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PMID |
Sentence |
1 |
8074995
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However, P-cadherin, plakoglobin and vinculin are the only markers detected in future glomerular cells.
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2 |
9422981
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The cytoplasmic focal adhesion proteins vinculin, talin, paxillin, p130CAS, and pp125FAK were detected, although vinculin appeared to be confined mainly to the mesangium.
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3 |
11553524
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CD2AP and p130Cas localize to different F-actin structures in podocytes.
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4 |
11553524
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Mice lacking the 80-kDa CD2-associated protein (CD2AP) develop progressive renal failure that starts soon after birth with proteinuria and foot process effacement by unknown mechanisms.
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5 |
11553524
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CD2AP has been identified and cloned independently by virtue of its interaction with the T cell protein CD2 and with the docking protein p130Cas.
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6 |
11553524
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In the present study we examined the localization of CD2AP and p130Cas in the mouse glomerulus and in cultured podocytes.
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7 |
11553524
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In glomeruli, CD2AP and p130Cas immunofluorescence were observed in podocytes, where they colocalized with F-actin in foot processes.
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8 |
11553524
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In cultured podocytes, p130Cas was enriched at sites of focal adhesions, where it colocalized like vinculin with F-actin at stress fiber ends.
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9 |
11553524
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The spot-shaped F-actin structures were also stained by antibodies against the actin nucleation Arp2/3 complex and cortactin, both contributing to dynamic actin assembly.
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10 |
11553524
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Moreover, CD2AP spots in cultured podocytes were in close spatial association with actinin-4, but not actinin-1.
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11 |
11553524
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Our results suggest that CD2AP and p130Cas, which both colocalize with F-actin in podocytes in situ, possess different functions.
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12 |
11553524
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Whereas p130Cas is found in focal adhesions, CD2AP seems to be involved in the regulation of highly dynamic F-actin structures in podocyte foot processes.
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13 |
18855004
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When compared to equal amounts of fibronectin or collagen 1, myocilin was less effective in promoting substrate adhesion.
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14 |
18855004
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Twenty-five percent of cells that had attached to myocilin substrates showed spreading and expressed focal contacts which were labeled by vinculin/phalloidin staining.
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15 |
21380797
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Plasma from a case of recurrent idiopathic FSGS perturbs non-muscle myosin IIA (MYH9 protein) in human podocytes.
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16 |
21380797
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The MYH9 gene encodes a non-muscle myosin IIA heavy chain (NMMHC-IIA) expressed in podocytes.
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17 |
21380797
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We demonstrate in vitro that plasmapheresis effluent from our patient rapidly decreased cultured podocyte levels of the phosphorylated myosin light chain (MLC) that mediates NMMHC-IIA binding to actin and induced dispersion of NMMHC-IIA from its usual position along actin stress fibers.
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18 |
21380797
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FSGS plasma also caused dispersion of slit diaphragm proteins (nephrin and podocin) and vinculin-positive focal adhesion complexes.
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19 |
21440751
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For this purpose we evaluated the vinculin- and paxillin-containing adhesion complexes and α-smooth muscle actin (α-SMA) expression on tubular cells and glomerular podocytes in first year renal allograft biopsy specimens of 74 patients.
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20 |
25096716
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Furthermore, optineurin colocalizes with vinculin-labeled focal contacts of cultured podocytes and with lysosome-like structures.
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21 |
26936875
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Immunostaining of glomeruli from mice whose podocytes were null for Ndst1 (Ndst1(-/-)) showed a disrupted pattern of localization for the cell surface proteoglycan, syndecan-4, and for α-actinin-4 compared with controls.
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22 |
26936875
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The pattern of immunostaining for synaptopodin and nephrin did not show as significant alterations.
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23 |
26936875
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Immunostaining in vitro for several markers for molecules involved in cell-matrix interactions showed that Ndst1(-/-) cells had decreased clustering of syndecan-4 and decreased recruitment of protein kinase-Cα, α-actinin-4, vinculin, and phospho-focal adhesion kinase to focal adhesions.
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24 |
30258943
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The imPOD cells express most podocyte-related markers, including WT-1, Nephrin, Tubulin and Vinculin, but not differentiation marker Synaptopodin.
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25 |
30258943
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We further demonstrate that TGFβ1 induces a podocyte injury-like response in the FLP-reverted imPOD cells by suppressing the expression of slit diaphragm-associated proteins P-Cadherin and ZO-1 and upregulating the expression of mesenchymal markers, α-SMA, Vimentin and Nestin, as well as fibrogenic factors CTGF and Col1a1.
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26 |
30464326
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Neurofilament heavy polypeptide protects against reduction in synaptopodin expression and prevents podocyte detachment.
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27 |
30464326
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Immunofluorescence and co-immunoprecipitation analyses revealed that NEFH was colocalized with synaptopodin, a podocyte-specific marker.
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28 |
30464326
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High NEFH expression in podocytes prevented the Adriamycin-induced reduction in synaptopodin expression.
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29 |
30464326
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The siRNA-mediated knockdown of NEFH in podocytes reduced the number of vinculin-containing focal contacts, thereby reducing adhesion to the extracellular matrix and increasing podocyte detachment.
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30 |
30464326
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These findings indicate that NEFH is expressed in podocytes during the disease course and that it prevents the reduction in synaptopodin expression and detachment of podocytes.
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31 |
31675484
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Furthermore, Fn1 KO podocytes showed a significant down-regulation of the focal adhesion proteins talin, vinculin, and paxillin and a reduced cell spreading, indicating an important role of Fn1 in adhesion.
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32 |
33024228
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Western blot and immunocytochemistry confirmed the alteration in the protein expression of tubulin, vimentin, podocin, cofilin-1, vinculin, E-cadherin, nephrin, VCAM-1, tenascin-C, and β-catenin.
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