Frontiers: skeletal muscle sodium pump regulation: a translocation paradigm.

@article{Benziane2008FrontiersSM,
  title={Frontiers: skeletal muscle sodium pump regulation: a translocation paradigm.},
  author={Boubacar Benziane and Alexander V. Chibalin},
  journal={American journal of physiology. Endocrinology and metabolism},
  year={2008},
  volume={295 3},
  pages={
          E553-8
        }
}
  • B. Benziane, A. Chibalin
  • Published 2008
  • Biology, Medicine
  • American journal of physiology. Endocrinology and metabolism
The skeletal muscle sodium pump plays a major role in the removal of K(+) ions from the circulation postprandial, or after a physical activity bout, thereby preventing the development of hyperkalemia and fatigue. Insulin and muscle contractions stimulate Na(+)-K(+)-ATPase activity in skeletal muscle, at least partially via translocation of sodium pump units to the plasma membrane from intracellular stores. The molecular mechanism of this phenomenon is poorly understood. Due to the contradictory… Expand
Na,K-ATPase regulation in skeletal muscle.
TLDR
This review focuses on molecular mechanisms that underlie regulation of NKA in skeletal muscle by major extrinsic and local stimuli, such as insulin and the energy-sensing AMP-activated protein kinase, and the recently uncovered roles for glutathionylation, nitric oxide, and extracellular K(+) in the regulation. Expand
NO turns on Na,K‐ATPase in skeletal muscle
TLDR
The finding by Juel (2015) in this issue of Acta Physiologica that nitric oxide (NO) stimulates Na,K-ATPase in skeletal muscle provides an important novel insight into how skeletal muscle fine-tunes its Na, K-ATpase. Expand
Potassium‐transporting proteins in skeletal muscle: cellular location and fibre‐type differences
TLDR
The most important protein that mediates K+ reuptake in the T‐tubules is the Na+,K+‐ATPase α2 dimers, but a significant contribution of the strong inward rectifier K+ (Kir2.1) channel is also suggested. Expand
Altered expression and insulin-induced trafficking of Na+-K+-ATPase in rat skeletal muscle: effects of high-fat diet and exercise.
TLDR
Disturbances in skeletal muscle Na(+)-K (+)-ATPase regulation, particularly the alpha(2)-subunit, may contribute to impaired ion homeostasis in insulin-resistant states such as obesity and type 2 diabetes. Expand
Influence of chronic and acute spinal cord injury on skeletal muscle Na+-K+-ATPase and phospholemman expression in humans.
TLDR
The severity of the spinal cord lesion and the level of postinjury physical activity in patients with SCI are important factors controlling the expression of Na(+)-K(+)+)-ATPase and its regulatory proteins PLM and FXYD5. Expand
Na,K-ATPase Activity in Mouse Muscle is Regulated by AMPK and PGC-1α
TLDR
Test the hypothesis that AMP kinase (AMPK) and the transcriptional coactivator PGC-1α are underlying factors in long-term regulation of Na,K-ATPase isoform (α,β and PLM) abundance and Na+ affinity and confirmed that PLM phosphorylation is important for Na, K- ATPase function. Expand
Isoform-specific functions of Na,K-ATPase in skeletal muscle
TLDR
The data that have accumulated indicate that the α1 isoform of Na,K-ATPase fulfills the major pumping function and the α2 isoform fulfills additional functions related to the specific membrane localization of the protein, the functional interactions with the proteins and lipids of the environment, and fine-tuned regulation by a variety of factors, including motor activity. Expand
Effect of exercise and training on phospholemman phosphorylation in human skeletal muscle.
TLDR
It is shown that only acute exercise, and not short-term training, increases phosphorylation of PLM on Ser(63) and Ser(68), and data from one-legged cycling indicate that this effect of exercise on PLM phosphorylated is not due to systemic factors. Expand
The role of AMPK in regulation of Na+,K+-ATPase in skeletal muscle: does the gauge always plug the sink?
TLDR
The apparent paradox of AMPK-stimulated ATP consumption is discussed, which appears to contradict the idea that AMPK maintains the cellular energy balance by always suppressing ATP-consuming processes. Expand
Membrane lipid rafts are disturbed in the response of rat skeletal muscle to short-term disuse.
