ArticleBiophysical journal1996
Altered kinetics of contraction in skeletal muscle fibers containing a mutant myosin regulatory light chain with reduced divalent cation binding.
Article in Biophysical journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 47 citations in OpenAlex.
- Structure and function of human muscle fibres and muscle proteome in physically active older men.The Journal of physiology · 2017Article
- Effects of cross-bridge compliance on the force-velocity relationship and muscle power output.PloS one · 2017Article
- Article
- Human skeletal muscle fibre contractile properties and proteomic profile: adaptations to 3 weeks of unilateral lower limb suspension and active recovery.The Journal of physiology · 2015Article
- Review
- Potentiation in mouse lumbrical muscle without myosin light chain phosphorylation: is resting calcium responsible?The Journal of general physiology · 2013Article
- The cardiac acetyl-lysine proteome.PloS one · 2013Article
- Understanding cardiomyopathy phenotypes based on the functional impact of mutations in the myosin motor.Circulation research · 2012Review
- The significance of regulatory light chain phosphorylation in cardiac physiology.Archives of biochemistry and biophysics · 2011Review
- In the thick of it: HCM-causing mutations in myosin binding proteins of the thick filament.Circulation research · 2011Review
- The molecular effects of skeletal muscle myosin regulatory light chain phosphorylation.American journal of physiology. Regulatory, integrative and comparative physiology · 2009Article
- Regulatory light chain mutations associated with cardiomyopathy affect myosin mechanics and kinetics.Journal of molecular and cellular cardiology · 2009Article
- Kinetics of force recovery following length changes in active skinned single fibres from rabbit psoas muscle: analysis and modelling of the late recovery phase.The Journal of physiology · 2006Article
- A point mutation in the regulatory light chain reduces the step size of skeletal muscle myosin.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- Slowing effects of Mg2+ on contractile kinetics of skinned preparations of rat hearts depending on myosin heavy chain isoform content.Pflugers Archiv : European journal of physiology · 2003Article
- Ca2+ dependence of loaded shortening in rat skinned cardiac myocytes and skeletal muscle fibres.The Journal of physiology · 2000Article
- The effect of Ca2+ on the structure of synthetic filaments of smooth muscle myosin.Journal of muscle research and cell motility · 1999Article
- Regulation of skeletal muscle tension redevelopment by troponin C constructs with different Ca2+ affinities.Biophysical journal · 1999Article
- Behavior of N-phenylmaleimide-reacted muscle fibers in magnesium-free rigor solution.Biophysical journal · 1998Article
- Phosphorylation of myosin regulatory light chain eliminates force-dependent changes in relaxation rates in skeletal muscle.Biophysical journal · 1998Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
We examined the kinetic properties of rabbit skinned skeletal muscle fibers in which the endogenous myosin regulatory light chain (RLC) was partially replaced with a mutant RLC (D47A) containing a point mutation within the Ca2+/Mg2+ binding site that severely reduced its affinity for divalent cations. We found that when approximately 50% of the endogenous RLC was replaced by the mutant, maximum tension declined to approximately 60% of control and the rate constant of active tension redevelopment (ktr) after mechanical disruption of cross-bridges was reduced to approximately 70% of control. This reduction in ktr was not an indirect effect on kinetics due to a reduced number of strongly bound myosin heads, because when the strongly binding cross-bridge analog N-ethylmaleimide-modified myosin subfragment1 (NEM-S1) was added to the fibers, there was no effect upon maximum ktr. Fiber stiffness declined after D47A exchange in a manner indicative of a decrease in the number of strongly bound cross-bridges, suggesting that the force per cross-bridge was not significantly affected by the presence of D47A RLC. In contrast to the effects on ktr, the rate of tension relaxation in steadily activated fibers after flash photolysis of the Ca2+ chelator diazo-2 increased by nearly twofold after D47A exchange. We conclude that the incorporation of the nondivalent cation-binding mutant of myosin RLC decreases the proportion of cycling cross-bridges in a force-generating state by decreasing the rate of formation of force-generating bridges and increasing the rate of detachment. These results suggest that divalent cation binding to myosin RLC plays an important role in modulating the kinetics of cross-bridge attachment and detachment.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.