Regulation of fibronectin matrix deposition and cell proliferation by the PINCH‐ILK‐CH‐ILKBP complex

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Abstract
SPECIFIC AIMSIntegrin-linked kinase (ILK) is a cytoplasmic component of the cell-extracellular matrix contact sites. In this study, we have investigated the role of ILK and its binding proteins PINCH and CH-ILKBP (calponin homology domain-containing ILK binding protein) in renal glomerular mesangial cell proliferation and fibronectin matrix deposition, processes critically involved in the pathogenesis of glomerulosclerosis.PRINCIPAL FINDINGS1. ILK, PINCH, and CH-ILKBP form a ternary complex in primary glomerular mesangial cells and colocalize in fibrillar fibronectin matrix contactsTo test whether ILK, PINCH, and CH-ILKBP form a complex in primary glomerular mesangial cells, we immunoprecipitated CH-ILKBP from lysates of mesangial cells with a monoclonal anti-CH-ILKBP antibody. Analyses of the anti-CH-ILKBP immunoprecipitates with anti-CH-ILKBP, anti-ILK, anti-PINCH, and anti-paxillin antibodies showed that ILK and PINCH, but not paxillin, were coimmunoprecipitated with CH-ILKBP, indicating that ILK, PINC...
Funding Information
  • National Institutes of Health (DK54639)

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