TLDR
Evidence is provided to suggest that lipid raft disturbance, accompanied by intracellular Ca2+ dysregulation, is among the earliest remodeling events induced by skeletal muscle disuse, and strongly depends on motor nerve input and may involve interactions with the α2 Na-K-ATPase. Expand
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 43 REFERENCES
Role of muscle in regulating extracellular [K+].
TLDR
The K+ clamp, which measures insulin-stimulated cellular K+ uptake in vivo in the conscious rat, establishes the advantage of combining molecular analyses of Na,K-ATPase expression and activity with systems analyses of cellular K+, uptake and excretion in vivo to reveal regulatory mechanisms operating to control K+ homeostasis. Expand
Exercise increases the plasma membrane content of the Na+ -K+ pump and its mRNA in rat skeletal muscles.
TLDR
Examination of the effect of 1 h of treadmill running on the subcellular distribution and expression of Na+-K+ pump subunits in rat skeletal muscles concludes that increased presence of alpha1- and alpha2-polypeptides at the plasma membrane and subsequent elevation of the alpha1 and beta2-subunit mRNAs may be mechanisms by which acute exercise regulates the Na-k+ pump of skeletal muscle. Expand
Exercise-induced translocation of Na(+)-K(+) pump subunits to the plasma membrane in human skeletal muscle.
  • C. Juel, J. Nielsen, J. Bangsbo
  • Chemistry, Medicine
  • American journal of physiology. Regulatory, integrative and comparative physiology
  • 2000
TLDR
It is concluded that translocation of subunits is an important mechanism involved in the short time upregulation of the Na(+)-K(+) pumps in association with human muscle activity. Expand
Na+–K+ pump location and translocation during muscle contraction in rat skeletal muscle
TLDR
Muscle contraction induces translocation of the α subunits, which is suggested to be caused partly by structural changes in caveolae and partly by translocation from an intracellular pool. Expand
Insulin induces translocation of the alpha 2 and beta 1 subunits of the Na+/K(+)-ATPase from intracellular compartments to the plasma membrane in mammalian skeletal muscle.
TLDR
It is suggested that insulin induces an isoform-specific translocation of Na+ pump subunits from different intracellular sources to the PM and that the hormone-responsive enzyme in rat skeletal muscle is an alpha 2:beta 1 dimer. Expand
Na+-K+ pump regulation and skeletal muscle contractility.
  • T. Clausen
  • Chemistry, Medicine
  • Physiological reviews
  • 2003
TLDR
The Na+-K+ pump is a central target for regulation of Na-k+ distribution and excitability, essential for second-to-second ongoing maintenance of excitability during work. Expand
Reversibility of exercise-induced translocation of Na+-K+ pump subunits to the plasma membrane in rat skeletal muscle
TLDR
It is concluded that both low-intensity long-lasting running and short-lasting high-intensity contractions are able to induce a translocation of pump subunits to the sarcolemmal membrane. Expand
Insulin stimulates the translocation of Na+/K(+)-dependent ATPase molecules from intracellular stores to the plasma membrane in frog skeletal muscle.
TLDR
Findings support the view that insulin stimulates the translocation of Na+/K(+)-ATPase molecules from fraction II to the plasma membrane. Expand
Insulin-induced translocation of Na+-K+-ATPase subunits to the plasma membrane is muscle fiber type specific.
TLDR
It is concluded that the insulin-induced redistribution of the alpha 2- and beta 1-isoforms of the Na+-K+-ATPase from an intracellular pool to the plasma membrane in restricted to oxidative fiber-type skeletal muscles. Expand
Na+,K+-ATPase trafficking in skeletal muscle: insulin stimulates translocation of both alpha 1- and alpha 2-subunit isoforms.
TLDR
Insulin mediates Na(+),K(+)-ATPase alpha(1)- and alpha(2)-subunit translocation to the skeletal muscle plasma membrane via a PI 3-kinase-dependent mechanism. Expand
...
1
2
3
4
5
...