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Science 5 January 1990:
Vol. 247. no. 4938, pp. 77 - 79
DOI: 10.1126/science.1688470

Articles

Science, Vol 247, Issue 4938, 77-79
Copyright © 1990 by American Association for the Advancement of Science


articles

Inhibition of angiogenesis by recombinant human platelet factor-4 and related peptides

TE Maione, GS Gray, J Petro, AJ Hunt, AL Donner, SI Bauer, HF Carson, and RJ Sharpe

Repligen Corporation, Cambridge, MA 02139.

Recombinant human platelet factor-4 (rhPF4), purified from Escherichia coli, inhibited blood vessel proliferation in the chicken chorioallantoic membrane in a dose-dependent manner. Treatment of several cell types with rhPF4 in vitro suggested that the angiostatic effect was due to specific inhibition of growth factor-stimulated endothelial cell proliferation. The inhibitory activities were associated with the carboxyl-terminal, heparin-binding region of the molecule and could be abrogated by including heparin in the test samples, an indication that sulfated polysaccharides might modulate the angiostatic activity of platelet factor-4 in vivo. Understanding of the mechanisms of control of angiogenesis by endogenous proteins should facilitate the development of effective treatments for diseases of pathogenic neovascularization such as Kaposi's sarcoma, diabetic retinopathy, and malignant tumor growth.


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Interferon-inducible protein-10 identified as a mediator of tumor necrosis in vivo.
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