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Science 17 September 1999:
Vol. 285. no. 5435, pp. 1926 - 1928
DOI: 10.1126/science.285.5435.1926
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Reports

Antiangiogenic Activity of the Cleaved Conformation of the Serpin Antithrombin

Michael S. O'Reilly, 13* Steven Pirie-Shepherd, 1 William S. Lane, 2 Judah Folkman 1

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.

1 Department of Surgery, Children's Hospital, Departments of Surgery and Cellular Biology,
2 Harvard Microchemistry Facility, 16 Divinity Avenue, Cambridge, MA 02138, USA.
3 Joint Center for Radiation Therapy, Harvard Medical School, 300 Longwood Avenue, Boston, MA 02115, USA.
*   To whom correspondence should be addressed. E-mail: oreilly{at}hub.tch.harvard.edu

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G. A. McMahon, E. Petitclerc, S. Stefansson, E. Smith, M. K. K. Wong, R. J. Westrick, D. Ginsburg, P. C. Brooks, and D. A. Lawrence (2001)
J. Biol. Chem. 276, 33964-33968
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The Serpins Are an Expanding Superfamily of Structurally Similar but Functionally Diverse Proteins. EVOLUTION, MECHANISM OF INHIBITION, NOVEL FUNCTIONS, AND A REVISED NOMENCLATURE.
G. A. Silverman, P. I. Bird, R. W. Carrell, F. C. Church, P. B. Coughlin, P. G. W. Gettins, J. A Irving, D. A. Lomas, C. J. Luke, R. W. Moyer, et al. (2001)
J. Biol. Chem. 276, 33293-33296
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Phylogeny of the Serpin Superfamily: Implications of Patterns of Amino Acid Conservation for Structure and Function.
J. A. Irving, R. N. Pike, A. M. Lesk, and J. C. Whisstock (2000)
Genome Res. 10, 1845-1864
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