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Isoform‐specific and exercise intensity‐dependent activation of 5′‐AMP‐activated protein kinase in human skeletal muscle
Open accessAbstract
1. 5'-AMP-activated protein kinase (AMPK) has been suggested to play a key role in the regulation of metabolism in skeletal muscle. AMPK is activated in treadmill-exercised and electrically stimulated rodent muscles. Whether AMPK is activated during exercise in humans is unknown. 2. We investigated the degree of activation and deactivation of alpha-isoforms of AMPK during and after exercise. Healthy human subjects performed bicycle exercise on two separate occasions at either a low ( approximately 50% maximum rate of O2 uptake (VO2,max) for 90 min) or a high ( approximately 75% VO2,max for 60 min) intensity. Biopsies from the vastus lateralis muscle were obtained before and immediately after exercise, and after 3 h of recovery. 3. We observed a 3- to 4-fold activation of the alpha2-AMPK isoform immediately after high intensity exercise, whereas no activation was observed after low intensity exercise. The activation of alpha2-AMPK was totally reversed 3 h after exercise. In contrast, alpha1-AMPK was not activated during either of the two exercise trials. 4. The in vitro AMP dependency of alpha2-AMPK was significantly greater than that of alpha1-AMPK ( approximately 3- vs. approximately 2-fold). 5. We conclude that in humans activation of alpha2-AMPK during exercise is dependent upon exercise intensity. The stable activation of alpha2-AMPK, presumably due to the activation of an upstream AMPK kinase, is compatible with a role for this kinase complex in the regulation of skeletal muscle metabolism during exercise, whereas the lack of stable alpha1-AMPK activation makes this kinase complex a less likely candidate.
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“AMPK activity increases rapidly and then returns to baseline levels within the first 3 h after high-intensity exercise [63]”
From Using Molecular Biology to Maximize Concurrent Training (2014) · cites this paper as [63]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
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“High-intensity exercise activates both AMPK and peroxisome proliferator-activated receptor co-activator (PGC-1α) to a greater extent than low-intensity exercise in skeletal muscle”
From Effect of Exercise Training on Fat Loss—Energetic Perspectives and the Role of Improved Adipose Tissue Function and Body Fat Distribution (2021) · cites this paper as Wojtaszewski et al., 2000
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“Consistent with this, AMPK is activated during exercise in both rodents and humans [51-60], in an intensity-dependent manner [57,59-61].”
From AMPK and Exercise: Glucose Uptake and Insulin Sensitivity (2013) · cites this paper as [57]
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“Consistent with this, AMPK is activated during exercise in both rodents and humans [51-60], in an intensity-dependent manner [57,59-61].”
From AMPK and Exercise: Glucose Uptake and Insulin Sensitivity (2013) · cites this paper as [57]
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5' AMP-activated protein kinase activation causes GLUT4 translocation in skeletal muscle.
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Mammalian AMP-activated protein kinase subfamily
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Malonyl-CoA, fuel sensing, and insulin resistance
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Cited by
Sorted by citations
Fiber Types in Mammalian Skeletal Muscles
Schiaffino, S., & Reggiani, C. (2011) · Physiological Reviews · doi:10.1152/physrev.00031.2010 · Cited by 3,022
Exercise Metabolism and the Molecular Regulation of Skeletal Muscle Adaptation
Egan, B., & Zierath, J. R. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2012.12.012 · Cited by 2,084
Steinberg, G. R., & Kemp, B. E. (2009) · Physiological Reviews · doi:10.1152/physrev.00011.2008 · Cited by 1,672
Exercise, GLUT4, and skeletal muscle glucose uptake
Richter, E. A., & Hargreaves, M. (2013) · Physiological Reviews · doi:10.1152/physrev.00038.2012 · Cited by 1,407
Self-citationSkeletal muscle energy metabolism during exercise
Hargreaves, M., & Spriet, L. L. (2020) · Nature Metabolism · doi:10.1038/s42255-020-0251-4 · Cited by 1,408
Metadata
- Authors
- Wojtaszewski, J. F. P., Nielsen, P., Hansen, B. F., Richter, E. A., & Kiens, B.
- Affiliations
- University of Copenhagen (DK)
- Novo Nordisk (Denmark) (DK)
- Corresponding author
- Wojtaszewski, Jørgen F. P.
- Venue
- The Journal of Physiology
- Publisher
- Wiley
- Published
- 2000-10
- Volume
- 528
- Issue
- 1
- Pages
- 221-226
- ISSN
- 0022-3751 (ISSN-L)
- 1469-7793
- PMC
- PMC2270117
- OpenAlex
- W2140558936
- Semantic Scholar
- 4455ede831ee4c56d6d419343f5a067b2777281c
- Cited by
- 435
- References
- 25
- Citations by year
- 2026: 7 · 2025: 11 · 2024: 10 · 2023: 11 · 2022: 19 · 2021: 18 · 2020: 23 · 2019: 16 · 2018: 13 · 2017: 13 · 2016: 19 · 2015: 18 · 2014: 14 · 2013: 23 · 2012: 16
- FWCI
- 6.52
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- The Journal of Physiology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Research at the University of Copenhagen (University of Copenhagen) (submittedVersion)
- Funders
- Sundhed og Sygdom, Det Frie Forskningsråd
- Danmarks Grundforskningsfond
- 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, exercise intensity, skeletal muscle metabolism, vastus lateralis, post-exercise recovery, human exercise
- MeSH terms
- Adult, Enzyme Activation, Exercise Test, Physical Exertion, Glycogen, Humans, Isoenzymes, Male, Multienzyme Complexes, Protein Serine-Threonine Kinases, Muscle, Skeletal, AMP-Activated Protein Kinases
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