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Cited by 161Metabolism, Diabetes, and CancerCardiovascular and exercise physiologyMuscle metabolism and nutrition

The DOI matches its Crossref record; 47 of the 47 references it cites were found in a registry or an index.

5′-AMP-activated protein kinase activity and protein expression are regulated by endurance training in human skeletal muscle

Frøsig, Christian, Jørgensen, Sebastian B., Hardie, D. Grahame, Richter, Erik A., Wojtaszewski, Jørgen F. P.·2004·American Journal of Physiology-Endocrinology and Metabolism
DOI 10.1152/ajpendo.00317.2003
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Abstract

The 5′-AMP-activated protein kinase (AMPK) is proposed to be involved in signaling pathways leading to adaptations in skeletal muscle in response to both a single exercise bout and exercise training. This study investigated the effect of endurance training on protein content of catalytic (α 1, α 2) and regulatory (β 1, β 2 and γ 1, γ 2, γ 3) subunit isoforms of AMPK as well as on basal AMPK activity in human skeletal muscle. Eight healthy young men performed supervised one-legged knee extensor endurance training for 3 wk. Muscle biopsies were obtained before and 15 h after training in both legs. In response to training the protein content of α 1, β 2 and γ 1 increased in the trained leg by 41, 34, and 26%, respectively (α 1 and β 2 P < 0.005, γ 1 P < 0.05). In contrast, the protein content of the regulatory γ 3-isoform decreased by 62% in the trained leg ( P = 0.01), whereas no effect of training was seen for α 2, β 1, and γ 2. AMPK activity associated with the α 1- and the α 2-isoforms increased in the trained leg by 94 and 49%, respectively (both P < 0.005). In agreement with these observations, phosphorylation of α-AMPK-(Thr 172) and of the AMPK target acetyl-CoA carboxylase-β(Ser 221) increased by 74 and 180%, respectively (both P < 0.001). Essentially similar results were obtained in four additional subjects studied 55 h after training. This study demonstrates that protein content and basal AMPK activity in human skeletal muscle are highly susceptible to endurance exercise training. Except for the increase in γ 1 protein, all observed adaptations to training could be ascribed to local contraction-induced mechanisms, since they did not occur in the contralateral untrained muscle.

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Metadata

Authors
Frøsig, C., Jørgensen, S. B., Hardie, D. G., Richter, E. A., & Wojtaszewski, J. F. P.
Affiliations
University of Copenhagen (DK)
ORCID
Venue
American Journal of Physiology-Endocrinology and Metabolism
Publisher
American Physiological Society
Published
2004-03
Volume
286
Issue
3
Pages
E411-E417
ISSN
  • 0193-1849 (ISSN-L)
  • 1522-1555
DOI
10.1152/ajpendo.00317.2003
OpenAlex
W2063486797
Cited by
161
References
47
Citations by year
2025: 3 · 2024: 2 · 2023: 3 · 2022: 2 · 2021: 5 · 2020: 1 · 2019: 4 · 2018: 9 · 2017: 1 · 2016: 4 · 2015: 9 · 2014: 6 · 2013: 15 · 2012: 11
FWCI
6.27
Type
journal article
Language
en
Open access
closed
Locations
  • American Journal of Physiology-Endocrinology and Metabolism (publishedVersion)
  • PubMed (publishedVersion)
  • Research at the University of Copenhagen (University of Copenhagen) (submittedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
  • Health Sciences › Medicine › Physiology (medical) › Cardiovascular and exercise physiology
  • Health Sciences › Nursing › Nutrition and Dietetics › Muscle metabolism and nutrition
Keywords
AMPK, endurance training, skeletal muscle, AMPK isoforms, ACACB, Thr172 phosphorylation, muscle protein content, exercise adaptation, knee extension exercise
MeSH terms
Adaptation, Physiological, Adult, Enzyme Activation, Exercise Test, Humans, Isoenzymes, Knee, Male, Multienzyme Complexes, Muscle Contraction, Physical Education and Training, Physical Endurance, Exercise, Gene Expression Regulation, Enzymologic, Protein Serine-Threonine Kinases, Muscle, Skeletal, AMP-Activated Protein Kinases

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