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Originally published In Press as doi:10.1074/jbc.C200044200 on February 20, 2002

J. Biol. Chem., Vol. 277, Issue 16, 13371-13374, April 19, 2002
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ACCELERATED PUBLICATION
Loss of p53 Compensates for alpha v-Integrin Function in Retinal Neovascularization*

Staffan StrömbladDagger §, Arun Fotedar, Howard Brickner, Chandra Theesfeld||, Edith Aguilar de Diaz||, Martin Friedlander||, and David A. Cheresh**

From the Dagger  Department of Microbiology, Pathology, and Immunology, Karolinska Institutet, 141 86 Huddinge, and Södertörns Högskola, 141 04 Huddinge, Sweden, the  Sidney Kimmel Cancer Center, San Diego, California 92121, and Departments of || Cell Biology and ** Immunology and Vascular Biology, The Scripps Research Institute, La Jolla, California 92037

alpha v-Integrin antagonists block neovascularization in various species, whereas 20% of alpha v-integrin null mice are born with many normal looking blood vessels. Given that blockade of alpha v-integrins during angiogenesis induces p53 activity, we utilized p53 null mice to elucidate whether loss of p53 can compensate for alpha v-integrin function in neovascularization of the retina. Murine retinal vascularization was inhibited by systemic administration of an alpha v-integrin antagonist. In contrast, mice lacking p53 were refractory to this treatment, indicating that neovascularization in normal mice depends on alpha v-integrin-mediated suppression of p53. Blockade of alpha v-integrins during neovascularization resulted in an induction of p21CIP1 in wild type and, surprisingly, in p53 null retinas, indicating that alpha v-integrin ligation regulates p21CIP1 levels in a p53-independent manner. In conclusion, we demonstrate for the first time an in vivo intracellular mechanism for compensation of integrin function and that p53 and alpha v-integrins act in concert during retinal neovascularization.

* This work was supported by grants from the Swedish Cancer Society, The Swedish Medical Research Council, and the Magnus Bergvall Foundation (to S. S.), National Institutes of Health Grants CA74435 (to A. F.) and CA 502289 and CA 45726 (to D. A. C.), and NEI, National Institutes of Health Grant EY11254 (to M. F.).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: Karolinska Institutet, Huddinge University Hospital F46, SE-141 86 Huddinge, Sweden. Tel.: 46-8-585-81032; Fax: 46-8-585-81020; E-mail: Staffan.Stromblad@ impi.ki.se.

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