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Cited by 351Metabolism, Diabetes, and CancerCardiovascular and exercise physiologyExercise and Physiological Responses

Exercise induces isoform-specific increase in 5'AMP-activated protein kinase activity in human skeletal muscle

Fujii, Nobuharu, Hayashi, Tatsuya, Hirshman, Michael F., Smith, Jeremy T., Habinowski, Susan A., Kaijser, Lennart, Mu, James, Ljungqvist, Olle +4 more·2000·Biochemical and Biophysical Research Communications
DOI 10.1006/bbrc.2000.3073
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Abstract

The 5'AMP-activated protein kinase (AMPK) is stimulated by contractile activity in rat skeletal muscle. AMPK has emerged as an important signaling intermediary in the regulation of cell metabolism being linked to exercise-induced changes in muscle glucose and fatty acid metabolism. In the present study, we determined the effects of exercise on isoform-specific AMPK activity (alpha1 and alpha2) in human skeletal muscle. Needle biopsies of vastus lateralis muscle were obtained from seven healthy subjects at rest, after 20 and 60 min of cycle ergometer exercise at 70% of VO(2)max, and 30 min following the 60 min exercise bout. In comparison to the resting state, AMPK alpha2 activity significantly increased at 20 and 60 min of exercise, and remained at a higher level with 30 min of recovery. AMPK alpha1 activity tended to slightly decrease with 20 min of exercise at 70%VO(2)max; however, the change was not statistically significant. AMPK alpha1 activities were at basal levels at 60 min of exercise and 30 min of recovery. On a separate day, the same subjects exercised for 20 min at 50% of VO(2)max. Exercise at this intensity did not change alpha2 activity, and similar to exercise at 70% of VO(2)max, there was no significant change in alpha1 activity. In conclusion, exercise at a higher intensity for only 20 min leads to increases in AMPK alpha2 activity but not alpha1 activity. These results suggest that the alpha2-containing AMPK complex, rather than alpha1, may be involved in the metabolic responses to exercise in human skeletal muscle.

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  • Endurance exercise studies with rodents and humans have shown AMPK signaling and mRNAs involved in mitochondrial biogenesis increase hours following exercise.

    “endurance exercise studies with rodents and humans have shown AMPK signaling and mRNAs involved in mitochondrial biogenesis increase hours following exercise (Fujii et al., 2000; Atherton et al., 2005; Jorgensen et al., 2005)”

    From Skeletal Muscle Ribosome and Mitochondrial Biogenesis in Response to Different Exercise Training Modalities (2021) · cites this paper as Fujii et al., 2000

  • Both AMPK α1 and α2 are activated during exercise.

    “Both AMPK α1 and α2 are activated during exercise; however, α1 activity appears to be increased during high intensity muscle contractions, which are equivalent to >100% maximal oxygen consumption (VO2 Max; measure of maximal exercise capacity) [59,62,63].”

    From AMPK and Exercise: Glucose Uptake and Insulin Sensitivity (2013) · cites this paper as [59]

  • AMPK α1 activity is increased during high intensity muscle contractions equivalent to >100% VO2 Max.

    “Both AMPK α1 and α2 are activated during exercise; however, α1 activity appears to be increased during high intensity muscle contractions, which are equivalent to >100% maximal oxygen consumption (VO2 Max; measure of maximal exercise capacity) [59,62,63].”

    From AMPK and Exercise: Glucose Uptake and Insulin Sensitivity (2013) · cites this paper as [59]

  • AMPK activation during exercise is intensity-dependent.

    “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 [59]

  • AMPK is activated during exercise in both rodents and humans.

    “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 [59]

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Authors
Fujii, N., Hayashi, T., Hirshman, M. F., Smith, J. T., Habinowski, S. A., Kaijser, L., Mu, J., Ljungqvist, O., Birnbaum, M. J., Witters, L. A., Thorell, A., & Goodyear, L. J.
Affiliations
  • Brigham and Women's Hospital (US)
  • Dartmouth College (US)
  • Karolinska Institutet (SE)
  • Howard Hughes Medical Institute (US)
Corresponding author
Goodyear, Laurie J.
ORCID
Venue
Biochemical and Biophysical Research Communications
Publisher
Elsevier BV
Published
2000-07
Volume
273
Issue
3
Pages
1150-1155
ISSN
0006-291X (ISSN-L)
DOI
10.1006/bbrc.2000.3073
OpenAlex
W2050689899
Cited by
351
References
29
Citations by year
2026: 3 · 2025: 3 · 2024: 8 · 2023: 4 · 2022: 9 · 2021: 8 · 2020: 17 · 2019: 9 · 2018: 9 · 2017: 9 · 2016: 16 · 2015: 18 · 2014: 12 · 2013: 13 · 2012: 12
FWCI
7.48
Type
journal article
Language
en
Open access
closed
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations
  • Biochemical and Biophysical Research Communications (publishedVersion)
  • PubMed (publishedVersion)
Funders
National Institute of Arthritis and Musculoskeletal and Skin Diseases (AR45670, R01AR045670, AR-42338)
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 › Rehabilitation › Exercise and Physiological Responses
Keywords
AMPK, AMPK isoforms, AMPKα1, AMPKα2, physical activity, skeletal muscle, vastus lateralis, exercise intensity, post-exercise recovery, muscle metabolism, glucose metabolism, fatty acid metabolism
MeSH terms
Adenosine Triphosphate, Adult, Amino Acid Sequence, Blood Glucose, Female, Glycogen, Humans, Isoenzymes, Male, Molecular Sequence Data, Phosphocreatine, Protein Kinases, Exercise, Muscle, Skeletal, Lactic Acid

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