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KMID : 0624620130460040230
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BMB Reports
2013 Volume.46 No. 4 p.230 ~ p.235
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Nephrin phosphorylation regulates podocyte adhesion through the PINCH-1-ILK-α-parvin complex
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Zha Dongqing
Chen Cheng
Liang Wei
Chen Xinghua
Ma Tean
Yang Hongxia
Van Goor Harry
Ding Guohua
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Abstract
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Nephrin, a structural molecule, is also a signaling molecule after phosphorylation. Inhibition ofnephrin phosphorylation is correlated with podocyte injury. The PINCH-1-ILK-α-parvin (PIP)complex plays a crucial role in cell adhesion and cytoskeleton formation. We hypothesized thatnephrin phosphorylation influenced cytoskeleton and cell adhesion in podocytes by regulating the PIP complex. The nephrin phosphorylation, PIP complex formation, and F-actin in Wistar rats intraperitoneally injected with puromycin aminonucleoside were gradually decreased but increased with time, coinciding with the recovery from glomerular/podocyte injury and proteinuria. In cultured podocytes, PIP complex knockdown resulted in cytoskeleton reorganization and decreased celladhesion and spreading. Nephrin and its phosphorylation were unaffected after PIP complexknockdown. Furthermore, inhibition of nephrin phosphorylation suppressed PIP complexexpression, disorganized podocyte cytoskeleton, and decreased cell adhesion and spreading. These findings indicate that alterations in nephrin phosphorylation disorganize podocytecytoskeleton and decrease cell adhesion through a PIP complex-dependent mechanism.
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KEYWORD
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Cell adhesion, Nephrin phosphorylation, PINCH-1-ILK-α-parvin complex, Podocyte
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