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A more recent version of this article appeared on November 1, 2007

Published online before print September 14, 2007
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Copyright © 2007 American Society for Investigative Pathology
American Journal of Pathology, doi:10.2353/ajpath.2007.070146

Accepted for publication August 10, 2007.

Article

Plasmin-Cleaved {beta}-2-Glycoprotein 1 Is an Inhibitor of Angiogenesis

Taro Sakai, Krishnakumar Balasubramanian, Sourindra Maiti, Jyotsna B. Halder, and Alan J. Schroit@

From the Department of Cancer Biology, The University of Texas, M. D. Anderson Cancer Center, Houston, Texas

@ To whom correspondence should be addressed. E-mail: aschroit{at}mdanderson.org.


  Abstract

{beta}-2-Glycoprotein 1, an abundant plasma glycoprotein, binds anionic cell surfaces and functions as a regulator of thrombosis. Here, we show that cleavage of the kringle domain at Lys317/Thr318 switches its function to a regulator of angiogenesis. In vitro, the cleaved protein specifically inhibited the proliferation and migration of endothelial cells. The protein was without effect on preformed endothelial cell tubes. In vivo, the cleaved protein inhibited neovascularization into subcutaneously implanted Matrigel and Gelfoam sponge implants and the growth of orthotopically injected tumors. Collectively, these data indicate that plasmin-cleaved {beta}-2-glycoprotein 1 is a potent antiangiogenic and antitumor molecule of potential therapeutic significance.






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Copyright © 2007 by the American Society for Investigative Pathology.