Effect of Exercise Intensity on Skeletal Muscle AMPK Signaling in Humans

Chen, Zhi-Ping; Stephens, Terry J.; Murthy, Sid; Canny, Benedict J.; Hargreaves, Mark; Witters, Lee A.; Kemp, Bruce E.; McConell, Glenn K.

doi:10.2337/diabetes.52.9.2205

Cited by 369Metabolism, Diabetes, and CancerCardiovascular and exercise physiologyMuscle metabolism and nutrition

Effect of Exercise Intensity on Skeletal Muscle AMPK Signaling in Humans

Chen, Zhi-Ping, Stephens, Terry J., Murthy, Sid, Canny, Benedict J., Hargreaves, Mark, Witters, Lee A., Kemp, Bruce E., McConell, Glenn K.·2003·Diabetes

DOI 10.2337/diabetes.52.9.2205

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Abstract

The effect of exercise intensity on skeletal muscle AMP-activated protein kinase (AMPK) signaling and substrate metabolism was examined in eight men cycling for 20 min at each of three sequential intensities: low (40 ± 2% Vo2 peak), medium (59 ± 1% Vo2 peak), and high (79 ± 1% Vo2 peak). Muscle free AMP/ATP ratio only increased at the two higher exercise intensities (P < 0.05). AMPK α1 (1.5-fold) and AMPK α2 (5-fold) activities increased from low to medium intensity, with AMPK α2 activity increasing further from medium to high intensity. The upstream AMPK kinase activity was substantial at rest and only increased 50% with exercise, indicating that, initially, signaling through AMPK did not require AMPK kinase posttranslational modification. Acetyl-CoA carboxylase (ACC)-β phosphorylation was sensitive to exercise, increasing threefold from rest to low intensity, whereas neuronal NO synthase (nNOS)μ phosphorylation was only observed at the higher exercise intensities. Glucose disappearance (tracer) did not increase from rest to low intensity, but increased sequentially from low to medium to high intensity. Calculated fat oxidation increased from rest to low intensity in parallel with ACCβ phosphorylation, then declined during high intensity. These results indicate that ACCβ phosphorylation is especially sensitive to exercise and tightly coupled to AMPK signaling and that AMPK activation does not depend on AMPK kinase activation during exercise.

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Phosphorylation of AMPK is not the most sensitive measure of AMPK activity.
“the phosphorylation of AMPK is not the most sensitive measure of AMPK activity”
From Using Molecular Biology to Maximize Concurrent Training (2014) · cites this paper as [54]
A direct measure of AMPK activity or phosphorylation of its downstream target acetyl-CoA carboxylase shows both allosteric activation by AMP or ADP and the effect of phosphorylation.
“a direct measure of activity or the phosphorylation of its downstream target acetyl-CoA carboxylase show both the allosteric activation by AMP or ADP and the effect of phosphorylation [54]”
From Using Molecular Biology to Maximize Concurrent Training (2014) · cites this paper as [54]
Muscle AMP/ATP ratio and AMPK activity increase with exercise intensity.
“the muscle AMP/ATP ratio and AMPK activity increases with exercise intensity [54].”
From Using Molecular Biology to Maximize Concurrent Training (2014) · cites this paper as [54]
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 [58]

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“With the caveat that the phosphorylation of AMPK is not the most sensitive measure of AMPK activity (a direct measure of activity or the phosphorylation of its downstream target acetyl-CoA carboxylase show both the allosteric activation by AMP or ADP and the effect of phosphorylation [54]), this suggests that another…”
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Progressive increase in human skeletal muscle AMPKα2 activity and ACC phosphorylation during exercise
Stephens, T. J., Chen, Z.-P., Canny, B. J., Michell, B. J., Kemp, B. E., & McConell, G. K. (2002) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00101.2001 · Cited by 148 · see citing works
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Dissociation of AMPK activity and ACCβ phosphorylation in human muscle during prolonged exercise
Wojtaszewski, J. F. P., Mourtzakis, M., Hillig, T., Saltin, B., & Pilegaard, H. (2002) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)02465-8 · Cited by 126 · see citing works
Intensified exercise training does not alter AMPK signaling in human skeletal muscle.
Clark, S., Chen, Z.-P., Murphy, K., Aughey, R., McKenna, M. J., Kemp, B., & Hawley, J. (2004) · American Journal of Physiology. Endocrinology and Metabolism · doi:10.1152/ajpendo.00462.2003 · Cited by 78 · see citing works
Self-citation
Intensified exercise training does not alter AMPK signalling in human skeletal muscle
Clark, S., Aughey, R., Mckenna, M., Hawley, J., Chen, Z., Murphy, K., & Kemp, B. (2004) · RMIT Research Repository (RMIT University Library) · Cited by 1 · see citing works
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Effect of exercise intensity and hypoxia on skeletal muscle AMPK signaling and substrate metabolism in humans
Wadley, G. D., Lee, R. S., Canny, B. J., Wasuntarawat, C., Chen, Z. P., Hargreaves, M., Kemp, B. E., & McConell, G. K. (2005) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00464.2005 · Cited by 107 · see citing works
Self-citation

Authors: Chen, Z.-P., Stephens, T. J., Murthy, S., Canny, B. J., Hargreaves, M., Witters, L. A., Kemp, B. E., & McConell, G. K.
Affiliations: St. Vincent’s Institute of Medical Research, University of Melbourne, Fitzroy, Victoria, Australia
Monash University (AU)
The University of Melbourne (AU)
Deakin University (AU)
Dartmouth College (US)
ORCID: Hargreaves, Mark
Kemp, Bruce E.
McConell, Glenn K.
Venue: Diabetes
Publisher: American Diabetes Association
Published: 2003-09-01
Volume: 52
Issue: 9
Pages: 2205-2212
ISSN: 0012-1797 (ISSN-L)
1939-327X
DOI: 10.2337/diabetes.52.9.2205
OpenAlex: W2142716760
Cited by: 369
References: 55
Citations by year: 2026: 9 · 2025: 13 · 2024: 10 · 2023: 11 · 2022: 18 · 2021: 12 · 2020: 26 · 2019: 16 · 2018: 16 · 2017: 15 · 2016: 17 · 2015: 18 · 2014: 20 · 2013: 20 · 2012: 14
FWCI: 5.64
Type: journal article
Language: en
Open access: closed
Locations: Diabetes (publishedVersion)
PubMed (publishedVersion)
Victoria University Research Repository (Victoria University) (submittedVersion)
Funders: Institut National de la Santé et de la Recherche Médicale
National Institutes of Health
National Health and Medical Research Council
National Medical Research Council
National Institute of Diabetes and Digestive and Kidney Diseases (DK-35712, R01DK035712)
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
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Muscle metabolism and nutrition
Keywords: exercise intensity, AMPK, skeletal muscle, neuronal nitric oxide synthase, glucose disappearance, fat oxidation, substrate metabolism
MeSH terms: AMP-Activated Protein Kinase Kinases, Adult, Physical Exertion, Fatty Acids, Nonesterified, Glucose, Humans, Male, Nitric Oxide, Oxygen Consumption, Phosphorylation, Protein Kinases, Rest, Signal Transduction, Muscle, Skeletal, Nitric Oxide Synthase, Nitric Oxide Synthase Type I

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Effect of Exercise Intensity on Skeletal Muscle AMPK Signaling in Humans

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