title: Oral glucose ingestion attenuates exercise-induced activation of 5'-AMP-activated protein kinase in human skeletal muscle.
abstract: 5'-AMP-activated protein kinase (AMPK) has been suggested to be a 'metabolic master switch' regulating various aspects of muscle glucose and fat metabolism. In isolated rat skeletal muscle, glucose suppresses the activity of AMPK and in human muscle glycogen loading decreases exercise-induced AMPK activation. We hypothesized that oral glucose ingestion during exercise would attenuate muscle AMPK activation. Nine male subjects performed two bouts of one-legged knee-extensor exercise at 60% of maximal workload. The subjects were randomly assigned to either consume a glucose containing drink or a placebo drink during the two trials. Muscle biopsies were taken from the vastus lateralis before and after 2 h of exercise. Plasma glucose was higher (6.0 +/- 0.2 vs. 4.9 +/- 0.1 mmol L-1, P < 0.001), whereas glycerol (44.8 +/- 7.8 vs. 165.7 +/- 22.3 micromol L-1), and free fatty acid (169.3 +/- 9.5 vs. 1161 +/- 144.9 micromol L-1) concentrations were lower during the glucose compared to the placebo trial (both P < 0.001). Calculated fat oxidation was lower during the glucose trial (0.17 +/- 0.02 vs. 0.25 +/- 0.03 g min-1, P < 0.001). Activation of alpha2-AMPK was attenuated in the glucose trial compared to the placebo trial (0.24 +/- 0.07 vs. 0.46 +/- 0.14 pmol mg-1 min-1, P = 0.03), whereas the alpha1-AMPK activity was not different between trials or affected by exercise. AMPK and the downstream target of AMPK, acetyl-CoA carboxylase-beta, were phosphorylated as a response to exercise, but neither was significantly different between the two trials. We conclude that oral glucose ingestion attenuates the exercise-induced activation of alpha2-AMPK, bringing further support for a fuel-sensing role of AMPK in skeletal muscle.
authors.affiliation: The Centre of Inflammation and Metabolism, Department of Infectious Diseases, Copenhagen Muscle Research Centre, Rigshospitalet and Faculty of Health Sciences, University of Copenhagen, Copenhagen, Denmark. thorbjorn_akerstrom@inflammation-metabolism.dk
authors.forename: Thorbjorn C A
authors.initials: TC
authors.lastname: Akerstrom
authors.forename: Jesper B
authors.initials: JB
authors.lastname: Birk
authors.forename: Ditte K
authors.initials: DK
authors.lastname: Klein
authors.forename: Christian
authors.initials: C
authors.lastname: Erikstrup
authors.forename: Peter
authors.initials: P
authors.lastname: Plomgaard
authors.forename: Bente Klarlund
authors.initials: BK
authors.lastname: Pedersen
authors.forename: Jørgen
authors.initials: J
authors.lastname: Wojtaszewski
mesh_terms: D055372:AMP-Activated Protein Kinases; D000284:Administration, Oral; D000328:Adult; D004789:Enzyme Activation / Q000187:drug effects; D015444:Exercise / Q000502:physiology*; D005947:Glucose / Q000008:administration & dosage* / Q000494:pharmacology*; D006003:Glycogen / Q000378:metabolism; D006801:Humans; D008297:Male; D009097:Multienzyme Complexes / Q000378:metabolism*; D018482:Muscle, Skeletal / Q000187:drug effects* / Q000201:enzymology*; D010766:Phosphorylation; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism*; D052097:Quadriceps Muscle / Q000378:metabolism; D013997:Time Factors
chemical_list: D009097:Multienzyme Complexes; D006003:Glycogen; C526181:PRKAA2 protein, human; D017346:Protein Serine-Threonine Kinases; D055372:AMP-Activated Protein Kinases; C526180:PRKAA1 protein, human; D005947:Glucose