Abstract #4919

Effect of Knockout of Two Acetyl-CoA Carboxylase Isoforms in the Isolated Mouse Heart on Oxidation of Exogenous and Endogenous Energy Sources

Gaurav Sharma¹, Chai-Wan Kim^2,3, Xiaodong Wen¹, A. Dean Sherry^1,4,5, Chalermchai Khemtong^1,6,7, Craig R. Malloy^1,2,4, and Jay D. Horton^2,3

¹Advanced Imaging Research Center, University of Texas Southwestern Medical Center, Dallas, TX, United States, ²Department of Internal Medicine, University of Texas Southwestern Medical Center, Dallas, TX, United States, ³Department of Molecular Genetics, University of Texas Southwestern Medical Center, Dallas, TX, United States, ⁴Department of Radiology, University of Texas Southwestern Medical Center, Dallas, TX, United States, ⁵Department of Chemistry, University of Texas at Dallas, Richardson, TX, United States, ⁶Department of Medicine, Division of Endocrinology, Diabetes and Metabolism, University of Florida, Gainesville, FL, United States, ⁷Department of Biochemistry and Molecular Biology, University of Florida, Gainesville, FL, United States

Synopsis

The product of acetyl-CoA carboxylase (ACC), malonyl-CoA, inhibits oxidation of long chain fatty acids by mitochondria. Cardiac-specific deletion of ACC-2 is associated with increased oxidation of fatty acids, as expected, the effects on glucose oxidation are controversial, and increased oxidation of stored triglycerides has been postulated. Expression of the other isoform, ACC-1, is preserved in ACC-2 mutant hearts, so alternative sources of malonyl-CoA may be important. We found that knock out of both isoforms was associated with a small increase in fatty acid oxidation, a small decrease in glucose oxidation, and little effect on oxidation of stored energy supplies.

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