Factor VII-activating protease (FSAP) inhibits growth factor-mediated cell proliferation and migration of vascular smooth muscle cells 1 CHRISTIAN KANNEMEIER * , NADIA AL-FAKHRI † , KLAUS T. PREISSNER * and SANDIP M. KANSE * ,2 * Institute for Biochemistry and † Institute for Clinical Chemistry, Justus-Liebig-University Giessen, Germany 2 Correspondence: Institute for Biochemistry, Justus-Liebig-University Giessen, Friedrichstr. 24, 35392 Giessen, Germany. E-mail: sandip.kanse@biochemie.med.uni-giessen.de <h3>SPECIFIC AIMS</h3> 1. The homology of factor VII activating protease (FSAP) to proteases with known effects on vascular cellular functions such as hepatocyte growth factor activator, tissue plasminogen activator or urokinase, and the association of a genetic polymorphism in FSAP, Marburg I, with carotid stenosis prompted us to investigate the influence of FSAP on vascular smooth muscle cell (VSMC) proliferation and migration. 2. The effect of FSAP on rapid phosphorylation events in cells was analyzed. 3. Since heparin binds to and activates FSAP, its influence on the cellular effects of FSAP was investigated as was the role of serine protease inhibitors. 4. Proteolysis of platelet-derived growth factor-BB (PDGF-BB) or its receptor by FSAP was analyzed. 5. Interaction of FSAP with PDGF-BB and the influence of FSAP on PDGF-BB binding to cells were investigated. 6. The distribution
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