The direct molecular effects of fatigue and myosin regulatory light chain phosphorylation on the actomyosin contractile apparatus.

@article{Greenberg2010TheDM,
  title={The direct molecular effects of fatigue and myosin regulatory light chain phosphorylation on the actomyosin contractile apparatus.},
  author={M. Greenberg and T. Mealy and Michelle A Jones and D. Szczesna-Cordary and Jeffrey R. Moore},
  journal={American journal of physiology. Regulatory, integrative and comparative physiology},
  year={2010},
  volume={298 4},
  pages={
          R989-96
        }
}
Skeletal muscle, during periods of exertion, experiences several different fatigue-based changes in contractility, including reductions in force, velocity, power output, and energy usage. The fatigue-induced changes in contractility stem from many different factors, including alterations in the levels of metabolites, oxidative damage, and phosphorylation of the myosin regulatory light chain (RLC). Here, we measured the direct molecular effects of fatigue-like conditions on actomyosin's unloaded… Expand
Recent Insights into Muscle Fatigue at the Cross-Bridge Level
The effects of phosphate and acidosis on regulated thin-filament velocity in an in vitro motility assay.
The effect of skeletal myosin light chain kinase gene ablation on the fatigability of mouse fast muscle
Phosphate enhances myosin-powered actin filament velocity under acidic conditions in a motility assay.
Recent insights into the molecular basis of muscular fatigue.
  • E. Debold
  • Chemistry, Medicine
  • Medicine and science in sports and exercise
  • 2012
Myosin phosphorylation and force potentiation in skeletal muscle: evidence from animal models
Myosin phosphorylation improves contractile economy of mouse fast skeletal muscle during staircase potentiation
Phosphorylation of myosin regulatory light chain has minimal effect on kinetics and distribution of orientations of cross bridges of rabbit skeletal muscle.
  • D. Duggal, J. Nagwekar, +4 authors J. Borejdo
  • Chemistry, Medicine
  • American journal of physiology. Regulatory, integrative and comparative physiology
  • 2014
...
1
2
3
4
...

References

SHOWING 1-10 OF 63 REFERENCES
Modulation of the actomyosin interaction during fatigue of skeletal muscle
  • R. Cooke
  • Biology, Medicine
  • Muscle & nerve
  • 2007
Inhibition of shortening velocity of skinned skeletal muscle fibers in conditions that mimic fatigue.
The molecular effects of skeletal muscle myosin regulatory light chain phosphorylation.
The cross-bridge cycle and skeletal muscle fatigue.
  • R. Fitts
  • Chemistry, Medicine
  • Journal of applied physiology
  • 2008
Myosin light chain phosphorylation in vertebrate striated muscle: regulation and function.
Mechanics of actomyosin bonds in different nucleotide states are tuned to muscle contraction.
  • Bin Guo, W. Guilford
  • Chemistry, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
  • 2006
Phosphorylation of the regulatory light chains of myosin affects Ca2+ sensitivity of skeletal muscle contraction.
Changes in interfilament spacing mimic the effects of myosin regulatory light chain phosphorylation in rabbit psoas fibers.
Alteration of cross-bridge kinetics by myosin light chain phosphorylation in rabbit skeletal muscle: implications for regulation of actin-myosin interaction.
  • H. Sweeney, J. Stull
  • Chemistry, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
  • 1990
...
1
2
3
4
5
...