Cited by 217Metabolism, Diabetes, and CancerAdipose Tissue and MetabolismPeroxisome Proliferator-Activated Receptors

AMPK as a metabolic switch in rat muscle, liver and adipose tissue after exercise

Ruderman, N. B., Park, H., Kaushik, V. K., Dean, D., Constant, S., Prentki, M., Saha, A. K.·2003·Acta Physiologica Scandinavica

Abstract

UNLABELLED: An increasing body of evidence has revealed that activation of adenosine monophosphate (AMP)-activated protein kinase (AMPK)-activated protein kinase increases fatty acid oxidation by lowering the concentration of malonyl coenzyme A (CoA), an inhibitor of carnitine palmitoyl transferase 1. Studies carried out primarily in skeletal muscle suggest that AMPK modulates the concentration of malonyl CoA by concurrently phosphorylating and inhibiting acetyl CoA carboxylase (ACC), the rate limiting enzyme in malonyl CoA synthesis, and phosphorylating and activating malonyl CoA decarboxylase (MCD), an enzyme involved in its degradation. We have recently observed that AMPK and MCD activities are increased and ACC activity diminished in skeletal muscle, liver and, surprisingly, in adipose tissue 30 min following exercise (treadmill run) in normal rats. In liver and adipose tissue these changes were associated with a decrease in the activity of glycerol-3-phosphate acyltransferase (GPAT), which catalyses the first committed reaction in glycerolipid synthesis and, which like ACC, is phosphorylated and inhibited by AMPK. Similar changes in ACC, MCD and GPAT were observed following the administration of 5-aminoimidazole 4-carboxamide-riboside (AICAR), further indicating that the exercise-induced alterations in these enzymes were AMPK-mediated. CONCLUSIONS: (1) AMPK plays a major role in regulating lipid metabolism in multiple tissues following exercise. (2) The net effect of its activation is to increase fatty acid oxidation and diminish glycerolipid synthesis. (3) The relevance of these findings to the regulation of muscle glycogen repletion in the post-exercise state and to the demonstrated ability of AMPK activation to decrease adiposity and increase insulin sensitivity in rodents remains to be determined.

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Crossref · 10.1046/j.1365-201x.2003.01164.x

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Authors
Ruderman, N. B., Park, H., Kaushik, V. K., Dean, D., Constant, S., Prentki, M., & Saha, A. K.
Affiliations
  • Boston University (US)
  • Université de Montréal (CA)
Corresponding author
Ruderman, N. B.
Venue
Acta Physiologica Scandinavica
Publisher
Wiley
Published
2003-07-16
Volume
178
Issue
4
Pages
435-442
ISSN
  • 0001-6772 (ISSN-L)
  • 1365-201X
OpenAlex
W2169826533
Cited by
217
References
35
Citations by year
2026: 1 · 2025: 2 · 2024: 3 · 2023: 2 · 2022: 7 · 2021: 8 · 2020: 7 · 2019: 10 · 2018: 4 · 2017: 8 · 2016: 4 · 2015: 15 · 2014: 14 · 2013: 21 · 2012: 14
FWCI
0.98
Type
journal article
Language
en
Open access
closed
Locations
  • Acta Physiologica Scandinavica (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • National Institutes of Health (5r01dk019514-35)
  • National Institute of Diabetes and Digestive and Kidney Diseases (DK-49147, DK-19514, R01DK049147)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
  • Health Sciences › Medicine › Physiology › Adipose Tissue and Metabolism
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Peroxisome Proliferator-Activated Receptors
Keywords
AMPK, physical activity, fatty acid oxidation, malonyl-CoA, carnitine palmitoyltransferase 1, acetyl-CoA carboxylase, malonyl-CoA decarboxylase, glycerol-3-phosphate acyltransferase, glycerolipid biosynthesis, skeletal muscle, liver, adipose tissue, AICAR, insulin sensitivity, adiposity
MeSH terms
Acetyl-CoA Carboxylase, Adipose Tissue, Aminoimidazole Carboxamide, Animals, Glycerol-3-Phosphate O-Acyltransferase, Hypoglycemic Agents, Liver, Malonyl Coenzyme A, Physical Conditioning, Animal, Ribonucleotides, Cyclic AMP-Dependent Protein Kinases, Muscle, Skeletal, Rats

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