Glucose restriction inhibits skeletal myoblast differentiation by activating SIRT1 through AMPK-mediated regulation of Nampt.

@article{Fulco2008GlucoseRI,
  title={Glucose restriction inhibits skeletal myoblast differentiation by activating SIRT1 through AMPK-mediated regulation of Nampt.},
  author={M. Fulco and Y. Cen and P. Zhao and E. Hoffman and M. McBurney and A. Sauve and V. Sartorelli},
  journal={Developmental cell},
  year={2008},
  volume={14 5},
  pages={
          661-73
        }
}
It is intuitive to speculate that nutrient availability may influence differentiation of mammalian cells. Nonetheless, a comprehensive complement of the molecular determinants involved in this process has not been elucidated yet. Here, we have investigated how nutrients (glucose) affect skeletal myogenesis. Glucose restriction (GR) impaired differentiation of skeletal myoblasts and was associated with activation of the AMP-activated protein kinase (AMPK). Activated AMPK was required to promote… Expand
AMPK inhibits myoblast differentiation through a PGC-1alpha-dependent mechanism.
TLDR
It is demonstrated that AICAR-induced AMPK phosphorylation inhibits cell cycle transition, reducing differentiation of myoblasts into myotubes, through PGC-1alpha-FOXO3A-p21. Expand
The AMPK-SIRT signaling network regulates glucose tolerance under calorie restriction conditions.
TLDR
It is demonstrated that skeletal muscle-specific AMPK deficiency impairs the beneficial effects of CR on glucose tolerance and that these effects may be dependent on reduced SIRT1 levels. Expand
Concurrent regulation of AMP-activated protein kinase and SIRT1 in mammalian cells.
TLDR
Findings raise the possibility that glucose-induced changes in AMPK are linked to alterations in SIRT1 abundance and activity and possibly cellular redox state. Expand
Diet and exercise signals regulate SIRT3 and activate AMPK and PGC-1α in skeletal muscle
TLDR
It is reported here that SIRT3 responds dynamically to both exercise and nutritional signals in skeletal muscle to coordinate downstream molecular responses, and it is shown that exercise training increases Sirt3 expression as well as associated CREB phosphorylation and PGC-1α up-regulation. Expand
AMP-activated protein kinase stimulates myostatin expression in C2C12 cells.
  • A. Das, Qiyuan Yang, +5 authors M. Du
  • Chemistry, Medicine
  • Biochemical and biophysical research communications
  • 2012
TLDR
Results indicate that AMPK stimulates myostatin expression in C2C12 cells, providing an explanation for the negative effect of AMPK on muscle growth. Expand
AMPK regulates energy expenditure by modulating NAD+ metabolism and SIRT1 activity
TLDR
It is demonstrated that AMPK controls the expression of genes involved in energy metabolism in mouse skeletal muscle by acting in coordination with another metabolic sensor, the NAD+-dependent type III deacetylase SIRT1. Expand
NAMPT regulates mitochondria biogenesis via NAD metabolism and calcium binding proteins during skeletal muscle contraction
TLDR
The results indicated that the AMPK-NAMPT signal is a key player for muscle contraction induced SIRT1 expression and PGC-1α deacetylation, which influences mitochondrial biogenesis. Expand
Specific Sirt1 Activator-mediated Improvement in Glucose Homeostasis Requires Sirt1-Independent Activation of AMPK
TLDR
It is shown that SRT1720 activates AMPK in a Sirt1-independent manner and S RT1720 activating AMPK by inhibiting a cAMP degrading phosphodiesterase (PDE) in a competitive manner and weight loss induced by SRT 1720 is not sufficient to improve glucose tolerance. Expand
Interdependence of AMPK and SIRT1 for metabolic adaptation to fasting and exercise in skeletal muscle.
