Plasmin-cleaved β-2-glycoprotein 1 is an inhibitor of angiogenesis

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

Research output: Contribution to journalArticlepeer-review

31 Scopus citations


β-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 β-glycoprotein 1 is a potent antiangiogenic and antitumor molecule of potential therapeutic significance.

Original languageEnglish (US)
Pages (from-to)1659-1669
Number of pages11
JournalAmerican Journal of Pathology
Issue number5
StatePublished - Nov 2007

ASJC Scopus subject areas

  • Pathology and Forensic Medicine


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