AMPK‐independent pathways regulate skeletal muscle fatty acid oxidation

Dzamko, Nicolas; Schertzer, Jonathan D.; Ryall, James G.; Steel, Rohan; Macaulay, S. Lance; Wee, Sheena; Chen, Zhi‐Ping; Michell, Belinda J.; Oakhill, Jonathan S.; Watt, Matthew J.; Jørgensen, Sebastian Beck; Lynch, Gordon S.; Kemp, Bruce E.; Steinberg, Gregory R.

doi:10.1113/jphysiol.2008.159814

Cited by 147Metabolism, Diabetes, and CancerAdipose Tissue and MetabolismPeroxisome Proliferator-Activated Receptors

AMPK‐independent pathways regulate skeletal muscle fatty acid oxidation

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Dzamko, Nicolas, Schertzer, Jonathan D., Ryall, James G., Steel, Rohan, Macaulay, S. Lance, Wee, Sheena, Chen, Zhi‐Ping, Michell, Belinda J. +6 more·2008·The Journal of Physiology

DOI 10.1113/jphysiol.2008.159814PMC PMC2655404

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Abstract

The activation of AMP‐activated protein kinase (AMPK) and phosphorylation/inhibition of acetyl‐CoA carboxylase 2 (ACC2) is believed to be the principal pathway regulating fatty acid oxidation. However, during exercise AMPK activity and ACC Ser‐221 phosphorylation does not always correlate with rates of fatty acid oxidation. To address this issue we have investigated the requirement for skeletal muscle AMPK in controlling aminoimidazole‐4‐carboxymide‐1‐β‐d‐ribofuranoside (AICAR) and contraction‐stimulated fatty acid oxidation utilizing transgenic mice expressing a muscle‐specific kinase dead (KD) AMPK α2. In wild‐type (WT) mice, AICAR and contraction increased AMPK α2 and α1 activities, the phosphorylation of ACC2 and rates of fatty acid oxidation while tending to reduce malonyl‐CoA levels. Despite no activation of AMPK in KD mice, ACC2 phosphorylation was maintained, malonyl‐CoA levels were reduced and rates of fatty acid oxidation were comparable between genotypes. During treadmill exercise both KD and WT mice had similar values of respiratory exchange ratio. These studies suggested the presence of an alternative ACC2 kinase(s). Using a phosphoproteomics‐based approach we identified 18 Ser/Thr protein kinases whose phosphorylation was increased by greater than 25% in contracted KD relative to WT muscle. Utilizing bioinformatics we predicted that extracellular regulated protein‐serine kinase (ERK1/2), inhibitor of nuclear factor (NF)‐κB protein‐serine kinase β (IKKβ) and protein kinase D (PKD) may phosphorylate ACC2 at Ser‐221 but during in vitro phosphorylation assays only AMPK phosphorylated ACC2. These data demonstrate that AMPK is not essential for the regulation of fatty acid oxidation by AICAR or muscle contraction.

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AMPK α2 KO and α2KD mice have reduced AMPK T172 phosphorylation and α2 activity in skeletal muscle.
“AMPK α2 KO and α2KD mice have reduced AMPK T172 phosphorylation and α2 activity in skeletal muscle, but enhanced or modestly reduced α1 activity, respectively [31,33,34].”
From AMPK and Exercise: Glucose Uptake and Insulin Sensitivity (2013) · cites this paper as [34]

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Authors: Dzamko, N., Schertzer, J. D., Ryall, J. G., Steel, R., Macaulay, S. L., Wee, S., Chen, Z., Michell, B. J., Oakhill, J. S., Watt, M. J., Jørgensen, S. B., Lynch, G. S., Kemp, B. E., & Steinberg, G. R.
Affiliations: The University of Melbourne (AU)
Commonwealth Scientific and Industrial Research Organisation (AU)
Monash University (AU)
University of Copenhagen (DK)
ORCID: Dzamko, Nicolas
Schertzer, Jonathan D.
Ryall, James G.
Steel, Rohan
Macaulay, S. Lance
Wee, Sheena
Oakhill, Jonathan S.
Watt, Matthew J.
Jørgensen, Sebastian Beck
Lynch, Gordon S.
Kemp, Bruce E.
Steinberg, Gregory R.
Venue: The Journal of Physiology
Publisher: Wiley
Published: 2008-11-28
Volume: 586
Issue: 23
Pages: 5819-5831
ISSN: 0022-3751 (ISSN-L)
1469-7793
DOI: 10.1113/jphysiol.2008.159814
PMC: PMC2655404
OpenAlex: W1622535892
Cited by: 147
References: 65
Citations by year: 2026: 3 · 2025: 3 · 2024: 9 · 2023: 6 · 2022: 7 · 2021: 3 · 2020: 7 · 2019: 4 · 2018: 3 · 2017: 10 · 2016: 6 · 2015: 14 · 2014: 10 · 2013: 8 · 2012: 13
FWCI: 5.62
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor)
Locations: The Journal of Physiology (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Research at the University of Copenhagen (University of Copenhagen) (publishedVersion)
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, skeletal muscle, fatty acid oxidation, acetyl-CoA carboxylase 2, AICAR, muscle contraction, malonyl-CoA, respiratory exchange ratio, physical activity, ERK1/2, IKKβ, protein kinase D, phosphoproteomics
MeSH terms: Acetyl-CoA Carboxylase, Aminoimidazole Carboxamide, Animals, Carnitine O-Palmitoyltransferase, Sterol Esterase, Enzyme Inhibitors, Epoxy Compounds, Fatty Acids, Malonyl Coenzyme A, Mice, Inbred Strains, Mice, Transgenic, Motor Activity, Muscle Contraction, Oxidation-Reduction, Phosphorylation, Ribonucleotides, Immunoblotting, Signal Transduction, Muscle, Skeletal, Palmitic Acid, Mice, AMP-Activated Protein Kinases

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AMPK‐independent pathways regulate skeletal muscle fatty acid oxidation

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