Open AccessHuman Podocytes Adhere to the KRGDS Motif of the α3α4α5 Collagen IV Network
Author(s) -
Corina M. Borza,
Dorin-Bogdan Borza,
Vadim Pedchenko,
Moin A. Saleem,
Peter W. Mathieson,
Yoshikazu Sado,
Heather M. Hudson,
Ambra Pozzi,
Juan Saus,
Dale R. Abrahamson,
Roy Zent,
Billy G. Hudson
Publication year - 2008
Publication title -
journal of the american society of nephrology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.451
H-Index - 279
eISSN - 1533-3450
pISSN - 1046-6673
DOI - 10.1681/asn.2007070793
Subject(s) - integrin , podocyte , glomerular basement membrane , microbiology and biotechnology , basement membrane , cell adhesion , chemistry , phosphorylation , type iv collagen , cell adhesion molecule , rgd motif , cell , biology , biochemistry , laminin , extracellular matrix , glomerulonephritis , endocrinology , kidney , proteinuria
Podocyte adhesion to the glomerular basement membrane is required for proper function of the glomerular filtration barrier. However, the mechanism whereby podocytes adhere to collagen IV networks, a major component of the glomerular basement membrane, is poorly understood. The predominant collagen IV network is composed of triple helical protomers containing the alpha3alpha4alpha5 chains. The protomers connect via the trimeric noncollagenous (NC1) domains to form hexamers at the interface. Because the NC1 domains of this network can potentially support integrin-dependent cell adhesion, it was determined whether individual NC1 monomers or alpha3alpha4alpha5 hexamers support podocyte adhesion. It was found that, although human podocytes did not adhere to NC1 domains proper, they did adhere via integrin alphavbeta3 to a KRGDS motif located adjacent to alpha3NC1 domains. Because the KRGDS motif is a site of phosphorylation, its interactions with integrin alphavbeta3 may play a critical role in cell signaling in physiologic and pathologic states.