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1 Institute of Exercise and Sport Sciences and 4 August Krogh Institute, Copenhagen Muscle Research Centre, University of Copenhagen, DK-2100 Copenhagen, Denmark; 2 Wellcome Trust Biocentre, Division of Molecular Physiology, University of Dundee, Dundee DD1 4HN, Scotland, United Kingdom; and 3 Joslin Diabetes Center, Harvard Medical School, Boston, Massachusetts 02215
5'-AMP-activated
protein kinase (AMPK) has been proposed to be a pivotal factor in
cellular responses to both acute exercise and exercise
training. To investigate whether protein levels and gene
expression of catalytic (
1, 2) and
regulatory (
1, 2, 
1,
2, 3) AMPK subunits and exercise-induced
AMPK activity are influenced by exercise training status, muscle
biopsies were obtained from seven endurance exercise-trained and seven
sedentary young healthy men. The 1- and
2-AMPK mRNA contents in trained subjects were both
117 ± 2% of that in sedentary subjects (not significant), whereas mRNA for 3 was 61 ± 1% of that in
sedentary subjects (not significant). The level of
1-AMPK protein in trained subjects was 185 ± 34%
of that in sedentary subjects (P < 0.05), whereas the
levels of the remaining subunits (2, 1,
2, 1, 2, 3) were similar in trained and sedentary subjects. At the end of 20 min of
cycle exercise at 80% of peak O2 uptake, the increase in
phosphorylation of -AMPK (Thr172) was blunted in the
trained group (138 ± 38% above rest) compared with the sedentary
group (353 ± 63% above rest) (P < 0.05). Acetyl CoA-carboxylase -phosphorylation (Ser221), which is a
marker for in vivo AMPK activity, was increased by exercise in both
groups but to a lower level in trained subjects (32 ± 5 arbitrary
units) than in sedentary controls (45 ± 1 arbitrary units)
(P < 0.01). In conclusion, trained human skeletal
muscle has increased 1-AMPK protein levels and blunted
AMPK activation during exercise.
acetyl coenzyme A-carboxylase-; phosphocreatine; adenine
nucleotides; glycogen
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