AJP - Heart Calcium Transients and Cell-Sarcomere
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Am J Physiol Heart Circ Physiol 276: H53-H62, 1999;
0363-6135/99 $5.00
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Vol. 276, Issue 1, H53-H62, January 1999

Effect of angiotensin-converting enzyme inhibition on protein kinase C and SR proteins in heart failure

Yasuchika Takeishi, Ajit Bhagwat, Nancy A. Ball, Darryl L. Kirkpatrick, Muthu Periasamy, and Richard A. Walsh

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-alpha and -epsilon 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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