ArticleBiophysical journal2008
Effect of inorganic phosphate on the force and number of myosin cross-bridges during the isometric contraction of permeabilized muscle fibers from rabbit psoas.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.
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Who cites it
59 citing papers in PubMed, 89 citations in OpenAlex.
- Phosphate and acidosis cause fibre type-specific changes to cellular and molecular contractile mechanics at 37°C in skeletal muscle from older adults.Experimental physiology · 2026Article
- Theoretical treatment of tension transients in muscle following sudden changes in orthophosphate concentration: implications for energy transduction.Journal of muscle research and cell motility · 2025Article
- Delayed phosphate release can highly improve energy efficiency of muscle contraction.Biophysical journal · 2025Article
- The elementary step that generates force and sinusoidal analysis in striated muscle fibers.Journal of muscle research and cell motility · 2025Review
- Characterizing the concentration and load dependence of phosphate binding to rabbit fast skeletal actomyosin.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- A mechanokinetic actomyosin model predicts different orthophosphate sensitivities of force and ATP turnover rate during isometric muscle contraction.Frontiers in physiology · 2025Article
- The order of things: phosphate release or the power stroke, which does actomyosin do first?Frontiers in physiology · 2025Review
- Multiple pathways of the actin-myosin cycle in energy transduction and the release of orthophosphate in muscle.Frontiers in physiology · 2025Review
- Phosphate rebinding induces force reversal via slow backward cycling of cross-bridges.Frontiers in physiology · 2024Article
- Creatine Kinase Equilibration and ΔGInternational journal of molecular sciences · 2023Article
- The force of the myosin motor sets cooperativity in thin filament activation of skeletal muscles.Communications biology · 2022Article
- The effects of inorganic phosphate on muscle force development and energetics: challenges in modelling related to experimental uncertainties.Journal of muscle research and cell motility · 2021Article
- Phosphate has dual roles in cross-bridge kinetics in rabbit psoas single myofibrils.The Journal of general physiology · 2021Article
- Active Force Generation in Cardiac Muscle Cells: Mathematical Modeling and Numerical Simulation of the Actin-Myosin Interaction.Vietnam journal of mathematics · 2021Review
- The Location and Rate of the Phosphate Release Step in the Muscle Cross-Bridge Cycle.Biophysical journal · 2020Article
- Orthophosphate increases the efficiency of slow muscle-myosin isoform in the presence of omecamtiv mecarbil.Nature communications · 2020Article
- Are Force Enhancement after Stretch and Muscle Fatigue Due to Effects of Elevated Inorganic Phosphate and Low Calcium on Cross Bridge Kinetics?Medicina (Kaunas, Lithuania) · 2020Article
- Regulation of myofilament force and loaded shortening by skeletal myosin binding protein C.The Journal of general physiology · 2019Article
- 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
- Thick Filament Protein Network, Functions, and Disease Association.Comprehensive Physiology · 2018Review
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
The relation between the chemical and mechanical steps of the myosin-actin ATPase reaction that leads to generation of isometric force in fast skeletal muscle was investigated in demembranated fibers of rabbit psoas muscle by determining the effect of the concentration of inorganic phosphate (Pi) on the stiffness of the half-sarcomere (hs) during transient and steady-state conditions of the isometric contraction (temperature 12 degrees C, sarcomere length 2.5 mum). Changes in the hs strain were measured by imposing length steps or small 4 kHz oscillations on the fibers in control solution (without added Pi) and in solution with 3-20 mM added Pi. At the plateau of the isometric contraction in control solution, the hs stiffness is 22.8 +/- 1.1 kPa nm(-1). Taking the filament compliance into account, the total stiffness of the array of myosin cross-bridges in the hs (e) is 40.7 +/- 3.7 kPa nm(-1). An increase in [Pi] decreases the stiffness of the cross-bridge array in proportion to the isometric force, indicating that the force of the cross-bridge remains constant independently of [Pi]. The rate constant of isometric force development after a period of unloaded shortening (r(F)) is 23.5 +/- 1.0 s(-1) in control solution and increases monotonically with [Pi], attaining a maximum value of 48.6 +/- 0.9 s(-1) at 20 mM [Pi], in agreement with the idea that Pi release is a relatively fast step after force generation by the myosin cross-bridge. During isometric force development at any [Pi], e and thus the number of attached cross-bridges increase in proportion to the force, indicating that, independently of the speed of the process that leads to myosin attachment to actin, there is no significant (>1 ms) delay between generation of stiffness and generation of force by the cross-bridges.
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