Chronic activation of 5'-AMP-activated protein kinase increases GLUT-4, hexokinase, and glycogen in muscle.

@article{Holmes1999ChronicAO,
  title={Chronic activation of 5'-AMP-activated protein kinase increases GLUT-4, hexokinase, and glycogen in muscle.},
  author={Burton F. Holmes and E J Kurth-Kraczek and William W. Winder},
  journal={Journal of applied physiology},
  year={1999},
  volume={87 5},
  pages={
          1990-5
        }
}
This study was designed to determine whether chronic chemical activation of AMP-activated protein kinase (AMPK) would increase glucose transporter GLUT-4 and hexokinase in muscles similarly to periodic elevation of AMPK that accompanies endurance exercise training. The adenosine analog, 5-aminoimidazole-4-carboxamide ribonucleoside (AICAR), has previously been shown to be taken up by cells and phosphorylated to form a compound (5-aminoimidazole-4-carboxamide ribonucleotide) that mimics the… 

Figures and Tables from this paper

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.
Effect of acute activation of 5'-AMP-activated protein kinase on glycogen regulation in isolated rat skeletal muscle.
TLDR
The results suggest that AMPK does not mediate contraction- Stimulated glycogen synthesis or glycogenolysis in skeletal muscle and also that acute AMPK activation leads to an increased glycolytic flux by antagonizing contraction-stimulated glycogens synthesis.
AMP-activated protein kinase activates transcription of the UCP3 and HKII genes in rat skeletal muscle.
TLDR
Evidence is provided that AMPK signaling is linked to the transcriptional regulation of select metabolic genes in skeletal muscle by a single-leg arterial infusion technique employed in fully conscious rats.
Increased expression of GLUT-4 and hexokinase in rat epitrochlearis muscles exposed to AICAR in vitro.
TLDR
Examination of the effect of incubating rat epitrochlearis muscles in culture medium in the presence or absence of 5-aminoimidazole-4-carboxamide ribonucleoside (AICAR) provides strong evidence in support of the hypothesis that the activation of AMPK that occurs in muscle during exercise is involved in mediating the adaptive increases in GLUT-4 and hexokinase.
AMP-activated protein kinase activation prevents denervation-induced decline in gastrocnemius GLUT-4.
TLDR
Evidence is provided that some effects of denervation may be prevented by chemical activation of the appropriate signaling pathways as well as the extent ofDenervation-induced muscle atrophy was similar in AICAR-treated vs. saline-treated rats.
Glycogen-dependent effects of 5-aminoimidazole-4-carboxamide (AICA)-riboside on AMP-activated protein kinase and glycogen synthase activities in rat skeletal muscle.
TLDR
It is concluded that acute AICA-riboside treatment leads to phosphorylation and deactivation of glycogen synthase in skeletal muscle and may be a target for AMPK in vivo.
Chronic activation of 5'-AMP-activated protein kinase changes myosin heavy chain expression in growing pigs.
TLDR
Results indicate that activation of AMPK by AICAR causes muscle to assume a faster-contracting, more glycolytic nature.
Activation of AMP kinase enhances sensitivity of muscle glucose transport to insulin.
TLDR
Results provide evidence that the increase in insulin sensitivity of muscle glucose transport that follows exercise is mediated by activation of AMPK and involves a step beyond PKB in the pathway by which insulin stimulates glucose transport.
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.
...
...

References

SHOWING 1-10 OF 38 REFERENCES
5' AMP-activated protein kinase activation causes GLUT4 translocation in skeletal muscle.
TLDR
Evidence is provided that the increased glucose uptake observed with AMPK activation by AICA-riboside in perfused rat hindlimb muscles is due to an increase in the translocation of GLUT4 to surface membranes.
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.
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.
Inactivation of acetyl-CoA carboxylase and activation of AMP-activated protein kinase in muscle during exercise.
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.
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 metabolism
  • 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.
Exercise induces a transient increase in transcription of the GLUT-4 gene in skeletal muscle.
TLDR
It is proposed that the increase in GLut-4 mRNA evident with extended periods of training may result from a shift to pretranslational control and is the cumulative effect of repeated postexercise transient increases in GLUT-4 gene transcription.
Exercise training reverses insulin resistance in muscle by enhanced recruitment of GLUT-4 to the cell surface.
TLDR
Training improves insulin-stimulated glucose transport in muscle of the obese Zucker rat by increasing GLUT-4 content and by altering the normal intracellular distribution of these transporters such that they are now capable of migrating to the cell surface in response to the insulin stimulus.
Exercise induces rapid increases in GLUT4 expression, glucose transport capacity, and insulin-stimulated glycogen storage in muscle.
TLDR
The results show that a rapid increase in GLUT4 expression is an early adaptive response of muscle to exercise and appears to be mediated by pretranslational mechanisms that enhance replenishment of muscle glycogen stores.
The AMP-activated/SNF1 protein kinase subfamily: metabolic sensors of the eukaryotic cell?
TLDR
AMP-activated protein kinase and SNF1-related protein kinases in higher plants are likely to be involved in the response of plant cells to environmental and/or nutritional stress.
Rapid reversal of adaptive increases in muscle GLUT-4 and glucose transport capacity after training cessation.
TLDR
The results support the conclusion that the rapid reversal of the increase in the insulin responsiveness of muscle glucose transport after cessation of training is explained by the short half-life of the GLUT-4 protein.
...
...