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J Am Soc Nephrol 13:19-26, 2002
© 2002 American Society of Nephrology

Interaction of the Leucine-Rich Repeats of Polycystin-1 with Extracellular Matrix Proteins: Possible Role in Cell Proliferation

Ashraf N. Malhas, Ramadan A. Abuknesha and Robert G. Price

Division of Life Sciences, King’s College London, London, United Kingdom.

Correspondence to Professor R.G. Price, Division of Life Sciences, King’s College London, 150 Stamford Street, London SE1 9NN, UK. Phone: +44-0-2078484451; Fax: +44-0-2078484500; E-mail: robert.price{at}kcl.ac.uk

ABSTRACT. Polycystin-1, the product of the PKD1 gene, is a membrane-bound multidomain protein with a unique structure and a molecular weight of {approx}460 kD. The purpose of this study is to investigate the binding of the cystein-flanked leucine-rich repeats (LRR) of polycystin-1 to extracellular matrix (ECM) components. These interactions may play a role in normal renal development as well as the pathogenesis of autosomal-dominant polycystic kidney disease (ADPKD). In vitro assays were used to assess the binding of a fusion protein containing the LRR of polycystin-1 and that of affinity purified polycystin-1 to a number of ECM components. The results showed that the LRR modulate the binding of polycystin-1 to collagen I, fibronectin, laminin, and cyst fluid–derived laminin fragments. The addition of the LRR fusion protein to cells in culture resulted in a significant dose-dependant reduction in the rate of proliferation. Cyst fluid–derived laminin fragments had a stimulatory effect on cell proliferation, which was reversed by the LRR fusion protein. These results suggest that the LRR of polycystin-1 act as mediators of the polycystin-1 interaction with the ECM. The observed suppression effect of the LRR on cell proliferation suggests a functional role of the LRR-mediated polycystin-1 involvement in cell-matrix and cell-cell interactions. These interactions may result in the enhanced cell proliferation that is a characteristic feature of ADPKD.




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