ArticleBiophysical journal2010
Is the cross-bridge stiffness proportional to tension during muscle fiber activation?
Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
- Effects of chemical myosin II cross-bridge inhibitors on eccentric force production in skinned muscle fibres.Experimental physiology · 2026Article
- The Mechanism of Modulation of Cardiac Force by Temperature.International journal of molecular sciences · 2025Article
- Effects of shortening velocity on the stiffness to force ratio during isometric force redevelopment suggest mechanisms of residual force depression.Scientific reports · 2023Article
- Three-dimensional mapping of ultrasound-derived skeletal muscle shear wave velocity.Frontiers in bioengineering and biotechnology · 2023Article
- Cross-bridge mechanics estimated from skeletal muscles' work-loop responses to impacts in legged locomotion.Scientific reports · 2021Article
- Changes in the Viscoelastic Properties of theFrontiers in physiology · 2020Article
- Directional Dependence of Experimental Trunk Stiffness: Role of Muscle-Stiffness Variation of Nonneural Origin.Applied bionics and biomechanics · 2020Article
- Myosin Cross-Bridge Behaviour in Contracting Muscle-The TInternational journal of molecular sciences · 2019Article
- A mechanical model of the half-sarcomere which includes the contribution of titin.Journal of muscle research and cell motility · 2019Article
- Nonlinear Actomyosin Elasticity in Muscle?Biophysical journal · 2019Article
- Thick-Filament Extensibility in Intact Skeletal Muscle.Biophysical journal · 2018Article
- The force and stiffness of myosin motors in the isometric twitch of a cardiac trabecula and the effect of the extracellular calcium concentration.The Journal of physiology · 2018Article
- Mechanical parameters of the molecular motor myosin II determined in permeabilised fibres from slow and fast skeletal muscles of the rabbit.The Journal of physiology · 2018Article
- Effects of myosin inhibitors on the X-ray diffraction patterns of relaxed and calcium-activated rabbit skeletal muscle fibers.Biophysics and physicobiology · 2018Article
- Phosphate increase during fatigue affects crossbridge kinetics in intact mouse muscle at physiological temperature.The Journal of physiology · 2017Article
- Force and number of myosin motors during muscle shortening and the coupling with the release of the ATP hydrolysis products.The Journal of physiology · 2015Article
- High ionic strength depresses muscle contractility by decreasing both force per cross-bridge and the number of strongly attached cross-bridges.Journal of muscle research and cell motility · 2015Article
- Poorly understood aspects of striated muscle contraction.BioMed research international · 2015Review
- Phosphate and acidosis act synergistically to depress peak power in rat muscle fibers.American journal of physiology. Cell physiology · 2014Article
- The contributions of filaments and cross-bridges to sarcomere compliance in skeletal muscle.The Journal of physiology · 2014Article
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The cross-bridge stiffness can be used to estimate the number of S1 that are bound to actin during contraction, which is a critical parameter for elucidating the fundamental mechanism of the myosin motor. At present, the development of active tension and the increase in muscle stiffness due to S1 binding to actin are thought to be linearly related to the number of cross-bridges formed upon activation. The nonlinearity of total stiffness with respect to active force is thought to arise from the contribution of actin and myosin filament stiffness to total sarcomere elasticity. In this work, we reexamined the relation of total stiffness to tension during activation and during exposure to N-benzyl-p-toluene sulphonamide, an inhibitor of cross-bridge formation. In addition to filament and cross-bridge elasticity, our findings are best accounted for by the inclusion of an extra elasticity in parallel with the cross-bridges, which is formed upon activation but is insensitive to the subsequent level of cross-bridge formation. By analyzing the rupture tension of the muscle (an independent measure of cross-bridge formation) at different levels of activation, we found that this additional elasticity could be explained as the stiffness of a population of no-force-generating cross-bridges. These findings call into question the assumption that active force development can be taken as directly proportional to the cross-bridge number.
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