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J. Biol. Chem., Vol. 275, Issue 21, 15926-15932, May 26, 2000
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From the Center for Cardiovascular Research, University of
Rochester, Rochester, New York 14642
Several signal transduction events
induced by angiotensin II (AngII) binding to the angiotensin II type 1 receptor resemble those evoked by platelet-derived growth factor (PDGF)
binding to the PDGF-
Angiotensin II Induces Transactivation of Two Different
Populations of the Platelet-derived Growth Factor
Receptor
KEY ROLE FOR THE p66 ADAPTOR PROTEIN Shc*
§,¶,
, and
receptor (PDGF-R). We report here, in
agreement with previous data, that AngII and PDGF-B-chain homodimer
(PDGF-BB) stimulate tyrosine phosphorylation of the PDGF-R. Both
AngII and PDGF-BB stimulated the phosphorylation of PDGF-R via the binding of tyrosine-phosphorylated Shc to PDGF-R. Both PDGF-BB- and
AngII-induced phosphorylation of the Shc·PDGF-R complex was inhibited by antioxidants such as N-acetylcysteine and
Tiron, but not by calcium chelation. However, transactivation of
PDGF-R by AngII (measured by PDGF-R tyrosine phosphorylation)
differed significantly from PDGF-BB. Evidence to support different
mechanisms of PDGF-R phosphorylation includes differences in the
time course of PDGF-R phosphorylation, differing effects of
inhibitors of the endogenous PDGF-R tyrosine kinase and Src family
tyrosine kinases, differing results when the PDGF-R was directly
immunoprecipitated (PDGF-R-antibody) versus
coimmunoprecipitated (Shc-antibody), and cell fractionation studies
that suggested that the Shc·PDGF-R complexes phosphorylated by
AngII and PDGF-BB were located in separate subcellular compartments.
These studies are the first to suggest that transactivation of tyrosine
kinase receptors by G protein-coupled receptors involves a unique
pathway that regulates a population of tyrosine kinase receptors
different from the endogenous tyrosine kinase ligand.
*
This work was supported in part by Grants R01 HL49192 and
R01 HL59975 from the NHLBI, National Institutes of Health (to
B. C. B.).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.
The first two authors contributed equally to this work.
§
Supported by De Drie Lichten, The Netherlands. Present address:
Dept. of Pathology, University of Maastricht, Maastricht, The Netherlands.
¶
Supported by Grant HA 2868/1-1 from the Deutsche Forschungsgemeinschaft.
Present address: Dept. of Clinical Laboratory, Hiroshima
University School of Medicine, 1-2-3 Kasumi, Minami-ku Hiroshima 734, Japan.
**
To whom correspondence should be addressed: University of
Rochester, Cardiovascular Research Center, 601 Elmwood Ave., Rochester, NY 14642. Tel.: 716-273-1946; Fax: 716-273-1497; E-mail:
bradford_berk@urmc.rochester.edu.
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