AMP kinase is not required for the GLUT4 response to exercise and denervation in skeletal muscle.

@article{Holmes2004AMPKI,
  title={AMP kinase is not required for the GLUT4 response to exercise and denervation in skeletal muscle.},
  author={Burton F. Holmes and David B Lang and Morris J. Birnbaum and James Mu and G. Lynis Dohm},
  journal={American journal of physiology. Endocrinology and metabolism},
  year={2004},
  volume={287 4},
  pages={
          E739-43
        }
}
An acute bout of exercise increases muscle GLUT4 mRNA in mice, and denervation decreases GLUT4 mRNA. AMP-activated protein kinase (AMPK) activity in skeletal muscle is also increased by exercise, and GLUT4 mRNA is increased in mouse skeletal muscle after treatment with AMPK activator 5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside(AICAR). These findings suggest that AMPK activation might be responsible for the increase in GLUT4 mRNA expression in response to exercise. To investigate the… 
View on PubMed
ajpendo.physiology.org
64 Citations
Highly Influential Citations
3
Background Citations
28
Methods Citations
1
Results Citations
5

Figures from this paper

64 Citations

Citation Type

Citation Type

AMPKα is essential for acute exercise-induced gene responses but not for exercise training-induced adaptations in mouse skeletal muscle.
TLDR
AMPKα1 and -α2 subunits are important for acute exercise-induced mRNA responses of some genes and may be involved in regulating basal metabolic protein expression but seem to be less important in exercise training-induced adaptations in metabolic proteins.
Reduced glycogen availability is associated with increased AMPKalpha2 activity, nuclear AMPKalpha2 protein abundance, and GLUT4 mRNA expression in contracting human skeletal muscle.
  • G. Steinberg, M. Watt, +5 authors B. Kemp
  • Biology
    Applied physiology, nutrition, and metabolism = Physiologie appliquee, nutrition et metabolisme
  • 2006
TLDR
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.
Role of AMPKalpha2 in basal, training-, and AICAR-induced GLUT4, hexokinase II, and mitochondrial protein expression in mouse muscle.
TLDR
The alpha2-KO was associated with an approximately 20% reduction in mitochondrial markers in both muscle types and abolished AICAR-induced increases in protein expression in WG, suggesting that AMPKalpha2 may not be essential for metabolic adaptations of skeletal muscles to exercise training.
GLUT4 is not essential for exercise-induced exaggerated muscle glycogen degradation in AMPKα2 knockout mice
Skeletal muscle and heart LKB1 deficiency causes decreased voluntary running and reduced muscle mitochondrial marker enzyme expression in mice.
TLDR
Evidence is provided for a critical role of LKB1 in muscle physiology, one of which is maintaining basal levels of mitochondrial oxidative enzymes, and that it is essential for maintaining mitochondrial marker proteins in skeletal muscle.
Role of AMPK in skeletal muscle gene adaptation in relation to exercise.
TLDR
Although decreased AMPK activity in muscle causes reduced protein expression of mitochondrial enzymes in the basal state, AMPK does not appear to be indispensable for exercise-training induced increase in mitochondrial enzyme expression.
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.
Regulation of GLUT4 expression in denervated skeletal muscle.
  • E. B. Jensen, D. Zheng, +4 authors G. Dohm
  • Biology
    American journal of physiology. Regulatory, integrative and comparative physiology
  • 2009
TLDR
The findings indicate that withdrawal of a GEF- or MEF2-dependent signal is not likely a major determinant of the denervation effect on GLUT4 expression, and the response to denervation may be mediated by other elements present in the basal promoter of theGLUT4 gene.
Multiple signalling pathways redundantly control glucose transporter GLUT4 gene transcription in skeletal muscle
TLDR
The results point to a muscle type‐specific and redundant regulation of GLUT4 enhancer based on the interplay of multiple signalling pathways, all of which are known to affect myocyte enhancing factor 2 (MEF2) transcriptional activity, a point of convergence of different pathways on muscle gene regulation.
How is AMPK activity regulated in skeletal muscles during exercise?
TLDR
The role of LKB1 and phosphatase PP2C in nucleotide-dependent activation of AMPK, and ionized calcium in CaMKK-dependent activated AMPK in working muscle is discussed and the influence of reactive oxygen species produced within the muscle as well as muscle glycogen and TAK1 in regulating AMPK during exercise is discussed.
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 37 REFERENCES
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.
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.
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.
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.
Effects of AICAR and exercise on insulin-stimulated glucose uptake, signaling, and GLUT-4 content in rat muscles.
TLDR
Chronic AICAR administration and long-term exercise both improve insulin-stimulated glucose transport in skeletal muscle in a fiber-type-specific way, and this is associated with an increase in GLUT-4 content.
AMP-activated protein kinase (AMPK) is activated in muscle of subjects with type 2 diabetes during exercise.
TLDR
People with type 2 diabetes have normal exercise-induced AMPK alpha2 activity and normal expression of the alpha1, alpha2 and beta1 isoforms and Pharmacological activation of AMPK may be an attractive target for the treatment of type 2abetes.
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.
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.
Time course of GLUT4 and AMPK protein expression in human skeletal muscle during one month of physical training
TLDR
GLUT4 protein expression increases substantially after seven days of endurance training with no further increase with prolonged training at progressively increasing workloads, while AMPKα1 and α2 behave differently in their expression in response to endurance training.
Effect of denervation on the expression of two glucose transporter isoforms in rat hindlimb muscle.
TLDR
The data suggest that the insulin resistance of glucose transport early after denervation does not reflect a decrease in total glucose transporter number; however, decreased GLUT-4 expression may contribute to its increased severity after 3 d.
...
1
2
3
4
...