Regulation of 5'AMP-activated protein kinase activity and substrate utilization in exercising human skeletal muscle.

@article{Wojtaszewski2003RegulationO5,
  title={Regulation of 5'AMP-activated protein kinase activity and substrate utilization in exercising human skeletal muscle.},
  author={J{\o}rgen F. P. Wojtaszewski and Christopher MacDonald and J Nielsen and Ylva Hellsten and David Grahame Hardie and Bruce E. Kemp and Bente Kiens and Erik A. Richter},
  journal={American journal of physiology. Endocrinology and metabolism},
  year={2003},
  volume={284 4},
  pages={
          E813-22
        }
}
The metabolic role of 5'AMP-activated protein kinase (AMPK) in regulation of skeletal muscle metabolism in humans is unresolved. We measured isoform-specific AMPK activity and beta-acetyl-CoA carboxylase (ACCbeta) Ser(221) phosphorylation and substrate balance in skeletal muscle of eight athletes at rest, during cycling exercise for 1 h at 70% peak oxygen consumption, and 1 h into recovery. The experiment was performed twice, once in a glycogen-loaded (glycogen concentration approximately 900… 

Figures and Tables from this paper

AMP‐activated protein kinase in contraction regulation of skeletal muscle metabolism: necessary and/or sufficient?

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.

Interleukin-6 release from human skeletal muscle during exercise: relation to AMPK activity.

The present data are compatible with a role for AMPK in IL-6 release during exercise or a role in activating AMPK, either of which are independent sensors of a low muscle glycogen concentration during exercise.

5’ Adenosine Monophosphate-Activated Protein Kinase, Metabolism and Exercise

This review discusses the putative roles of AMPK in acute and chronic exercise responses, and suggests avenues for future AMPK research in exercise physiology and biochemistry.

Reduced glycogen availability is associated with increased AMPKalpha2 activity, nuclear AMPKalpha2 protein abundance, and GLUT4 mRNA expression in contracting human skeletal muscle.

  • G. SteinbergM. Watt B. Kemp
  • Biology
    Applied physiology, nutrition, and metabolism = Physiologie appliquee, nutrition et metabolisme
  • 2006
It is suggested that increased activation of AMPK alpha2 under conditions of low muscle glycogen enhances AM PK alpha2 nuclear translocation and increases GLUT4 mRNA expression in response to exercise in human skeletal muscle.

Skeletal muscle basal AMP-activated protein kinase activity is chronically elevated in alloxan-diabetic dogs: impact of exercise.

Elevated preexercise SkM AMPKalpha1 and -alpha2 activities contribute to the ongoing basal supply of glucose and fatty acid metabolism in suboptimally controlled hypoinsulinemic diabetic dogs; but whether they also play a permissive role in the metabolic stress response to exercise remains uncertain.

Intensified exercise training does not alter AMPK signaling in human skeletal muscle.

It is indicated that, in well-trained individuals, short-term HIT improves metabolic control but does not blunt AMPK signaling in response to intense exercise.

Genetic impairment of AMPKalpha2 signaling does not reduce muscle glucose uptake during treadmill exercise in mice.

Findings suggest that AMPKalpha2 signaling is not essential in regulating glucose uptake in mouse skeletal muscle during treadmill exercise and that other mechanisms play a central role.

Skeletal Muscle Eukaryotic Elongation Factor 2 (eEF2) Response to Acute Resistance Exercise in Young and Old Men and Women : Relationship to Muscle Glycogen Content and 5'-AMP-Activated Protein Kinase (AMPK) Activity

It is suggested that higher muscle glycogen content may result in lower AMPK activation and consequently lower inhibitory eEF2 phosphorylation in response to a resistance training session in the muscles of both younger and older individuals thereby potentially enabling greater translation elongation protein synthesis and muscle growth regardless of age.

AMP-Activated Protein Kinase in the Heart: Role During Health and Disease

AMP-activated protein kinase is a heterotrimeric enzyme that is expressed in most mammalian tissues including cardiac muscle, suggesting involvement in a number of human disorders including cardiac hypertrophy, apoptosis, cancer, and atherosclerosis.
...

References

SHOWING 1-10 OF 65 REFERENCES

Exercise induces isoform-specific increase in 5'AMP-activated protein kinase activity in human skeletal muscle.

Exercise at a higher intensity for only 20 min leads to increases in AMPK alpha2 activity but not alpha1 activity, suggesting that the alpha2-containing AMPK complex, rather than alpha1, may be involved in the metabolic responses to exercise in human skeletal muscle.

AMPK signaling in contracting human skeletal muscle: acetyl-CoA carboxylase and NO synthase phosphorylation.

Observations support the concept that inhibition of ACC is an important component in stimulating fatty acid oxidation in response to exercise and that there is coordinated regulation of nNOSmu to protect the muscle from ischemia/metabolic stress.

AMP-activated protein kinase activity and glucose uptake in rat skeletal muscle.

Tetanic contractions of isolated epitrochlearis muscles in vitro significantly increased the activity of both AMPK isoforms in a dose-dependent manner and at a similar rate compared with increases in 3-MG uptake, suggesting the activation of AMPK alpha 2-containing complexes may be more important in regulating exercise-mediated skeletal muscle metabolism in vivo.

Dissociation of AMP-activated protein kinase activation and glucose transport in contracting slow-twitch muscle.

In slow-twitch muscles, high glycogen levels inhibit contraction-induced AMPK activation without affecting glucose transport, suggesting that AM PK activation is not an essential signaling step in glucose transport stimulation in skeletal muscle.

Dissociation of AMPK activity and ACCbeta phosphorylation in human muscle during prolonged exercise.

Progressive increase in human skeletal muscle AMPKalpha2 activity and ACC phosphorylation during exercise.

AMPKalpha2 activity and ACCbeta phosphorylation increase progressively during moderate exercise at approximately 60% of VO(2 peak) in humans, with these responses more closely coupled to muscle glycogen content than muscle AMP/ATP ratio.

5'-AMP-activated protein kinase activity and subunit expression in exercise-trained human skeletal muscle.

In conclusion, trained human skeletal muscle has increased alpha(1)-AMPK protein levels and blunted AMPK activation during exercise.

Evidence for 5′AMP-Activated Protein Kinase Mediation of the Effect of Muscle Contraction on Glucose Transport

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.

AMP kinase activation ameliorates insulin resistance induced by free fatty acids in rat skeletal muscle.

  • G. S. OlsenB. Hansen
  • Biology, Chemistry
    American journal of physiology. Endocrinology and metabolism
  • 2002
The mechanism by which AMPK activation ameliorates the lipid-induced insulin resistance probably involves induction of compensatory mechanisms overriding the insulin resistance.

Metabolic stress and altered glucose transport: activation of AMP-activated protein kinase as a unifying coupling mechanism.

The activation of AMPK may be a common mechanism leading to insulin-independent glucose transport in skeletal muscle under conditions of metabolic stress, and this hypothesis is tested under several conditions that evoke metabolic stress accompanied by intracellular fuel depletion.
...