AMPK and the biochemistry of exercise: implications for human health and disease
Open accessAbstract
AMPK (AMP-activated protein kinase) is a phylogenetically conserved fuel-sensing enzyme that is present in all mammalian cells. During exercise, it is activated in skeletal muscle in humans, and at least in rodents, also in adipose tissue, liver and perhaps other organs by events that increase the AMP/ATP ratio. When activated, AMPK stimulates energy-generating processes such as glucose uptake and fatty acid oxidation and decreases energy-consuming processes such as protein and lipid synthesis. Exercise is perhaps the most powerful physiological activator of AMPK and a unique model for studying its many physiological roles. In addition, it improves the metabolic status of rodents with a metabolic syndrome phenotype, as does treatment with AMPK-activating agents; it is therefore tempting to attribute the therapeutic benefits of regular physical activity to activation of AMPK. Here we review the acute and chronic effects of exercise on AMPK activity in skeletal muscle and other tissues. We also discuss the potential role of AMPK activation in mediating the prevention and treatment by exercise of specific disorders associated with the metabolic syndrome, including Type 2 diabetes and Alzheimer's disease.
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Stress-responsive proteins such as serine/threonine kinase 11 and calcium/calmodulin-dependent protein kinase 2 can phosphorylate AMPK at Thr172 and increase its activity.
“Stress-responsive proteins, such as serine/threonine kinase 11 and calcium/calmodulin-dependent protein kinase 2, can also act to phosphorylate AMPK at the Thr172 residue and increase its activity (Richter and Ruderman, 2009).”
From Skeletal Muscle Ribosome and Mitochondrial Biogenesis in Response to Different Exercise Training Modalities (2021) · cites this paper as Richter and Ruderman, 2009
The Regulation of AMPK section identifies LKB1 (serine/threonine kinase 11) as an upstream AMPK kinase and says phosphorylation at Thr172 increases AMPK activity. Its “CAMKK, TAK-1 and SIRT1” subsection says CaMKKβ can phosphorylate AMPK at Thr172, but CaMKK is calcium/calmodulin-dependent protein kinase kinase, not the calcium/calmodulin-dependent protein kinase 2 named in the claim. No page number is available in our copy. (LLM, conf=0.87)
Experimental — accuracy not yet measuredActive AMPK stimulates mitochondrial biogenesis and angiogenesis, and increases appetite at hypothalamic level by stimulating secretion of adiponectin, which promotes glucose uptake and fatty acid oxidation in muscle cells.
“Furthermore, active AMPK stimulates mitochondrial biogenesis and angiogenesis, and increases appetite at the hypothalamic level by stimulating the secretion of adiponectin, which in turn promotes glucose uptake by and fatty acid oxidation in muscle cells [21,22].”
From Exercise-Induced Muscle–Fat Crosstalk: Molecular Mediators and Their Pharmacological Modulation for the Maintenance of Metabolic Flexibility in Aging (2025) · cites this paper as [22]
The Introduction (page unavailable) links AMPK to mitochondrial biogenesis, angiogenesis, and hypothalamic control of food intake. The Hypothalamus section reports that increased hypothalamic AMPK activity accompanies increased food intake, while the muscle-metabolism section describes AMPK-related glucose uptake and fatty-acid oxidation. The paper does not support the claimed chain in which AMPK stimulates adiponectin secretion, which then produces the appetite and muscle effects. (LLM, conf=0.90)
Experimental — accuracy not yet measuredHigh AMP concentrations during exercise lead to increased binding of AMP with AMPK.
“High adenosine monophosphate (AMP) concentrations during exercise (as a result of high ATP turnover) lead to increased binding of AMP with AMPK (Richter and Ruderman, 2009)”
From Skeletal Muscle Ribosome and Mitochondrial Biogenesis in Response to Different Exercise Training Modalities (2021) · cites this paper as Richter and Ruderman, 2009
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Self-citationStructural Basis for Glycogen Recognition by AMP-Activated Protein Kinase
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AMP-Activated Protein Kinase Is Not Down-Regulated in Human Skeletal Muscle of Obese Females
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Exercise rapidly increases eukaryotic elongation factor 2 phosphorylation in skeletal muscle of men
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Self-citationSelective suppression of AMP-activated protein kinase in skeletal muscle: update on ‘lazy mice’
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AMP-activated protein kinase mediates VEGF-stimulated endothelial NO production
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Muscle malonyl-CoA decreases during exercise
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Self-citationAnalysis of the Role of the AMP-Activated Protein Kinase in the Response to Cellular Stress
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Self-citationFunctional role of AMP‐activated protein kinase in the heart during exercise
Musi, N., Hirshman, M. F., Arad, M., Xing, Y., FUJII, N. L., Pomerleau, J. M., Ahmad, F., Berul, C. I., Seidman, J. G., Tian, R., et al. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.02.052 · Cited by 77 · see citing works
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IMP metabolism in human skeletal muscle after exhaustive exercise
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Self-citation
Flagged first, then by citations
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Self-citation
- Authors
- Richter, E. A., & Ruderman, N. B.
- Affiliations
- University of Copenhagen (DK)
- Boston University (US)
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 2009-02-11
- Volume
- 418
- Issue
- 2
- Pages
- 261-275
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- PMC
- PMC2779044
- OpenAlex
- W2060851332
- Cited by
- 481
- References
- 228
- Citations by year
- 2026: 21 · 2025: 28 · 2024: 31 · 2023: 23 · 2022: 27 · 2021: 35 · 2020: 28 · 2019: 31 · 2018: 27 · 2017: 28 · 2016: 26 · 2015: 32 · 2014: 22 · 2013: 29 · 2012: 30
- FWCI
- 2.29
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Biochemical Journal (publishedVersion)
- PubMed (publishedVersion)
- Research at the University of Copenhagen (University of Copenhagen) (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health (5r01dk019514-35)
- National Heart, Lung, and Blood Institute (P01HL068758)
- National Institute of Diabetes and Digestive and Kidney Diseases (R01 DK19514, R01DK067509, R01-DK-019514)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Health Sciences › Medicine › Physiology › Adipose Tissue and Metabolism
- Health Sciences › Medicine › Rehabilitation › Exercise and Physiological Responses
- Keywords
- AMPK, physical activity, AMP/ATP ratio, skeletal muscle, metabolic syndrome, type 2 diabetes, Alzheimer's disease, glucose uptake, fatty acid oxidation, energy metabolism, AMPK activators
- MeSH terms
- Animals, Disease, Health, Humans, Models, Biological, Motor Activity, Muscle Contraction, Time Factors, Biomarkers, Exercise, Muscle, Skeletal, AMP-Activated Protein Kinases
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