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Division of Cardiology, University of Cincinnati College of Medicine, Cincinnati, Ohio 45267
We tested the
hypothesis that activation of protein kinase C (PKC) isoforms in
pressure-overload heart failure was prevented by angiotensin-converting
enzyme (ACE) inhibition, resulting in normalization of cardiac
sarcoplasmic reticulum (SR) Ca2+
ATPase (SERCA) 2a and phospholamban protein levels and improvement in
intracellular Ca2+ handling.
Aortic-banded and control guinea pigs were given ramipril (5 mg · kg
1 · day
1)
or placebo for 8 wk. Ramipril-treated banded animals had lower left
ventricular (LV) and lung weight, improved survival, increased isovolumic LV mechanics, and improved cardiomyocyte
Ca2+ transients compared with
placebo-treated banded animals. This was associated with maintenance of
SERCA2a and phospholamban protein expression. Translocation of PKC-
and -
was increased in placebo-treated banded guinea pigs compared
with controls and was attenuated significantly by treatment with
ramipril. We conclude that ACE inhibition attenuates PKC translocation
and prevents downregulation of
Ca2+ cycling protein expression in
pressure-overload hypertrophy. This represents a mechanism for the
beneficial effects of this therapy on LV function and survival in heart failure.
angiotensin II; hypertrophy; sarcoplasmic reticulum calcium adenosine triphosphatase; phospholamban
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