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5′-AMP-activated protein kinase activity and protein expression are regulated by endurance training in human skeletal muscle
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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“Whilst γ3 appears to be predominantly expressed in glycolytic muscles, training reduces γ3 expression in humans [10,49], which may be an adaptive response to enhanced oxidative capacity (preference for lipid oxidation).”
From AMPK and Exercise: Glucose Uptake and Insulin Sensitivity (2013) · cites this paper as [49]
In the citing paper
“AMPK γ3 expression is reduced following strength training in obese type 2 diabetic humans and endurance training in healthy men [10,49].”
From AMPK and Exercise: Glucose Uptake and Insulin Sensitivity (2013) · cites this paper as [49]
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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)
- 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
- 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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