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Prepublished online as a Blood First Edition Paper on May 15, 2003; DOI 10.1182/blood-2003-04-1114. This Article Full Text Full Text (PDF) All Versions of this Article: 2003-04-1114v1 102/6/2108    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 Naik, M. U. Articles by Naik, U. P. Search for Related Content PubMed PubMed Citation Articles by Naik, M. U. Articles by Naik, U. P. Related Collections Hemostasis, Thrombosis, and Vascular Biology Cell Adhesion and Motility Signal Transduction Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  Blood, 15 September 2003, Vol. 102, No. 6, pp. 2108-2114 HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY Signaling through JAM-1 and v3 is required for the angiogenic action of bFGF: dissociation of the JAM-1 and v3 complex Meghna U. Naik, Shaker A. Mousa, Charles A. Parkos, and Ulhas P. Naik From the Department of Biological Sciences, University of Delaware, Newark; Albany College of Pharmacy, NY; and Epithelial Pathobiology Research Unit, Department of Pathology, Emory University School of Medicine, Atlanta, GA. Growth factor–induced neovascularization has received a great deal of attention because it is fundamental to the growth and metastasis of solid tumors. This multistep process requires extensive signaling through growth factor receptors and integrins. Among the integrins involved in this process, integrin v3 is specific to basic fibroblast growth factor (bFGF)–induced angiogenesis. Here we show that junctional adhesion molecule 1/A (JAM-1/A) and v3 form a complex in the absence of bFGF. JAM-1, which is normally localized at the cell-cell junctions of quiescent endothelial cells, redistributes to the cell surface on bFGF treatment. Blockage of the extracellular domain of JAM-1 inhibits bFGF-induced endothelial cell morphology, proliferation, and angiogenesis. Additionally, mutation in the JAM-1 cytoplasmic domain blocks bFGF-induced mitogen-activated protein (MAP) kinase activation and ablates its ability to induce endothelial cell tube formation, suggesting that signaling through JAM-1 is key to bFGF-induced signaling. Immunoprecipitation analysis suggests that bFGF signaling dissociates the JAM-1/ v3 complex, allowing for signaling through JAM-1 and v3. In addition, blockage of either JAM-1 or v3 inhibits bFGF-induced MAP kinase activation. Thus, our results suggest that signaling through JAM-1 and v3 is necessary for bFGF-induced angiogenesis. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: X. Li, M. Stankovic, B. P.-L. Lee, M. Aurrand-Lions, C. N. Hahn, Y. Lu, B. A. Imhof, M. A. Vadas, and J. R. Gamble JAM-C Induces Endothelial Cell Permeability Through Its Association and Regulation of {beta}3 Integrins Arterioscler Thromb Vasc Biol, August 1, 2009; 29(8): 1200 - 1206. [Abstract] [Full Text] [PDF] E. A. Severson, W. Y. Lee, C. T. Capaldo, A. Nusrat, and C. A. Parkos Junctional Adhesion Molecule A Interacts with Afadin and PDZ-GEF2 to Activate Rap1A, Regulate {beta}1 Integrin Levels, and Enhance Cell Migration Mol. Biol. Cell, April 1, 2009; 20(7): 1916 - 1925. [Abstract] [Full Text] [PDF] M. R. Cera, M. Fabbri, C. Molendini, M. Corada, F. 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