TLDR
It is concluded that AMPK acts as the primordial trigger for fasting- and exercise-induced adaptations in skeletal muscle and that activation of SIRT1 and its downstream signaling pathways are improperly triggered in AMPK-deficient states. Expand
The Role of AMPK in the Regulation of Skeletal Muscle Size, Hypertrophy, and Regeneration
  • D. M. Thomson
  • Biology, Medicine
  • International journal of molecular sciences
  • 2018
TLDR
The current data indicate that AMPK does play an important role in regulating muscle mass and regeneration, with AMPKα1 playing a prominent role in stimulating anabolism and in regulating satellite cell dynamics during regeneration, and AM PKα2 playing a potentially more important role on regulating muscle degradation during atrophy. Expand
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 79 REFERENCES
A role for AMP-activated protein kinase in contraction- and hypoxia-regulated glucose transport in skeletal muscle.
TLDR
Data indicate that AMPK transmits a portion of the signal by which muscle contraction increases glucose uptake, but other AMPK-independent pathways also contribute to the response. Expand
Nutrient control of glucose homeostasis through a complex of PGC-1α and SIRT1
TLDR
It is shown that the Sir2 homologue, SIRT1 controls the gluconeogenic/glycolytic pathways in liver in response to fasting signals through the transcriptional coactivator PGC-1α, and this findings have strong implications for the basic pathways of energy homeostasis, diabetes and lifespan. Expand
AMP-activated protein kinase (AMPK) action in skeletal muscle via direct phosphorylation of PGC-1α
Activation of AMP-activated kinase (AMPK) in skeletal muscle increases glucose uptake, fatty acid oxidation, and mitochondrial biogenesis by increasing gene expression in these pathways. However, theExpand
Sir2 regulates skeletal muscle differentiation as a potential sensor of the redox state.
TLDR
Results indicate that Sir2 regulates muscle gene expression and differentiation by possibly functioning as a redox sensor in response to exercise, food intake, and starvation, Sir2 may sense modifications of the redox state and promptly modulate gene expression. Expand
The Energy Sensor AMP-activated Protein Kinase Directly Regulates the Mammalian FOXO3 Transcription Factor*
TLDR
It is found that AMPK directly regulates mammalian FOXO3, a member of the FOXO family of Forkhead transcription factors known to promote resistance to oxidative stress, tumor suppression, and longevity, by phosphorylation by AMPK at six previously unidentified regulatory sites. Expand
Chronic activation of AMP-activated kinase as a strategy for slowing aging.
TLDR
The development of AMPK activators which do not share metformin's modest risk of inducing lactic acidosis--apparently reflecting an inhibition of mitochondrial complex 1 that is not intrinsic to AMPK activity--might aid the practical applicability of this pro-longevity strategy. Expand
Resveratrol stimulates AMP kinase activity in neurons
TLDR
It is shown that resveratrol activated AMPK in Neuro2a cells and primary neurons in vitro as well as in the brain, suggesting that neuronal activation of AMPK by resver atrol could affect neuronal energy homeostasis and contribute to the neuroprotective effects of resverAtrol. Expand
SIRT1 Functionally Interacts with the Metabolic Regulator and Transcriptional Coactivator PGC-1α*
TLDR
The cellular effects of overexpression of SIRT1, the closest mammalian ortholog of Sir2, are examined and it is demonstrated that SIRT 1 catalyzes PGC-1α deacetylation both in vitro and in vivo. Expand
Sirt1 promotes fat mobilization in white adipocytes by repressing PPAR-γ
TLDR
It is shown that the mammalian SIR2 orthologue, Sirt1 (sirtuin 1), activates a critical component of calorie restriction in mammals; that is, fat mobilization in white adipocytes. Expand
Role of AMP-activated protein kinase in mechanism of metformin action.
TLDR
It is reported that metformin activates AMPK in hepatocytes; as a result, acetyl-CoA carboxylase (ACC) activity is reduced, fatty acid oxidation is induced, and expression of lipogenic enzymes is suppressed. Expand
...
1
2
3
4
5
...