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

The DOI matches its Crossref record; 57 of the 57 references it cites were found in a registry or an index.

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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Metadata

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
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 › Physiology (medical) › Cardiovascular and exercise physiology
  • Health Sciences › Nursing › Nutrition and Dietetics › 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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