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Cited by 160Metabolism, Diabetes, and CancerCardiovascular and exercise physiologyAdipose Tissue and Metabolism

Exercise Increases Nuclear AMPK α2 in Human Skeletal Muscle

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McGee, Sean L., Howlett, Kirsten F., Starkie, Rebecca L., Cameron-Smith, David, Kemp, Bruce E., Hargreaves, Mark·2003·Diabetes
DOI 10.2337/diabetes.52.4.926
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Abstract

An acute bout of exercise increases skeletal muscle glucose uptake, improves glucose homeostasis and insulin sensitivity, and enhances muscle oxidative capacity. Recent studies have shown an association between these adaptations and the energy-sensing 5' AMP-activated protein kinase (AMPK), the activity of which is increased in response to exercise. Activation of AMPK has been associated with enhanced expression of key metabolic proteins such as GLUT-4, hexokinase II (HKII), and mitochondrial enzymes, similar to exercise. It has been hypothesized that AMPK might regulate gene and protein expression through direct interaction with the nucleus. The purpose of this study was to determine if nuclear AMPK alpha(2) content in human skeletal muscle was increased by exercise. Following 60 min of cycling at 72 +/- 1% of VO(2peak) in six male volunteers (20.6 +/- 2.1 years; 72.9 +/- 2.1 kg; VO(2peak) = 3.62 +/- 0.18 l/min), nuclear AMPK alpha(2) content was increased 1.9 +/- 0.4-fold (P = 0.024). There was no change in whole-cell AMPK alpha(2) content or AMPK alpha(2) mRNA abundance. These results suggest that nuclear translocation of AMPK might mediate the effects of exercise on skeletal muscle gene and protein expression.

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  • AMPK can translocate to the nucleus where it regulates histone deacetylases, transcription factors and transcriptional co-activators such as HDAC5, MEF2 and PGC-1α.

    “In a feed forward fashion AMPK can translocate to the nucleus [24,27] where it regulates Histone de-aceytlases, transcription factors and transcriptional co-activators such as histone deacetylase 5 (HDAC5), myocyte enhancing factor 2 (MEF2) and peroxisome proliferator activated receptor-γ co-activator-1α (PGC-1α) respectively (Figure 1) [28][29][30].”

    From New strategies in sport nutrition to increase exercise performance (2016) · cites this paper as [27]

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Authors
McGee, S. L., Howlett, K. F., Starkie, R. L., Cameron-Smith, D., Kemp, B. E., & Hargreaves, M.
Affiliations
  • Deakin University (AU)
  • Exercise, Muscle and Metabolism Unit, School of Health Sciences, Deakin University, Burwood, Australia
  • St Vincent's Hospital Melbourne (AU)
ORCID
Venue
Diabetes
Publisher
American Diabetes Association
Published
2003-04-01
Volume
52
Issue
4
Pages
926-928
ISSN
  • 0012-1797 (ISSN-L)
  • 1939-327X
DOI
10.2337/diabetes.52.4.926
OpenAlex
W2124798116
Cited by
160
References
25
Citations by year
2026: 6 · 2025: 3 · 2024: 6 · 2023: 3 · 2022: 4 · 2021: 6 · 2020: 12 · 2019: 2 · 2018: 3 · 2017: 7 · 2016: 10 · 2015: 10 · 2014: 7 · 2013: 8 · 2012: 9
FWCI
2.77
Type
journal article
Language
en
Open access
Licence
cc-by
Locations
  • Diabetes (publishedVersion)
  • PubMed (publishedVersion)
  • Figshare (submittedVersion, cc-by)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
  • Health Sciences › Medicine › Complementary and alternative medicine › Cardiovascular and exercise physiology
  • Health Sciences › Medicine › Physiology › Adipose Tissue and Metabolism
Keywords
AMPK, AMPKα2, nuclear translocation, physical activity, skeletal muscle, GLUT4, hexokinase 2, insulin sensitivity, glucose uptake, mitochondrial enzymes, gene expression regulation, cycling exercise
MeSH terms
Adult, Cell Nucleus, Humans, Male, Multienzyme Complexes, Oxygen Consumption, RNA, Messenger, Time Factors, Exercise, Protein Serine-Threonine Kinases, Muscle, Skeletal, AMP-Activated Protein Kinases

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