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J. Biol. Chem., Vol. 276, Issue 49, 46605-46611, December 7, 2001
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From the The hypothesis of this study is that the sodium
pump complex acts as an intracellular signal-transducing molecule in
canine vascular smooth muscle cells through its interaction with other membrane and cytoskeletal proteins. We have demonstrated that 1 nM ouabain induced transactivation of the epidermal
growth factor receptor (EGFR), resulting in increased proliferation and
bromodeoxyuridine (BrdUrd) uptake. Immunoprecipitation and Western
blotting showed that the EGFR and Src were phosphorylated within 5 min
of 10
Ouabain-induced Signaling and Vascular Smooth Muscle Cell
Proliferation*
,§¶
Department of Molecular Physiology and
Biophysics and the § Section of Cardiovascular Sciences,
Department of Medicine, Baylor College of Medicine, Houston, Texas
77030
9 M ouabain stimulation. Both
ouabain-induced DNA synthesis (BrdUrd uptake) and MAPK42/44
phosphorylation were inhibited by the Src inhibitor PP2, the EGFR
kinase inhibitor AG1478, the tyrosine kinase inhibitor genistein, and
the MEK1 inhibitor PD98059. Ouabain concentrations higher than 1 nM had little or no stimulating effect on proliferation or
BrdUrd uptake but did minimally activate ERK1/2. Thus, low
concentrations of ouabain, which do not inhibit the sodium pump
sufficiently to perturb the resting cellular ionic milieu, initiate a
transactivational signaling cascade leading to vascular smooth
muscle cell proliferation.
*
This study was supported by the DeBakey Heart Center and
National Institutes of Health Grant HL24585.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.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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