Activation of AMP-activated protein kinase increases mitochondrial enzymes in skeletal muscle.

@article{Winder2000ActivationOA,
  title={Activation of AMP-activated protein kinase increases mitochondrial enzymes in skeletal muscle.},
  author={William W. Winder and Burton F. Holmes and D. S. Rubink and Ellis B. Jensen and M M Chen and John O. Holloszy},
  journal={Journal of applied physiology},
  year={2000},
  volume={88 6},
  pages={
          2219-26
        }
}
Muscle contraction causes an increase in activity of 5'-AMP-activated protein kinase (AMPK). This study was designed to determine whether chronic chemical activation of AMPK will increase mitochondrial enzymes, GLUT-4, and hexokinase in different types of skeletal muscle of resting rats. In acute studies, rats were subcutaneously injected with either 5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside (AICAR; 1 mg/g body wt) in 0.9% NaCl or with 0.9% NaCl alone and were then anesthetized for… 
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Evidence supporting a necessary and/or sufficient role of AMPK in a broad spectrum of skeletal muscle contraction‐relevant processes, including glucose uptake, glycogen synthesis, post‐exercise insulin sensitivity, fatty acid (FA) uptake, intramuscular triacylglyceride hydrolysis, FA oxidation, suppression of protein synthesis, proteolysis, autophagy and transcriptional regulation of genes relevant to promoting an oxidative phenotype are critically examined.
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AICAR treatment does not promote glycogen accumulation in skeletal muscle in vivo by altering glycogen synthase and glycogen phosphorylase, and the increased glycogen is due to the well-known effects of AICAR to increase glucose uptake.
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