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. and McConell, Glenn K. 2003, Effect of exercise intensity on skeletal muscle AMPK signaling in humans, Diabetes, vol. 52, no. 9, pp. 2205-2212, doi: 10.2337/diabetes.52.9.2205.

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Title Effect of exercise intensity on skeletal muscle AMPK signaling in humans
Author(s) Chen, Zhi-Ping
Stephens, Terry J.
Murthy, Sid
Canny, Benedict J.
Hargreaves, Mark
Witters, Lee A.
Kemp, Bruce E.
McConell, Glenn K.
Journal name Diabetes
Volume number 52
Issue number 9
Start page 2205
End page 2212
Publisher American Diabetes Association
Place of publication New York, N.Y.
Publication date 2003-09
ISSN 0012-1797
Summary 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 a1 (1.5-fold) and AMPK a2 (5-fold) activities increased from low to medium intensity, with AMPK a2 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)-ßphosphorylation was sensitive to exercise, increasing threefold from rest to low intensity, whereas neuronal NO synthase (nNOS)µphosphorylation 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 ACCß phosphorylation, then declined during high intensity. These results indicate that ACCß 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.
Language eng
DOI 10.2337/diabetes.52.9.2205
Field of Research 060104 Cell Metabolism
HERDC Research category C1 Refereed article in a scholarly journal
Copyright notice ©2003, American Diabetes Association
Persistent URL http://hdl.handle.net/10536/DRO/DU:30008634

Document type: Journal Article
Collection: School of Exercise and Nutrition Sciences
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