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J Biol Chem, Vol. 274, Issue 23, 16349-16354, June 4, 1999
From the Division of Cardiovascular Research, St. Elizabeth's
Medical Center and Program in Cell, Molecular, and Developmental
Biology, Sackler School of Biomedical Studies, Tufts University School
of Medicine, Boston, Massachusetts 02135
Regulation of endothelial cell apoptosis is a
critical modulator of normal and pathological angiogenesis. In this
study, we examined the role of the protein kinase Akt/PKB in
endothelial cell survival in response to growth factor and matrix
attachment signals. Vascular endothelial growth factor(VEGF)-induced
cytoprotection of endothelial cell monolayers correlated with the
wortmannin-sensitive induction of Akt activity. Transfection of
an adenovirus expressing a dominant-negative Akt mutant decreased
endothelial cell viability in the presence of VEGF. Conversely,
adenoviral transduction of wild-type Akt facilitated the cell survival
effects of VEGF, whereas transduction of constitutively active Akt
conferred endothelial cell survival in the absence of VEGF.
Constitutively active Akt also conferred survival to endothelial cells
in suspension culture, whereas stimulation with VEGF did not. In
suspension cultures, VEGF stimulation was unable to activate Akt, and
Akt protein levels were repressed in cells undergoing anoikis. These
data suggest that cross-talk between growth factor- and
anchorage-dependent signaling pathways are essential for
Akt activation and endothelial cell survival.
Akt Mediates Cytoprotection of Endothelial Cells by Vascular
Endothelial Growth Factor in an Anchorage-dependent
Manner
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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