RGD Reference Report - Regulation of fatty acid oxidation of the heart by MCD and ACC during contractile stimulation. - Rat Genome Database

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

Authors: Goodwin, GW  Taegtmeyer, H 
Citation: Goodwin GW and Taegtmeyer H, Am J Physiol. 1999 Oct;277(4 Pt 1):E772-7.
RGD ID: 1600797
Pubmed: PMID:10516138   (View Abstract at PubMed)

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 (14)CO(2) production from [3-(14)C]malonyl-CoA, and ACC was measured specifically based on the portion of total carboxylase that is citrate sensitive. Increased heart work (1 microM 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 microM), 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.

Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
regulation of fatty acid beta-oxidation  IDA 1600797 RGD 

Objects Annotated

Genes (Rattus norvegicus)
Mlycd  (malonyl-CoA decarboxylase)


Additional Information