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J. Biol. Chem., Vol. 275, Issue 32, 24279-24283, August 11, 2000
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From the Alterations in the concentration of
malonyl-CoA, an inhibitor of carnitine palmitoyltransferase I,
have been linked to the regulation of fatty acid oxidation in skeletal
muscle. During contraction decreases in muscle malonyl-CoA
concentration have been related to activation of AMP-activated protein
kinase (AMPK), which phosphorylates and inhibits acetyl-CoA carboxylase
(ACC), the rate-limiting enzyme in malonyl-CoA formation. We report
here that the activity of malonyl-CoA decarboxylase (MCD) is increased in contracting muscle. Using either immunopurified enzyme or enzyme partially purified by
(NH4)2SO4 precipitation,
2-3-fold increases in the Vmax of MCD and a
40% decrease in its Km for malonyl-CoA (190 versus 119 µM) were observed in rat
gastrocnemius muscle after 5 min of contraction, induced by electrical
stimulation of the sciatic nerve. The increase in MCD activity was
markedly diminished when immunopurified enzyme was treated with protein phosphatase 2A or when phosphatase inhibitors were omitted from the
homogenizing solution and assay mixture. Incubation of extensor digitorum longus muscle for 1 h with 2 mM
5-aminoimidazole-4-carboxamide-1-
Activation of Malonyl-CoA Decarboxylase in Rat Skeletal Muscle by
Contraction and the AMP-activated Protein Kinase Activator
5-Aminoimidazole-4-carboxamide-1-
-D-ribofuranoside*
§,,
,,,
Diabetes Unit, Section of Endocrinology, and
Departments of Medicine, Physiology, and Biochemistry, Boston Medical
Center, Boston, Massachusetts 02118 and the ¶ Molecular Nutrition
Unit, Department of Nutrition and the CR-CHUM, University of
Montreal, Montreal, Quebec H2L 4M1, Canada
-D-ribofuranoside, a cell-permeable activator of AMPK, increased MCD activity 2-fold. Here, too, addition of protein phosphatase 2A to the
immunopellets reversed the increase of MCD activity. The results
strongly suggest that activation of AMPK during muscle contraction
leads to phosphorylation of MCD and an increase in its activity. They
also suggest a dual control of malonyl-CoA concentration by ACC and
MCD, via AMPK, during exercise.
*
This work was supported by United States Public Health
Service Grants DK 19514 and DK 49147 and a grant from the Juvenile Diabetes Foundation (to N. B. R. and A. K. S.) and
by grants from the Medical Research Council of Canada, the Canadian
Diabetes Association, and the Juvenile Diabetes Foundation
International (to M. P.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Recipient of a postdoctoral fellowship of the Juvenile
Diabetes Foundation.
**
Medical Research Council of Canada Scientist.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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