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1 Division of Endocrinology and Metabolism and 2 Department of Molecular and Cellular Physiology, College of Medicine, University of Cincinnati, Cincinnati, Ohio 45267-0547
Ets-1 is a transcription factor
that activates expression of matrix-degrading proteinases such as
collagenase and stromelysin. To study the control of
ets-1 gene expression in rat vascular smooth muscle cells (VSMC), cells were exposed to factors known to
regulate VSMC migration and proliferation. Platelet-derived growth
factor-BB (PDGF-BB), endothelin-1 (ET-1), and phorbol 12-myristate 13-acetate (PMA) induced a dose-dependent expression of
ets-1 mRNA. These effects were
abrogated by inhibition of protein kinase C (PKC) by H-7 or chronic
PMA treatment. Ets-1 mRNA was
superinduced by PDGF-BB and ET-1 in the presence of
cycloheximide. The chelation of intracellular
Ca2+ by
1,2-bis(2-aminophenoxy)ethane-N,N,N',N'-tetraacetic
acid-acetoxymethyl ester and the depletion of endoplasmic reticulum
intracellular Ca2+
concentration
([Ca2+]i)
by thapsigargin inhibited PDGF-BB- and ET-1-induced
ets-1 mRNA, whereas ethylene
glycol-bis(
-aminoethyl
ether)-N,N,N',N'-tetraacetic acid had no effect. However,
[Ca2+]i
release alone was not sufficient to increase
ets-1 mRNA. Forskolin blocked ET-1-,
PDGF-BB-, and PMA-induced ets-1 mRNA,
as well as inositol phosphate formation, consistent with an effect
through impairment of PKC activation. Inhibitors of
ets-1 gene expression, such as H-7 and
herbimycin A, inhibited the ET-1 induction of collagenase I mRNA. We
propose that ets-1 may be an important element in the orchestration of matrix proteinase expression and of
vascular remodeling after arterial injury.
gene expression; thapsigargin; collagenase I; endothelin-1; platelet-derived growth factor
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