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Am J Physiol Endocrinol Metab 277: E772-E777, 1999;
0193-1849/99 $5.00
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Vol. 277, Issue 4, E772-E777, October 1999

RAPID COMMUNICATION
Regulation of fatty acid oxidation of the heart by MCD and ACC during contractile stimulation

Gary W. Goodwin and Heinrich Taegtmeyer

Division of Cardiology, Department of Internal Medicine, University of Texas-Houston Medical School, Houston, Texas 77030

We tested the hypothesis that the level of malonyl-CoA, as well as the corresponding rate of total fatty acid oxidation of the heart, is regulated by the opposing actions of acetyl-CoA carboxylase (ACC) and malonyl-CoA decarboxylase (MCD). We used isolated working rat hearts perfused under physiological conditions. MCD in heart homogenates was measured specifically by 14CO2 production from [3-14C]malonyl-CoA, and ACC was measured specifically based on the portion of total carboxylase that is citrate sensitive. Increased heart work (1 µM epinephrine + 40% increase in afterload) elicited a 40% increase in total beta -oxidation of exogenous plus endogenous lipids, accompanied by a 33% decrease in malonyl-CoA. The basal activity and citrate sensitivity of ACC (reflecting its phosphorylation state) and citrate content were unchanged. AMP levels were also unchanged. MCD activity, when measured at a subsaturating concentration of malonyl-CoA (50 µM), was increased by 55%. We conclude that physiological increments in AMP during the work transition are insufficient to promote ACC phosphorylation by AMP-stimulated protein kinase. Rather, increased fatty acid oxidation results from increased malonyl-CoA degradation by MCD.

malonyl-CoA; citrate; acetyl-CoA carboxylase; malonyl-CoA decarboxylase


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