Skeletal muscle adaptation to exercise training: AMP-activated protein kinase mediates muscle fiber type shift

Diabetes. 2007 Aug;56(8):2062-9. doi: 10.2337/db07-0255. Epub 2007 May 18.

Abstract

Regular endurance exercise has profound benefits on overall health, including the prevention of obesity, cardiovascular disease, and diabetes. The objective of this study was to determine whether AMP-activated protein kinase (AMPK) mediates commonly observed adaptive responses to exercise training in skeletal muscle. Six weeks of voluntary wheel running induced a significant (P < 0.05) fiber type IIb to IIa/x shift in triceps muscle of wild-type mice. Despite similar wheel running capacities, this training-induced shift was reduced by approximately 40% in transgenic mice expressing a muscle-specific AMPKalpha2 inactive subunit. Sedentary mice carrying an AMPK-activating mutation (gamma1TG) showed a 2.6-fold increase in type IIa/x fibers but no further increase with training. To determine whether AMPK is involved in concomitant metabolic adaptations to training, we measured markers of mitochondria (citrate synthase and succinate dehydrogenase) and glucose uptake capacity (GLUT4 and hexokinase II). Mitochondrial markers increased similarly in wild-type and AMPKalpha2-inactive mice. Sedentary gamma1TG mice showed a approximately 25% increase in citrate synthase activity but no further increase with training. GLUT4 protein expression was not different in either line of transgenic mice compared with wild-type mice and tended to increase with training, although this increase was not statistically significant. Training induced a approximately 65% increase in hexokinase II protein in wild-type mice but not in AMPKalpha2-inactive mice. Hexokinase II was significantly elevated in sedentary gamma1TG mice, without an additional increase with training. AMPK is not necessary for exercise training-induced increases in mitochondrial markers, but it is essential for fiber type IIb to IIa/x transformation and increases in hexokinase II protein.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • AMP-Activated Protein Kinases
  • Adaptation, Biological*
  • Animals
  • Biomarkers / metabolism
  • Gene Expression Regulation, Enzymologic
  • Glucose Transporter Type 4 / metabolism
  • Hexokinase / metabolism
  • Mice
  • Mice, Transgenic
  • Mitochondrial Proteins / metabolism
  • Multienzyme Complexes / genetics
  • Multienzyme Complexes / metabolism*
  • Muscle, Skeletal / enzymology*
  • Mutation / genetics
  • Myosin Heavy Chains / metabolism
  • Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha
  • Physical Conditioning, Animal
  • Protein Serine-Threonine Kinases / genetics
  • Protein Serine-Threonine Kinases / metabolism*
  • Protein Subunits / genetics
  • Protein Subunits / metabolism
  • Trans-Activators / metabolism
  • Transcription Factors

Substances

  • Biomarkers
  • Glucose Transporter Type 4
  • Mitochondrial Proteins
  • Multienzyme Complexes
  • Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha
  • Ppargc1a protein, mouse
  • Protein Subunits
  • Slc2a4 protein, mouse
  • Trans-Activators
  • Transcription Factors
  • Hexokinase
  • Protein Serine-Threonine Kinases
  • AMP-Activated Protein Kinases
  • Myosin Heavy Chains