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Blood, 1 May 2007, Vol. 109, No. 9, pp. 3745-3748. Prepublished online as a Blood First Edition Paper on December 29, 2006; DOI 10.1182/blood-2006-08-039925. This Article Full Text Full Text (PDF) Supplemental Figures All Versions of this Article: blood-2006-08-039925v1 109/9/3745    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 Bix, G. Articles by Iozzo, R. V. Search for Related Content PubMed PubMed Citation Articles by Bix, G. Articles by Iozzo, R. V. Related Collections Hemostasis, Thrombosis, and Vascular Biology Brief Reports Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY Endorepellin, the C-terminal angiostatic module of perlecan, enhances collagen-platelet responses via the 2ß1-integrin receptor Gregory Bix1, Rex A. Iozzo1, Ben Woodall1, Michelle Burrows1, Angela McQuillan1, Shelly Campbell1, Gregg B. Fields2, and Renato V. Iozzo1 1 Department of Pathology, Anatomy and Cell Biology, and the Cell Biology and Signaling Program, Kimmel Cancer Center, Thomas Jefferson University, Philadelphia, PA; 2 Department of Chemistry and Biochemistry, Florida Atlantic University, Boca Raton, FL Endorepellin, a C-terminal fragment of the vascular basement membrane proteoglycan perlecan, inhibits angiogenesis via the 2ß1-integrin receptor. Because this integrin is also implicated in platelet-collagen responses and because endorepellin or its fragments are generated in response to injury and inflammation, we hypothesized that endorepellin could also affect platelet biology. We discovered that endorepellin supported 2ß1-dependent platelet adhesion, without appreciably activating or aggregating platelets. Notably, endorepellin enhanced collagen-evoked responses in platelets, in a src kinase-dependent fashion, and enhanced the collagen-inhibitory effect of an 2ß1-integrin function-blocking antibody. Collectively, these results suggest that endorepellin/2ß1-integrin interaction and effects are specific and dependent on cell type, differ from those emanated by exposure to collagen, and may be due to cellular differences in 2ß1-integrin activation/ligand affinity state. These studies also suggest a heretofore unrecognized role for angiostatic basement membrane fragments in platelet biology. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: J. D. San Antonio, J. J. Zoeller, K. Habursky, K. Turner, W. Pimtong, M. Burrows, S. Choi, S. Basra, J. S. Bennett, W. F. DeGrado, et al. A Key Role for the Integrin {alpha}2{beta}1 in Experimental and Developmental Angiogenesis Am. J. Pathol., September 1, 2009; 175(3): 1338 - 1347. [Abstract] [Full Text] [PDF] J.-F. Cailhier, I. Sirois, P. Laplante, S. Lepage, M.-A. Raymond, N. Brassard, A. Prat, R. V. Iozzo, A. V. Pshezhetsky, and M.-J. Hebert Caspase-3 Activation Triggers Extracellular Cathepsin L Release and Endorepellin Proteolysis J. Biol. Chem., October 3, 2008; 283(40): 27220 - 27229. [Abstract] [Full Text] [PDF] J. J. Zoeller, A. McQuillan, J. Whitelock, S.-Y. Ho, and R. V. Iozzo A central function for perlecan in skeletal muscle and cardiovascular development J. Cell Biol., April 21, 2008; 181(2): 381 - 394. [Abstract] [Full Text] [PDF] B. P. Woodall, A. Nystrom, R. A. Iozzo, J. A. Eble, S. Niland, T. Krieg, B. Eckes, A. Pozzi, and R. V. Iozzo Integrin {alpha}2 1 Is the Required Receptor for Endorepellin Angiostatic Activity J. Biol. Chem., January 25, 2008; 283(4): 2335 - 2343. [Abstract] [Full Text] [PDF]

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