Document Detail


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.
MedLine Citation:
PMID:  12065578     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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 approximately 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.
Authors:
Haejoe Park; Virendar K Kaushik; Scarlet Constant; Marc Prentki; Ewa Przybytkowski; Neil B Ruderman; Asish K Saha
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.     Date:  2002-06-13
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  277     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2002 Sep 
Date Detail:
Created Date:  2002-09-02     Completed Date:  2002-10-29     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  32571-7     Citation Subset:  IM    
Affiliation:
Diabetes Unit, Section of Endocrinology and Department of Medicine, Boston Medical Center, Boston, Massachusetts 02118, USA.
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MeSH Terms
Descriptor/Qualifier:
AMP-Activated Protein Kinases
Acetyl-CoA Carboxylase / metabolism*
Adipose Tissue / enzymology,  metabolism
Animals
Carboxy-Lyases / metabolism*
Gene Expression Regulation, Enzymologic
Glycerol-3-Phosphate O-Acyltransferase / metabolism*
Lipid Metabolism
Liver / enzymology
Male
Models, Biological
Multienzyme Complexes / metabolism*
Muscle, Skeletal / enzymology*
Phosphorylation
Physical Conditioning, Animal*
Precipitin Tests
Protein-Serine-Threonine Kinases / metabolism*
Rats
Rats, Sprague-Dawley
Spectrophotometry
Time Factors
Tissue Distribution
Grant Support
ID/Acronym/Agency:
DK 49147/DK/NIDDK NIH HHS; DK19514/DK/NIDDK NIH HHS
Chemical
Reg. No./Substance:
0/Multienzyme Complexes; EC 2.3.1.15/Glycerol-3-Phosphate O-Acyltransferase; EC 2.7.11.1/AMP-Activated Protein Kinases; EC 2.7.11.1/Protein-Serine-Threonine Kinases; EC 4.1.1.-/Carboxy-Lyases; EC 4.1.1.9/malonyl-CoA decarboxylase; EC 6.4.1.2/Acetyl-CoA Carboxylase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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