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Originally published In Press as doi:10.1074/jbc.M110219200 on January 9, 2002

J. Biol. Chem., Vol. 277, Issue 13, 10760-10766, March 29, 2002
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PTEN Modulates Vascular Endothelial Growth Factor-Mediated Signaling and Angiogenic Effects*

Jianhua HuangDagger and Christopher D. KontosDagger §

From the Dagger  Department of Medicine, Division of Cardiology and § Department of Pharmacology and Cancer Biology, Duke University Medical Center, Durham, North Carolina 27710

Phosphatidylinositol 3-kinase is activated by vascular endothelial growth factor (VEGF), and many of the angiogenic cellular responses of VEGF are regulated by the lipid products of phosphatidylinositol 3-kinase. The tumor suppressor PTEN has been shown to down-regulate phosphatidylinositol 3-kinase signaling, yet the effects of PTEN on VEGF-mediated signaling and angiogenesis are unknown. Inhibition of endogenous PTEN in cultured endothelial cells by adenovirus-mediated overexpression of a dominant negative PTEN mutant (PTEN-C/S) enhanced VEGF-mediated Akt phosphorylation, and this effect correlated with decreases in caspase-3 cleavage, caspase-3 activity, and DNA degradation after induction of apoptosis with tumor necrosis factor-alpha . Overexpression of PTEN-C/S also enhanced VEGF-mediated endothelial cell proliferation and migration. In contrast, overexpression of wild-type PTEN inhibited the anti-apoptotic, proliferative, and chemotactic effects of VEGF. Moreover, PTEN-C/S increased the length of vascular sprouts in the rat aortic ring assay and modulated VEGF-mediated tube formation in an in vitro angiogenesis assay, whereas PTEN-wild type inhibited these effects. Taken together, these findings demonstrate that PTEN potently modulates VEGF-mediated signaling and function and that PTEN is a viable target in therapeutic approaches to promote or inhibit angiogenesis.

* This work was supported in part by a grant-in-aid from the Mid-Atlantic Affiliate of the American Heart Association (to C. D. K.), by National Institutes of Health Grant HL 03557, and by a grant from the Procter & Gamble Health Care Research Center (to C. D. K.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Box 3629, Duke University Medical Center, Durham, NC 27710. Tel.: 919-684-2119; Fax: 919-684-8591; E-mail: cdkontos@duke.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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