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First published online 16 December 2003
doi: 10.1242/jcs.00871

Journal of Cell Science 117, 407-415 (2004)
Published by The Company of Biologists 2004
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Research Article

Integrin-linked kinase regulates vascular morphogenesis induced by vascular endothelial growth factor

Yayoi Kaneko, Kenji Kitazato and Yuji Basaki*

Cancer Research Laboratory, Taiho Pharmaceutical Co. Ltd, 1-27 Misugidai, Hanno, Saitama, 357-8527, Japan

* Author for correspondence (e-mail: y-basaki{at}taiho.co.jp)

Accepted 15 September 2003

Integrin-linked kinase (ILK) is one of the signaling moieties that interact with the cytoplasmic domains of integrin ß1 and ß3 subunits. Integrin-mediated outside-in signals cooperate with vascular endothelial growth factor (VEGF) receptor to promote morphological changes, cell proliferation and motility in endothelial cells. In this report we demonstrate that VEGF-induced vessel morphogenesis of human umbilical vein endothelial cells (HUVEC) was inhibited by the transfection of a dominant negative, kinase-deficient ILK (ILK-KD), as well as by treatment with the phosphatidylinositol 3-kinase inhibitor LY294002. VEGF induced phosphorylation of protein kinase B (PKB/Akt), a regulator of cell survival and apoptosis, on serine 473, but not on threonine 308, in an ILK-dependent manner. Furthermore, transfection of antisense ILK (ILK-AS) blocked the survival effect of VEGF in annexin-V binding assays, and a VEGF-mediated decrease in caspase activity was reversed by both ILK-KD and ILK-AS as measured by a homogeneous caspase-3/7 assay. We also demonstrate that both chemotactic migration and cell proliferation of HUVEC induced by VEGF were suppressed by the inhibition of ILK. We conclude that ILK plays an important role in vascular morphogenesis mediated by VEGF.

Key words: HUVEC, ILK, Morphogenesis, PKB/Akt, Survival, VEGF


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