ArticleThe Journal of physiology2006
Temperature change does not affect force between regulated actin filaments and heavy meromyosin in single-molecule experiments.
Article in The Journal of physiology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 37 citations in OpenAlex.
- The elementary step that generates force and sinusoidal analysis in striated muscle fibers.Journal of muscle research and cell motility · 2025Review
- The effect of gender and obesity in modulating cross-bridge function in cardiac muscle fibers.Journal of muscle research and cell motility · 2022Article
- Hypertrophic cardiomyopathy associated E22K mutation in myosin regulatory light chain decreases calcium-activated tension and stiffness and reduces myofilament CaThe FEBS journal · 2021Article
- Functional significance of HCM mutants of tropomyosin, V95A and D175N, studied withBiophysics and physicobiology · 2019Article
- Temperature Effects on Force and Actin⁻Myosin Interaction in Muscle: A Look Back on Some Experimental Findings.International journal of molecular sciences · 2018Review
- New Insights in Cardiac Calcium Handling and Excitation-Contraction Coupling.Advances in experimental medicine and biology · 2018Review
- Article
- Directional bleb formation in spherical cells under temperature gradient.Biophysical journal · 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
- Quantitative analysis and modeling probe polarity establishment in C. elegans embryos.Biophysical journal · 2015Article
- A study of tropomyosin's role in cardiac function and disease using thin-filament reconstituted myocardium.Journal of muscle research and cell motility · 2013Review
- The role of tropomyosin domains in cooperative activation of the actin-myosin interaction.Journal of molecular biology · 2011Article
- Crossbridge and filament compliance in muscle: implications for tension generation and lever arm swing.Journal of muscle research and cell motility · 2010Review
- Force and power generating mechanism(s) in active muscle as revealed from temperature perturbation studies.The Journal of physiology · 2010Review
- D-loop of actin differently regulates the motor function of myosins II and V.The Journal of biological chemistry · 2009Article
- The temperature dependence of cell mechanics measured by atomic force microscopy.Physical biology · 2009Article
- Tropomyosin period 3 is essential for enhancement of isometric tension in thin filament-reconstituted bovine myocardium.Journal of biophysics (Hindawi Publishing Corporation : Online) · 2009Article
- An analysis of the temperature dependence of force, during steady shortening at different velocities, in (mammalian) fast muscle fibres.Journal of muscle research and cell motility · 2008Article
- Impact of temperature on cross-bridge cycling kinetics in rat myocardium.The Journal of physiology · 2007Article
- Comparison of the tension responses to ramp shortening and lengthening in intact mammalian muscle fibres: crossbridge and non-crossbridge contributions.Journal of muscle research and cell motility · 2007Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 3 countries.
Funding
Abstract
The temperature dependence of sliding velocity, force and the number of cross-bridges was studied on regulated actin filaments (reconstituted thin filaments) when they were placed on heavy meromyosin (HMM) attached to a glass surface. The regulated actin filaments were used because our previous study on muscle fibres demonstrated that the temperature effect was much reduced in the absence of regulatory proteins. A fluorescently labelled thin filament was attached to the gelsolin-coated surface of a polystyrene bead. The bead was trapped by optical tweezers, and HMM-thin filament interaction was performed at 20-35 degrees C to study the temperature dependence of force at the single-molecule level. Our experiments showed that there was a small increase in force with temperature (Q10 = 1.43) and sliding velocity (Q10 = 1.46). The small increase in force was correlated with the small increase in the number of cross-bridges (Q10 = 1.49), and when force was divided by the number of cross-bridges, the result did not depend on the temperature (Q(10) = 1.03). These results demonstrate that the force each cross-bridge generates is fixed and independent of temperature. Our additional experiments demonstrate that tropomyosin (Tm) in the presence of troponin (Tn) and Ca2+ enhances both force and velocity, and a truncated mutant, Delta23Tm, diminishes force and velocity. These results are consistent with the hypothesis that Tm in the presence of Tn and Ca2+ exerts a positive allosteric effect on actin to make actomyosin linkage more secure so that larger forces can be generated.
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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.