Cited by 799Metabolism, Diabetes, and CancerAdipose Tissue and MetabolismPeroxisome Proliferator-Activated Receptors

Inactivation of acetyl-CoA carboxylase and activation of AMP-activated protein kinase in muscle during exercise

Winder, W. W., Hardie, D. G.·1996·American Journal of Physiology-Endocrinology and Metabolism

Abstract

Malonyl-CoA, an inhibitor of fatty acid oxidation in skeletal muscle mitochondria, decreases in rat skeletal muscle during exercise or in response to electrical stimulation. Regulation of rat skeletal muscle acetyl-CoA carboxylase (ACC), the enzyme that synthesizes malonyl-CoA, was studied in vitro and in vivo. Avidin-Sepharose affinity-purified ACC from hindlimb skeletal muscle was phosphorylated by purified liver AMP-activated protein kinase with a concurrent decrease in ACC activity. AMP-activated protein kinase was quantitated in resuspended ammonium sulfate precipitates of the fast-twitch red (type IIa fibers) region of the quadriceps muscle. Rats running on a treadmill at 21 m/min up a 15% grade show a 2.4-fold activation of AMP-activated protein kinase concurrently with a marked decrease in ACC activity in the resuspended ammonium sulfate precipitates at all citrate concentrations ranging from 0 to 20 mM. Malonyl-CoA decreased from a resting value of 1.85 +/- 0.29 to 0.50 +/- 0.09 nmol/g in red quadriceps muscle after 30 min of treadmill running. The activation of the AMP-activated protein kinase with consequent phosphorylation and inactivation of ACC may be one of the primary events in the control of malonyl-CoA and hence fatty acid oxidation during exercise.

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Crossref · 10.1152/ajpendo.1996.270.2.e299

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24 of 24 references verified0 citation errors · 0 not checkable

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  • Active AMPK is involved in the increase in fat oxidation during exercise.

    “Active AMPK is involved in the increase in fat oxidation during exercise [33]”

    From Using Molecular Biology to Maximize Concurrent Training (2014) · cites this paper as [33]

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Authors
Winder, W. W., & Hardie, D. G.
Affiliations
Brigham Young University (US)
Venue
American Journal of Physiology-Endocrinology and Metabolism
Published
1996-02-01
Volume
270
Issue
2
Pages
E299-E304
ISSN
  • 0193-1849 (ISSN-L)
  • 1522-1555
OpenAlex
W2169469988
Cited by
799
References
24
Citations by year
2026: 7 · 2025: 11 · 2024: 8 · 2023: 11 · 2022: 15 · 2021: 24 · 2020: 24 · 2019: 24 · 2018: 28 · 2017: 28 · 2016: 29 · 2015: 46 · 2014: 34 · 2013: 30 · 2012: 39
FWCI
5.22
Type
journal article
Language
en
Open access
closed
Locations
  • American Journal of Physiology-Endocrinology and Metabolism (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • Wellcome Trust
  • National Institute of Arthritis and Musculoskeletal and Skin Diseases (R01AR041438, AR-41438)
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
acetyl-CoA carboxylase, AMPK, malonyl-CoA, skeletal muscle, physical activity, fatty acid oxidation, enzyme phosphorylation, treadmill running, fast-twitch muscle, citrate, energy metabolism regulation
MeSH terms
Acetyl-CoA Carboxylase, Animals, Enzyme Activation, Male, Malonyl Coenzyme A, Motor Activity, Multienzyme Complexes, Phosphorylation, Protein Kinases, Rats, Sprague-Dawley, Protein Serine-Threonine Kinases, Muscle, Skeletal, Rats, AMP-Activated Protein Kinases, In Vitro Techniques

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