Journal of Applied Physiology
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J Appl Physiol 85: 1909-1914, 1998;
8750-7587/98 $5.00
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Vol. 85, Issue 5, 1909-1914, November 1998

Influence of malonyl-CoA and palmitate concentration on rate of palmitate oxidation in rat muscle

G. F. Merrill1, E. J. Kurth2, B. B. Rasmussen2, and W. W. Winder2

1 Department of Cell Biology and Neurosciences, Rutgers University, Piscataway, New Jersey 08854; and 2 Department of Zoology, Brigham Young University, Provo, Utah 84602

5-Aminoimidazole-4-carboxamide 1-beta -D-ribofuranoside (AICAR) is taken up by perfused skeletal muscle and phosphorylated to form 5-aminoimidazole-4-carboxamide-1-beta -D-ribofuraosyl-5'-monophosphate (analog of 5'-AMP) with consequent activation of AMP-activated protein kinase, phosphorylation of acetyl-CoA carboxylase, decrease in malonyl-CoA, and increase in fatty acid oxidation. This study was designed to determine the effect of increasing levels of palmitate on the rate of fatty acid oxidation. Malonyl-CoA concentration was manipulated with AICAR at different palmitate concentrations. Rat hindlimbs were perfused with Krebs-Henseleit bicarbonate containing 4% bovine serum albumin, washed bovine red cells, 200 µU/ml insulin, 10 mM glucose, and different concentrations of palmitate (0.1-1.0 mM) without or with AICAR (2.0 mM). Perfusion with medium containing AICAR was found to activate AMP-activated protein kinase in skeletal muscle, inactivate acetyl-CoA carboxylase, and decrease malonyl-CoA at all concentrations of palmitate. The rate of palmitate oxidation increased as a function of palmitate concentration in both the presence and absence of AICAR but was always higher in the presence of AICAR. These results provide additional evidence that malonyl-CoA is an important regulator of the rate of fatty acid oxidation at palmitate concentrations in the physiological range.

acetyl-CoA carboxylase; 5-aminoimidazole-4-carboxamide 1-beta -D-ribofuranoside; adenosine 5'-monophosphate-activated protein kinase; fatty acid oxidation


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