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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.

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Submitted August 9, 2006
Accepted December 21, 2006

Endorepellin, the C-terminal angiostatic module of perlecan, enhances collagen-platelet responses via the {alpha}2{beta}1 integrin receptor

Gregory Bix, Rex A. Iozzo, Ben Woodall, Michelle Burrows, Angela McQuillan, Shelly Campbell, Gregg B. Fields, and Renato V. Iozzo*

Department of Pathology, Anatomy and Cell Biology, and the Cell Biology and Signaling Program, Kimmel Cancer Center, Thomas Jefferson University, Philadelphia, PA, United States
Department of Chemistry and Biochemistry, Florida Atlantic University, Boca Raton, FL, United States

* Corresponding author; email: iozzo{at}mail.jci.tju.edu.

Endorepellin, a C-terminal fragment of the vascular basement membrane proteoglycan perlecan, inhibits angiogenesis via the {alpha}2{beta}1 integrin receptor. Because this integrin is also implicated in platelet-collagen responses, and because endorepellin and/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 {alpha}2{beta}1-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 a {alpha}2{beta}1 integrin function-blocking antibody. Collectively, these results suggest that endorepellin/{alpha}2{beta}1 integrin interaction and effects are specific and cell type dependent, differ from those emanated by exposure to collagen, and may be due to cellular differences in {alpha}2{beta}1 integrin activation/ligand affinity state. These studies also suggest a heretofore unrecognized role for angiostatic basement membrane fragments in platelet biology.


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