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(Received for publication, February 3, 1997, and in revised form, March 10, 1997)
From the Second Department of Internal Medicine, Osaka City
University Medical School, Osaka 545, Japan and the
§ Department of Molecular Biology, Yokohama City University
School of Medicine, Yokohama 236, Japan
To elucidate the physiological role of protein
kinase C (PKC)
Volume 272, Number 21,
Issue of May 23, 1997
pp. 13816-13822
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
Inhibits the Proliferation of Vascular
Smooth Muscle Cells by Suppressing G1 Cyclin
Expression
, a ubiquitously expressed isoform in vascular smooth
muscle cells (VSMC), PKC was stably overexpressed in A7r5 cells,
rat clonal VSMC. The [3H]thymidine incorporation in
A7r5 overexpressed with PKC (DVs) was suppressed to 37.1 ± 16.3% (mean ± S.D.) of the level in control or A7r5 transfected
with vector alone (EVs). The reduction of [3H]thymidine
incorporation was strongly correlated with overexpressed PKC levels.
Moreover, transient transfection of a dominant negative mutant of PKC
restored the reduced proliferation in DVs. Flow cytometry analysis
demonstrated that DVs were arrested in the G0/G1 phase of the cell cycle. Expression of
cyclins D1 and E and retinoblastoma protein phosphorylation were
reduced, while the protein levels of p27 were elevated in DVs as
compared with EVs. There were no significant differences in the
expression of c-fos, c-jun, c-myc,
cyclin D2, D3, cyclin-dependent kinase 2, cyclin-dependent kinase 4, and p21 among the clones. We
conclude that PKC inhibits the proliferation of VSMC by arresting
cells in G1 via mainly inhibiting the expression of cyclin
D1 and cyclin E.
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