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J. Biol. Chem., Vol. 277, Issue 36, 32571-32577, September 6, 2002
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From the Changes in the concentration of
malonyl-CoA in many tissues have been related to alterations in the
activity of acetyl-CoA carboxylase (ACC), the rate-limiting enzyme in
its formation. In contrast, little is known about the physiological
role of malonyl-CoA decarboxylase (MCD), an enzyme responsible for
malonyl-CoA catabolism. In this study, we examined the effects of
voluntary exercise on MCD activity in rat liver, skeletal muscle, and
adipose tissue. In addition, the activity of
sn-glycerol-3-phosphate acyltransferase (GPAT), which like
MCD and ACC can be regulated by AMP-activated protein kinase (AMPK),
was assayed. Thirty min after the completion of a treadmill run, MCD
activity was increased ~2-fold, malonyl-CoA levels were reduced, and
ACC and GPAT activities were diminished by 50% in muscle and liver.
These events appeared to be mediated via activation of AMPK since: 1)
AMPK activity was concurrently increased by exercise in both tissues;
2) similar findings were observed after the injection of 5-amino
4 imidazole carboxamide, an AMPK activator; 3) changes in the activity
of GPAT and ACC paralleled that of MCD; and 4) the increase in MCD
activity in muscle was reversed in vitro by incubating
immunoprecipitated enzyme from the exercised muscle with protein
phosphatase 2A, and it was reproduced by incubating immunopurified MCD
from resting muscle with purified AMPK. An unexpected finding was that
exercise caused similar changes in the activities of ACC, MCD, GPAT,
and AMPK and the concentration of malonyl-CoA in adipose
tissue. In conclusion: MCD, GPAT, and ACC are coordinately regulated by
AMPK in liver and adipose tissue in response to exercise, and except for GPAT, also in muscle. The results suggest that AMPK activation plays a major role in regulating lipid metabolism in many cells following exercise. They also suggest that in each of them, it acts to
increase fatty acid oxidation and decrease its esterification.
Coordinate Regulation of Malonyl-CoA Decarboxylase,
sn-Glycerol-3-phosphate Acyltransferase, and Acetyl-CoA
Carboxylase by AMP-activated Protein Kinase in Rat Tissues in Response
to Exercise*
,,,, and
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, University of Montreal,
Montreal, Quebec H2L 4M1, Canada
*
This work was supported by Grants DK 19514 and DK
49147 from the United States Public Health Service and a grant from the Juvenile Diabetes Foundation (to N. B. R. and A. K. S.) and 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.
To whom correspondence should be addressed: Diabetes and
Metabolism Unit, Boston University Medical Center, 650 Albany St., EBRC-827, Boston, MA 02118. Tel.: 617-638-7169; Fax: 617-638-7094; E-mail: aksaha@bu.edu.
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