ArticleBiophysical journal2002
A simple model with myofilament compliance predicts activation-dependent crossbridge kinetics in skinned skeletal fibers.
Article in Biophysical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 50 citations in OpenAlex.
- Stretch activation combats force loss from fatigue in fast-contracting mouse skeletal muscle fibers.The Journal of general physiology · 2025Article
- Disruption of Z-Disc Function Promotes Mechanical Dysfunction in Human Myocardium: Evidence for a Dual Myofilament Modulatory Role by Alpha-Actinin 2.International journal of molecular sciences · 2023Article
- Mechanical contribution to muscle thin filament activation.The Journal of biological chemistry · 2020Article
- A myosin-based mechanism for stretch activation and its possible role revealed by varying phosphate concentration in fast and slow mouse skeletal muscle fibers.American journal of physiology. Cell physiology · 2019Article
- Elastic domains of giant proteins in striated muscle: Modeling compliance with rulers.The Journal of general physiology · 2019Article
- A stochastic simulation of skeletal muscle calcium transients in a structurally realistic sarcomere model using MCell.PLoS computational biology · 2019Article
- Nebulin increases thin filament stiffness and force per cross-bridge in slow-twitch soleus muscle fibers.The Journal of general physiology · 2018Article
- Structural and functional impact of troponin C-mediated CaJournal of molecular and cellular cardiology · 2018Article
- Titin-mediated thick filament activation stabilizes myofibrils on the descending limb of their force-length relationship.Journal of sport and health science · 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
- L71F mutation in rat cardiac troponin T augments crossbridge recruitment and detachment dynamics against α-myosin heavy chain, but not against β-myosin heavy chain.Journal of muscle research and cell motility · 2016Article
- Contractile properties of developing human fetal cardiac muscle.The Journal of physiology · 2016Article
- Increased Titin Compliance Reduced Length-Dependent Contraction and Slowed Cross-Bridge Kinetics in Skinned Myocardial Strips from Rbm (20ΔRRM) Mice.Frontiers in physiology · 2016Article
- Flight capacity of Bactrocera dorsalis (Diptera: Tephritidae) adult females based on flight mill studies and flight muscle ultrastructure.Journal of insect science (Online) · 2015Article
- Significant role of female sex hormones in cardiac myofilament activation in angiotensin II-mediated hypertensive rats.The journal of physiological sciences : JPS · 2014Article
- A study of tropomyosin's role in cardiac function and disease using thin-filament reconstituted myocardium.Journal of muscle research and cell motility · 2013Review
- Effect of muscle length on cross-bridge kinetics in intact cardiac trabeculae at body temperature.The Journal of general physiology · 2013Article
- Familial hypertrophic cardiomyopathy related E180G mutation increases flexibility of human cardiac α-tropomyosin.FEBS letters · 2012Article
- Persistence length of human cardiac α-tropomyosin measured by single molecule direct probe microscopy.PloS one · 2012Article
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4 authors at 2 institutions in 1 country.
Funding
Abstract
The contribution of thick and thin filaments to skeletal muscle fiber compliance has been shown to be significant. If similar to the compliance of cycling cross-bridges, myofilament compliance could explain the difference in time course of stiffness and force during the rise of tension in a tetanus as well as the difference in Ca(2+) sensitivity of force and stiffness and more rapid phase 2 tension recovery (r) at low Ca(2+) activation. To characterize the contribution of myofilament compliance to sarcomere compliance and isometric force kinetics, the Ca(2+)-activation dependence of sarcomere compliance in single glycerinated rabbit psoas fibers, in the presence of ATP (5.0 mM), was measured using rapid length steps. At steady sarcomere length, the dependence of sarcomere compliance on the level of Ca(2+)-activated force was similar in form to that observed for fibers in rigor where force was varied by changing length. Additionally, the ratio of stiffness/force was elevated at lower force (low [Ca(2+)]) and r was faster, compared with maximum activation. A simple series mechanical model of myofilament and cross-bridge compliance in which only strong cross-bridge binding was activation dependent was used to describe the data. The model fit the data and predicted that the observed activation dependence of r can be explained if myofilament compliance contributes 60-70% of the total fiber compliance, with no requirement that actomyosin kinetics be [Ca(2+)] dependent or that cooperative interactions contribute to strong cross-bridge binding.
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