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Am J Physiol Lung Cell Mol Physiol 282: L1135-L1142, 2002. First published January 4, 2002; doi:10.1152/ajplung.00174.2001
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Vol. 282, Issue 5, L1135-L1142, May 2002

FAK blunts adenosine-homocysteine-induced endothelial cell apoptosis: requirement for PI 3-kinase

Robert E. Bellas, Elizabeth O. Harrington, Kerri Lynn Sheahan, Julie Newton, Caroline Marcus, and Sharon Rounds

Pulmonary Vascular Biology Research Laboratory, Providence Veterans Affairs Medical Center, and Department of Medicine, Brown Medical School, Providence, Rhode Island 02908

Treatment of cultured bovine pulmonary endothelial cells (BPAEC) with adenosine (Ado) alone or in combination with homocysteine (Hc) leads to disruption of focal adhesion complexes, caspase-dependent degradation of components of focal adhesion complexes, and subsequent apoptosis. Endothelial cells transiently overexpressing paxillin or p130Cas cDNAs underwent Ado-Hc-induced apoptosis to an extent similar to that of cells transfected with vector alone. However, overexpression of focal adhesion kinase (FAK) cDNA blunted Ado-Hc-induced apoptosis. FAK constructs lacking the central catalytic domain or containing a point mutation, rendering the catalytic domain enzymatically inactive, did not provide protection from apoptosis. Constructs containing a mutation in the major autophosphorylation site (tyrosine-397) similarly did not prevent cell death. A FAK mutant in amino acid 395, deficient in phosphatidylinositol 3-kinase (PI 3-kinase) binding, was not able to blunt apoptosis. Finally, overexpression of FAK did not provide protection from apoptosis in the presence of LY-294002, a PI 3-kinase inhibitor. Taken together, these data suggest that the survival signals mediated by overexpression of FAK in response to Ado-Hc-induced apoptosis require a PI 3-kinase-dependent pathway.

cell survival; paxillin; p130Cas; endothelium; focal adhesion complexes


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