| First Author | O'Reilly MS | Year | 1999 |
| Journal | Science | Volume | 285 |
| Issue | 5435 | Pages | 1926-8 |
| PubMed ID | 10489375 | Mgi Jnum | J:57720 |
| Mgi Id | MGI:1345582 | Doi | 10.1126/science.285.5435.1926 |
| Citation | O'Reilly MS, et al. (1999) Antiangiogenic activity of the cleaved conformation of the serpin antithrombin [see comments]. Science 285(5435):1926-8 |
| abstractText | 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. |
