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AICA riboside increases AMP-activated protein kinase, fatty acid oxidation, and glucose uptake in rat muscle.
TLDR
Evidence is provided that decreases in muscle content of malonyl-CoA can increase the rate of fatty acid oxidation, and perfusion with medium containing AICAR was found to activate AMPK in skeletal muscle, inactivate ACC, and decrease malony l-coA.
AMP-activated protein kinase, a metabolic master switch: possible roles in Type 2 diabetes.
  • W. Winder, D. Hardie
  • Biology, Medicine
    American journal of physiology. Endocrinology and…
  • 1 July 1999
TLDR
Increased recruitment of the AMPK signaling system, either by exercise or pharmaceutical activators, may be effective in correcting insulin resistance in patients with forms of impaired glucose tolerance and Type 2 diabetes resulting from defects in the insulin signaling cascade.
Inactivation of acetyl-CoA carboxylase and activation of AMP-activated protein kinase in muscle during exercise.
  • W. Winder, D. Hardie
  • Biology, Computer Science
    The American journal of physiology
  • 1 February 1996
TLDR
The activation of the AMP-activated protein kinase with consequent phosphorylation and inactivation of ACC may be one of the primary events in the control of malonyl-CoA and hence fatty acid oxidation during exercise.
Activation of AMP-activated protein kinase increases mitochondrial enzymes in skeletal muscle.
TLDR
The results suggest that chronic AMPK activation may mediate the effects of muscle contraction on some, but not all, biochemical adaptations of muscle to endurance exercise training.
Evidence for 5′AMP-Activated Protein Kinase Mediation of the Effect of Muscle Contraction on Glucose Transport
TLDR
Data suggest that AICAR and contraction stimulate glucose transport by a similar insulin-independent signaling mechanism and are consistent with the hypothesis that AMPK is involved in exercise-stimulated glucose uptake.
Chronic activation of 5'-AMP-activated protein kinase increases GLUT-4, hexokinase, and glycogen in muscle.
TLDR
Chronic chemical activation of AMPK results in increases in GLUT-4 protein, hexokinase activity, and glycogen, similarly to those induced by endurance training.
Energy-sensing and signaling by AMP-activated protein kinase in skeletal muscle.
  • W. Winder
  • Biology
    Journal of applied physiology
  • 1 September 2001
TLDR
It appears that AMPK has the capability of monitoring intramuscular energy charge and then acutely stimulating fat oxidation and glucose uptake to counteract the increased rates of ATP utilization during muscle contraction.
Phosphorylation-activity relationships of AMPK and acetyl-CoA carboxylase in muscle.
TLDR
Data provide the first evidence of a direct link between extent of phosphorylation of these proteins at sites recognized by the antibodies and activity of the enzymes in electrically stimulated muscle and in muscle of rats running on the treadmill.
AMP-activated protein kinase phosphorylates transcription factors of the CREB family.
TLDR
CREB and related proteins are direct downstream targets for AMPK and are therefore likely involved in mediating some effects of AMPK on expression of genes having a CRE in their promoters.
Regulation of muscle GLUT-4 transcription by AMP-activated protein kinase.
TLDR
AMP-activated protein kinase activation by AICAR increases GLut-4 transcription by a mechanism that requires response elements within 895 bp of human GLUT-4 proximal promoter and that may be cooperatively mediated by myocyte enhancer factor-2.
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