The DOI matches its Crossref record; 73 of the 73 references it cites were found in a registry or an index.
Energy sensing by the AMP-activated protein kinase and its effects on muscle metabolism
Open accessAbstract
The AMP-activated protein kinase (AMPK) is a sensor of cellular energy status, and a regulator of energy balance at both the cellular and whole body levels. Although ubiquitously expressed, its function is best understood in skeletal muscle. AMPK contains sites that reversibly bind AMP or ATP, with an increase in cellular AMP:ATP ratio (signalling a fall in cellular energy status) switching on the kinase. In muscle, AMPK activation is therefore triggered by sustained contraction, and appears to be particularly important in the metabolic changes that occur in the transition from resistance to endurance exercise. Once activated, AMPK switches on catabolic processes that generate ATP, while switching off energy-requiring processes not essential in the short term. Thus, it acutely activates glucose uptake (by promoting translocation of the transporter GLUT4 to the membrane) and fatty acid oxidation, while switching off glycogen synthesis and protein synthesis (the later via inactivation of the mammalian target-of-rapamycin pathway). Prolonged AMPK activation also causes some of the chronic adaptations to endurance exercise, such as increased GLUT4 expression and mitochondrial biogenesis. AMPK contains a glycogen-binding domain that causes a sub-fraction to bind to the surface of the glycogen particle, and it can inhibit glycogen synthesis by phosphorylating glycogen synthase. We have shown that AMPK is inhibited by exposed non-reducing ends in glycogen. We are working on the hypothesis that this ensures that glycogen synthesis is rapidly activated when glycogen becomes depleted after exercise, but is switched off again as soon as glycogen stores are replenished.
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“Therefore, it comes as no surprise that AMPK is a key mediator of the adaptation to endurance exercise, particularly in skeletal muscle (54).”
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“Prolonged AMPK activation can lead to a chronic adaptation to endurance exercise, like mitochondrial biogenesis and increased GLUT4 expression [60].”
From Regulation of Energy Substrate Metabolism in Endurance Exercise (2021) · cites this paper as [60]
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Metadata
- Authors
- Hardie, D. G.
- Affiliations
- University of Dundee (GB)
- Corresponding author
- Hardie, D. Grahame
- ORCID
- Hardie, D. Grahame
- Venue
- Proceedings of the Nutrition Society
- Publisher
- Cambridge University Press (CUP)
- Published
- 2010-11-11
- Volume
- 70
- Issue
- 1
- Pages
- 92-99
- ISSN
- 0029-6651 (ISSN-L)
- 1475-2719
- OpenAlex
- W2165667722
- Cited by
- 146
- References
- 73
- Citations by year
- 2026: 4 · 2025: 6 · 2024: 5 · 2023: 5 · 2022: 7 · 2021: 10 · 2020: 4 · 2019: 8 · 2018: 4 · 2017: 10 · 2016: 6 · 2015: 14 · 2014: 15 · 2013: 15 · 2012: 22
- FWCI
- 1.35
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Proceedings of The Nutrition Society (publishedVersion)
- PubMed (publishedVersion)
- Discovery Research Portal (University of Dundee) (submittedVersion)
- Funders
- Pfizer
- AstraZeneca
- University of Dundee
- Merck KGaA
- Wellcome Trust (080982, 081195)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Health Sciences › Nursing › Nutrition and Dietetics › Muscle metabolism and nutrition
- Health Sciences › Medicine › Physiology (medical) › Adipose Tissue and Metabolism
- Keywords
- AMPK, energy sensing, skeletal muscle metabolism, endurance exercise, resistance training, GLUT4 translocation, glucose uptake, fatty acid oxidation, glycogen synthesis, glycogen synthase phosphorylation, mTOR signaling, mitochondrial biogenesis, AMP/ATP ratio, exercise adaptation
- MeSH terms
- Adenosine Monophosphate, Adenosine Triphosphate, Energy Metabolism, Glucose, Glycogen, Humans, Muscle Contraction, Muscle Proteins, Signal Transduction, Exercise, Muscle, Skeletal, Lipid Metabolism, AMP-Activated Protein Kinases
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