ArticleBiophysical journal2007
Nonlinear force-length relationship in the ADP-induced contraction of skeletal myofibrils.
Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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25 citing papers in PubMed, 40 citations in OpenAlex.
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- Myosin and tropomyosin-troponin complementarily regulate thermal activation of muscles.The Journal of general physiology · 2023Article
- Nanoscopic changes in the lattice structure of striated muscle sarcomeres involved in the mechanism of spontaneous oscillatory contraction (SPOC).Scientific reports · 2020Article
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- Radial stiffness characteristics of the overlap regions of sarcomeres in isolated skeletal myofibrils in pre-force generating state.Biophysics and physicobiology · 2017Article
- A Beetle Flight Muscle Displays Leg Muscle Microstructure.Biophysical journal · 2016Article
- Force per cross-sectional area from molecules to muscles: a general property of biological motors.Royal Society open science · 2016Article
- Titin stiffness modifies the force-generating region of muscle sarcomeres.Scientific reports · 2016Article
- Model simulation of the SPOC wave in a bundle of striated myofibrils.Biophysics and physicobiology · 2016Article
- Spontaneous oscillatory contraction (SPOC) in cardiomyocytes.Biophysical reviews · 2015Article
- Radial stability of the actomyosin filament lattice in isolated skeletal myofibrils studied using atomic force microscopy.The journal of physiological sciences : JPS · 2013Article
- Sarcomere length-dependent Ca2+ activation in skinned rabbit psoas muscle fibers: coordinated regulation of thin filament cooperative activation and passive force.The journal of physiological sciences : JPS · 2011Article
- Non-muscle myosin II induces disassembly of actin stress fibres independently of myosin light chain dephosphorylation.Interface focus · 2011Article
- SPontaneous Oscillatory Contraction (SPOC): auto-oscillations observed in striated muscle at partial activation.Biophysical reviews · 2011Review
- Effects of actin-myosin kinetics on the calcium sensitivity of regulated thin filaments.The Journal of biological chemistry · 2010Article
- Regulatory mechanism of length-dependent activation in skinned porcine ventricular muscle: role of thin filament cooperative activation in the Frank-Starling relation.The Journal of general physiology · 2010Article
- Molecular motors as an auto-oscillator.HFSP journal · 2010Article
- History-dependent properties of skeletal muscle myofibrils contracting along the ascending limb of the force-length relationship.Proceedings. Biological sciences · 2010Article
- Inter-sarcomere coordination in muscle revealed through individual sarcomere response to quick stretch.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
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4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The regulatory mechanism of sarcomeric activity has not been fully clarified yet because of its complex and cooperative nature, which involves both Ca(2+) and cross-bridge binding to the thin filament. To reveal the mechanism of regulation mediated by the cross-bridges, separately from the effect of Ca(2+), we investigated the force-sarcomere length (SL) relationship in rabbit skeletal myofibrils (a single myofibril or a thin bundle) at SL > 2.2 microm in the absence of Ca(2+) at various levels of activation by exogenous MgADP (4-20 mM) in the presence of 1 mM MgATP. The individual SLs were measured by phase-contrast microscopy to confirm the homogeneity of the striation pattern of sarcomeres during activation. We found that at partial activation with 4-8 mM MgADP, the developed force nonlinearly depended on the length of overlap between the thick and the thin filaments; that is, contrary to the maximal activation, the maximal active force was generated at shorter overlap. Besides, the active force became larger, whereas this nonlinearity tended to weaken, with either an increase in [MgADP] or the lateral osmotic compression of the myofilament lattice induced by the addition of a macromolecular compound, dextran T-500. The model analysis, which takes into account the [MgADP]- and the lattice-spacing-dependent probability of cross-bridge formation, was successfully applied to account for the force-SL relationship observed at partial activation. These results strongly suggest that the cross-bridge works as a cooperative activator, the function of which is highly sensitive to as little as <or=1 nm changes in the lattice spacing.
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