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J. Biol. Chem., Vol. 275, Issue 43, 33920-33928, October 27, 2000
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From the Cancer Center, University of California, San Diego,
La Jolla, California 92093-0912
Recent studies indicate that angiogenesis
depends, in part, on ligation of integrin
Regulation of Integrin
v
3-mediated
Endothelial Cell Migration and Angiogenesis by Integrin
51 and Protein Kinase A*
5
1 by fibronectin. Evidence is now
provided that integrin 51 regulates the
function of integrin v3 on endothelial
cells during their migration in vitro or angiogenesis in vivo. Secretion of fibronectin by endothelial cells
leads to the ligation of integrin 51,
which potentiates v3-mediated migration
on vitronectin without influencing
v3-mediated cell adhesion. Endothelial
cell attachment to vitronectin suppresses protein kinase A (PKA)
activity, while addition of soluble
anti-51 restores this activity. Moreover,
agents that activate intracellular PKA, such as forskolin, dibutyryl
cAMP or 51 antagonists, suppress endothelial cell migration on vitronectin in vitro or
angiogenesis in vivo. In contrast, inhibitors of PKA
reverse the anti-migratory or anti-angiogenic effects mediated by
51 antagonists. Therefore, v3-mediated endothelial cell migration
and angiogenesis can be regulated by PKA activity, which depends on the
ligation state of integrin 51.
*
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: Cancer Center,
University of California, San Diego, 9500 Gilman Dr., La Jolla, CA
92093-0912. Tel.: 858-822-0086; Fax: 858-822-1325; E-mail: jvarner@ucsd.edu.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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