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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 (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 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 Social Bookmarking                   What's this? Submitted April 10, 2003 Accepted May 12, 2003 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* Department of Biological Sciences, University of Delaware, Newark, DE, USA Albany College of Pharmacy, Albany, NY, USA Department of Pathology and Laboratory Medicine, Emory University School of Medicine, Atlanta, GA, USA * Corresponding author; email: unaik{at}udel.edu. The process of growth factor-induced neovascularization has received a great deal of attention as it is fundamental to the growth and metastasis of solid tumors. This multi-step process requires extensive signaling through both growth factor receptors and integrins. Among the integrins known to be 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 upon 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 also 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. 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