Antiangiogenic activity of the cleaved conformation of the serpin antithrombin.

@article{Oreilly1999AntiangiogenicAO,
  title={Antiangiogenic activity of the cleaved conformation of the serpin antithrombin.},
  author={Michael S O'reilly and Steven R Pirie-Shepherd and William S. Lane and Judah M Folkman},
  journal={Science},
  year={1999},
  volume={285 5435},
  pages={1926-8}
}
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… CONTINUE READING