Antiangiogenic Activity of the Cleaved Conformation of the Serpin Antithrombin

Science  17 Sep 1999:
Vol. 285, Issue 5435, pp. 1926-1928
DOI: 10.1126/science.285.5435.1926

You are currently viewing the abstract.

View Full Text
As a service to the community, AAAS/Science has made this article free with registration.


Antithrombin, a member of the serpin family, functions as an inhibitor of thrombin and other enzymes. Cleavage of the carboxyl-terminal loop of antithrombin induces a conformational change in the molecule. Here it is shown that the cleaved conformation of antithrombin has potent antiangiogenic and antitumor activity in mouse models. The latent form of intact antithrombin, which is similar in conformation to the cleaved molecule, also inhibited angiogenesis and tumor growth. These data provide further evidence that the clotting and fibrinolytic pathways are directly involved in the regulation of angiogenesis.

  • * To whom correspondence should be addressed. E-mail: oreilly{at}

View Full Text

Cited By...