules that interact with the actinin-4 R1-R4 domain. METHODS: To identify such molecules, we performed a bacterial two-hybrid screening of a human kidney cDNA library using as a bait human actinin-4 R1-R4. We further verified the identified interactions by in vitro affinity assays and immunofluorescent studies of cultured human embryonic kidney HEK293 cells. To investigate the expression of the identified molecules in podocytes, in situ hybridization, and immunohistochemical studies were performed. RESULTS: One isolated cDNA from the library encoded humanin, a recently identified antiapoptotic peptide. In vitro affinity assays showed specific interactions of recombinant actinin-4 R1-R4, R1, R2, R3, and R4 proteins with humanin-Sepharose. PAN had no effect on these interactions. Green fluorescent protein-fused humanin and endogenous actinin colocalized mainly in the perinuclear cytoplasm of HEK293 cells. Altered colocalization was not observed by the addition of PAN. In situ hybridization and immunohistochemistry showed the expression of humanin in podocytes. CONCLUSIONS: Our results suggest that humanin is a novel binding partner of the actinin-4 R1-R4 domain in podocytes. Humanin and PAN are unlikely to compete for the same binding surface in actinin-4.

Actinin↗
PubMed1980

Effects of hypophysectomy on age-related changes in the rat kidney glomerulus: observations by scanning and transmission electron microscopy.

The kidney glomeruli of 9-month-old intact, 23-month-old intact, and 23-month-old hypophysectomized female rats were examined by scanning and transmission electron microscopy. With increasing age, the glomeruli increased in diameter and more podocyte microvilli were found. Hypophysectomy (4 months before sacrifice) reduced these values to levels approaching values seen in the 9-month intact controls. Transmission electron microscopy revealed that increased numbers of podocytes and endothelial cells had cytoplasmic dense bodies with advancing age. Granular cytoplasmic material, seen in podocytes, did not alter in frequency with age. Hypophysectomy reduced the number of cells containing the dense bodies as well as the number of podocytes containing granular material. Basal laminar thickness, while increasing with age, was unaffected by hypophysectomy. The results show that hypophysectomy can return some structural age-related changes to values seen in younger subjects. The effects are similar in some respects to the effects of dietary restriction.

Aging↗
PubMed1985

Ontogenesis of the glomerular C3b receptor (CR1) in fetal human kidney.

Ontogenesis of the glomerular C3b receptor (CR1) was studied in kidneys from 16 fetuses aged from 9 to 32 weeks, using immunohistochemical techniques and the F(ab')2 fragment of a monospecific rabbit antibody to CR1, and adherence of C3b-coated sheep erythrocytes. By indirect immunofluoresence, anti-CR1 stained presumptive glomerular epithelium from the end of the S-body stage of nephron differentiation. Staining increased with visceral epithelial cell proliferation and with differentiation of the nephron from the subcortical to the juxtamedullary part of the fetal kidney. Using electron microscopy and an indirect immunoperoxidase technique, CR1 antigen was detected on the plasma membrane in the basolateral part of primitive podocytes from the late S-body stage, following the acquisition by podocytes of the capacity to synthetize a basal lamina. Endothelial cells and mesangial cells did not stain for CR1 antigen. CR1 antigen was expressed by podocytes from the same stage of glomerular differentiation as was the CALLA antigen. Glomerular expression of CR1 on podocytes preceded that of Ia on glomerular endothelial cells. C3b-bearing sheep erythrocytes only adhered to clover-like lobulated glomeruli at a late stage of glomerular differentiation. Glomerular CR1, a specific marker of glomerular capillary epithelial cells is one of the earliest markers expressed by resident glomerular cells during renal ontogenesis.

Fetus↗
PubMed2001

CD2AP localizes to the slit diaphragm and binds to nephrin via a novel C-terminal domain.

CD2AP, an adapter protein containing multiple SH3 domains, plays a critical role in kidney function. Mice lacking CD2AP die soon after birth because of kidney failure. In the kidney, CD2AP is expressed in glomerular podocytes, which suggests that it may play a role in a specialized adhesion complex known as the slit diaphragm. One of the major components of the slit diaphragm is nephrin, a podocyte-specific protein. Here we demonstrate that CD2AP localizes to the slit diaphragm in podocytes using immunoelectron microscopy and that nephrin and CD2AP co-immunoprecipitate from a podocyte cell line. The specificity of this interaction was verified by mapping studies, which demonstrated that a novel domain at the C terminus of CD2AP interacts with the C-terminal portion of the nephrin cytoplasmic domain. These studies lend further support to the idea that CD2AP plays a role in the structural integrity of the slit diaphragm.

Adaptor Proteins, Signal Transducing↗