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Originally published In Press as doi:10.1074/jbc.M009698200 on May 31, 2001

J. Biol. Chem., Vol. 276, Issue 32, 30359-30365, August 10, 2001
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Akt Down-regulation of p38 Signaling Provides a Novel Mechanism of Vascular Endothelial Growth Factor-mediated Cytoprotection in Endothelial Cells*

Jean-Philippe GrattonDagger §, Manuel Morales-RuizDagger §||, Yasuko Kureishi**, David FultonDagger , Kenneth Walsh**, and William C. SessaDagger Dagger Dagger

From the Dagger  Department of Pharmacology and Molecular Cardiobiology Program, Boyer Center for Molecular Medicine, Yale University School of Medicine, New Haven, Connecticut 06536 and the ** Division of Cardiovascular Research, St. Elizabeth's Medical Center of Boston, Boston, Massachusetts 02135

Vascular endothelial growth factor (VEGF) utilizes a phosphoinositide 3-kinase (PI 3-kinase)/Akt signaling pathway to protect endothelial cells from apoptotic death. Here we show that PI 3-kinase/Akt signaling promotes endothelial cell survival by inhibiting p38 mitogen-activated protein kinase (MAPK)-dependent apoptosis. Blockade of the PI 3-kinase or Akt pathways in conjunction with serum withdrawal stimulates p38-dependent apoptosis. Blockade of PI 3-kinase/Akt also led to enhanced VEGF activation of p38 and apoptosis. In this context, the pro-apoptotic effect of VEGF is attenuated by the p38 MAPK inhibitor SB203580. VEGF stimulation of endothelial cells or infection with an adenovirus expressing constitutively active Akt causes MEKK3 phosphorylation, which is associated with decreased MEKK3 kinase activity and down-regulation of MKK3/6 and p38 MAPK activation. Conversely, activation-deficient Akt decreases VEGF-stimulated MEKK3 phosphorylation and increases MKK/p38 activation. Activation of MKK3/6 is not dependent on Rac activation since dominant negative Rac does not decrease p38 activation triggered by inhibition of PI 3-kinase. Thus, cross-talk between the Akt and p38 MAPK pathways may regulate the level of cytoprotection versus apoptosis and is a new mechanism to explain the cytoprotective actions of Akt.

* This work was supported in part by National Institute of Health Grants HL 61371 and HL 64793 (to W. C. S.), T32HL10183 (to D. F.), and AR 40197, HL 50692, AG 15052, and HD23681 (to K. W.) and by a grant-in-aid from the American Heart Association (to W. C. S.).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.

§ Both authors contributed equally to this work.

Supported by a fellowship from the Canadian Institutes of Health Research.

|| Supported by Ministerio de Educación y Cultura Grant EX99-38446345 and a grant from the Asociación Española para el Estudio del Hígado, Spain.

Dagger Dagger Established investigator of the American Heart Association. To whom correspondence should be addressed. Tel.: 203-737-2291; Fax: 203-737-2290; E-mail: william.sessa@yale.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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