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First published online 17 August 2004
doi: 10.1242/jcs.01331

Journal of Cell Science 117, 4559-4569 (2004)
Published by The Company of Biologists 2004
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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{ddagger}

Institute of Signaling, Developmental Biology and Cancer Research CNRS-UMR6543, Centre Antoine Lacassagne, 33 Avenue de Valombrose, 06189 Nice, France

{ddagger} Author for correspondence (e-mail: vanobber{at}unice.fr)

Accepted 26 May 2004

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 ß 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}5ß1 integrin and the organization of cell-matrix adhesions characterized by the disappearance of fibrillar (3D-like) adhesions that are rich in {alpha}5ß1 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 ß1 and ß3 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}5ß1-competent matrix-forming adhesions.

Key words: Integrin-linked kinase, Endothelial cells, Fibronectin fibrillogenesis, Adhesion, Migration


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