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Blood, 15 August 2006, Vol. 108, No. 4, pp. 1243-1250. Prepublished online as a Blood First Edition Paper on April 18, 2006; DOI 10.1182/blood-2005-11-4447. This Article Full Text Full Text (PDF) Supplemental Figures All Versions of this Article: 2005-11-4447v1 108/4/1243    most recent Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Favier, B. Articles by Bono, F. Search for Related Content PubMed PubMed Citation Articles by Favier, B. Articles by Bono, F. Related Collections Hemostasis, Thrombosis, and Vascular Biology Apoptosis Cell Adhesion and Motility Signal Transduction Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY Neuropilin-2 interacts with VEGFR-2 and VEGFR-3 and promotes human endothelial cell survival and migration Benoit Favier, Antoine Alam, Pauline Barron, Jacques Bonnin, Patricia Laboudie, Pierre Fons, Marie Mandron, Jean-Pascal Herault, Gera Neufeld, Pierre Savi, Jean-Marc Herbert, and Françoise Bono From the Sanofi-Synthelabo Research, Angiogenesis and Thrombosis Department, Toulouse, France; and the Bruce Rappaport Faculty of Medicine, Technion, Israel Institute of Technology, Haifa, Israel. Neuropilin 2 (NRP2) is a receptor for the vascular endothelial growth factor (VEGF) and the semaphorin (SEMA) families, 2 unrelated ligand families involved in angiogenesis and neuronal guidance. NRP2 specifically binds VEGF-A and VEGF-C, although the biological relevance of these interactions in human endothelial cells is poorly understood. In this study, we show that both VEGF-A and VEGF-C induce the interaction of NRP2 with VEGFR-2. This interaction correlated with an enhancement of the VEGFR-2 phosphorylation threshold. Overexpression of NRP2 in primary human endothelial cells promoted cell survival induced by VEGF-A and VEGF-C. In contrast, SEMA3F, another ligand for NRP2, was able to inhibit human endothelial cell survival and migration induced by VEGF-A and VEGF-C. Moreover, a siRNA targeting specifically NRP2 was a potent inhibitor of human endothelial cell migration induced by VEGF-A and VEGF-C. Thus, our data indicate that NRP2 acts as a coreceptor that enhances human endothelial cell biological responses induced by VEGF-A and VEGF-C. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: F. 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