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JCS ePress online publication date 17 Aug 2004
doi: 10.1242/jcs.01331

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Research Article

ILK is required for the assembly of matrix-forming adhesions and capillary morphogenesis in endothelial cells


Valérie Vouret-Craviari, Etienne Boulter, Dominique Grall, Cédric Matthews, and Ellen Van Obberghen-Schilling*
* Author for correspondence (e-mail: vanobber{at}unice.fr)

Integrins play a key role in regulating endothelial cell survival, migration and differentiated function during angiogenic blood-vessel remodeling. Integrin-linked kinase (ILK) is a multidomain protein that interacts with the cytoplasmic tail of integrin {beta} subunits and is thought to participate in integrin-mediated signal transduction. We report here that attenuation of ILK expression in cultured bovine aortic endothelial cells by RNA interference had marked effects on surface distribution of {alpha}5{beta}1 integrin and the organization of cell-matrix adhesions characterized by the disappearance of fibrillar (3D-like) adhesions that are rich in {alpha}5{beta}1 and paxillin, and associated fibrillar fibronectin matrix. This defect was not caused by a decrease in fibronectin mRNA levels or by intracellular retention of the protein. Adhesion to surface-adsorbed matrix proteins based on {beta}1 and {beta}3 integrin was enhanced following ILK depletion, whereas cell spreading, migration and multilayer alignment into capillary-like structures on Matrigel were impaired. We conclude that ILK is an important regulator of the endothelial phenotype and vascular network formation by directing the assembly and/or maturation of {alpha}5{beta}1-competent matrix-forming adhesions.


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