SEARCH:   Advanced

Blood, 1 February 2004, Vol. 103, No. 3, pp. 955-962. Prepublished online as a Blood First Edition Paper on October 2, 2003; DOI 10.1182/blood-2003-07-2214. This Article Full Text Full Text (PDF) Supplemental Figures All Versions of this Article: 2003-07-2214v1 103/3/955    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 Prager, G. W. Articles by Binder, B. R. Search for Related Content PubMed PubMed Citation Articles by Prager, G. W. Articles by Binder, B. R. 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  HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY Vascular endothelial growth factor (VEGF) induces rapid prourokinase (pro-uPA) activation on the surface of endothelial cells Gerald W. Prager, Johannes M. Breuss, Stefan Steurer, Judit Mihaly, and Bernd R. Binder From the Department of Vascular Biology and Thrombosis Research, University of Vienna, Vienna, Austria; and Bio Molecular Therapeutics (BMT) Research, Vienna, Austria. Vascular endothelial growth factor (VEGF) is the pivotal angiogenic growth factor activating endothelial cells to migrate, proliferate, and form capillary tubes. For an ordered endothelial cell migration, tissue invasion, and degradation of the extracellular matrix, proteolytic machinery is indispensable. Such machinery, suitable for localized proteolysis, is provided by the prourokinase-urokinase-plasmin system. Prourokinase (pro-uPA), the initial component of this system, is, however, synthesized in its inactive precursor form and as such bound to its cellular receptor uPAR. Here we identify a mechanism via which VEGF165 interacting with its receptor VEGFR-2 rapidly induces prourokinase activation that is dependent on a change in integrin affinity, activation of matrix metalloproteinase 2 (MMP-2), and pro-uPA being bound to its surface receptor uPAR. This VEGF-induced pro-uPA activation on endothelial cells is responsible for VEGF-dependent local fibrinolytic activity and might be one of the initial steps in the angiogenic process. (Blood. 2004;103:955-962) CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: Y. Liu, D. J. Cao, I. M. Sainz, Y.-L. Guo, and R. W. Colman The inhibitory effect of HKa in endothelial cell tube formation is mediated by disrupting the uPA-uPAR complex and inhibiting its signaling and internalization Am J Physiol Cell Physiol, July 1, 2008; 295(1): C257 - C267. [Abstract] [Full Text] [PDF] M.-J. Park, H.-J. Kwak, H.-C. Lee, D.-H. Yoo, I.-C. Park, M.-S. Kim, S.-H. Lee, C. H. Rhee, and S.-I. Hong Nerve Growth Factor Induces Endothelial Cell Invasion and Cord Formation by Promoting Matrix Metalloproteinase-2 Expression through the Phosphatidylinositol 3-Kinase/Akt Signaling Pathway and AP-2 Transcription Factor J. Biol. Chem., October 19, 2007; 282(42): 30485 - 30496. [Abstract] [Full Text] [PDF] T. L. Haas, J. L. Doyle, M. R. Distasi, L. E. Norton, K. M. Sheridan, and J. L. Unthank Involvement of MMPs in the outward remodeling of collateral mesenteric arteries Am J Physiol Heart Circ Physiol, October 1, 2007; 293(4): H2429 - H2437. [Abstract] [Full Text] [PDF] Y. Ben-Yosef, A. Miller, S. Shapiro, and N. Lahat Hypoxia of endothelial cells leads to MMP-2-dependent survival and death Am J Physiol Cell Physiol, November 1, 2005; 289(5): C1321 - C1331. [Abstract] [Full Text] [PDF] V. Leksa, S. Godar, H. B. Schiller, E. Fuertbauer, A. Muhammad, K. Slezakova, V. Horejsi, P. Steinlein, U. H. Weidle, B. R. Binder, et al. TGF-{beta}-induced apoptosis in endothelial cells mediated by M6P/IGFII-R and mini-plasminogen J. Cell Sci., October 1, 2005; 118(19): 4577 - 4586. [Abstract] [Full Text] [PDF] L. Ma, G. Francia, A. Viloria-Petit, D. J. Hicklin, J. du Manoir, J. Rak, and R. S. Kerbel In vitro Procoagulant Activity Induced in Endothelial Cells by Chemotherapy and Antiangiogenic Drug Combinations: Modulation by Lower-Dose Chemotherapy Cancer Res., June 15, 2005; 65(12): 5365 - 5373. [Abstract] [Full Text] [PDF] J. Yu, D. Bian, C. Mahanivong, R. K. Cheng, W. Zhou, and S. Huang p38 Mitogen-activated Protein Kinase Regulation of Endothelial Cell Migration Depends on Urokinase Plasminogen Activator Expression J. Biol. Chem., November 26, 2004; 279(48): 50446 - 50454. [Abstract] [Full Text] [PDF] G. W. Prager, J. M. Breuss, S. Steurer, D. Olcaydu, J. Mihaly, P. M. Brunner, H. Stockinger, and B. R. Binder Vascular Endothelial Growth Factor Receptor-2-Induced Initial Endothelial Cell Migration Depends on the Presence of the Urokinase Receptor Circ. Res., June 25, 2004; 94(12): 1562 - 1570. [Abstract] [Full Text] [PDF]

	Copyright © 2004 by American Society of Hematology         Online ISSN: 1528-0020