ArticleBiophysical journal2000
Temperature change does not affect force between single actin filaments and HMM from rabbit muscles.
Article in Biophysical journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 33 citations in OpenAlex.
- Myosin and tropomyosin-troponin complementarily regulate thermal activation of muscles.The Journal of general physiology · 2023Article
- Temperature-Dependent Activity of Motor Proteins: Energetics and Their Implications for Collective Behavior.Frontiers in cell and developmental biology · 2021Review
- Article
- Directional bleb formation in spherical cells under temperature gradient.Biophysical journal · 2015Article
- Biomechanics and the thermotolerance of development.PloS one · 2014Article
- Actomyosin kinetics of pure fast and slow rat myosin isoforms studied by in vitro motility assay approach.Experimental physiology · 2012Article
- Micromechanical thermal assays of Ca2+-regulated thin-filament function and modulation by hypertrophic cardiomyopathy mutants of human cardiac troponin.Journal of biomedicine & biotechnology · 2012Article
- The role of tropomyosin domains in cooperative activation of the actin-myosin interaction.Journal of molecular biology · 2011Article
- The temperature dependence of cell mechanics measured by atomic force microscopy.Physical biology · 2009Article
- Mechanism of tension generation in muscle: an analysis of the forward and reverse rate constants.Biophysical journal · 2007Article
- Temperature-dependence of isometric tension and cross-bridge kinetics of cardiac muscle fibers reconstituted with a tropomyosin internal deletion mutant.Biophysical journal · 2006Article
- Temperature change does not affect force between regulated actin filaments and heavy meromyosin in single-molecule experiments.The Journal of physiology · 2006Article
- The force exerted by a muscle cross-bridge depends directly on the strength of the actomyosin bond.Biophysical journal · 2004Article
- Instabilities in the transient response of muscle.Biophysical journal · 2003Article
- Kinetic effects of fiber type on the two subcomponents of the Huxley-Simmons phase 2 in muscle.Biophysical journal · 2003Article
- The elementary force generation process probed by temperature and length perturbations in muscle fibres from the rabbit.The Journal of physiology · 2002Article
- Force and velocity of mycoplasma mobile gliding.Journal of bacteriology · 2002Article
- Temperature effect on isometric tension is mediated by regulatory proteins tropomyosin and troponin in bovine myocardium.The Journal of physiology · 2002Article
- Effect of temperature on elementary steps of the cross-bridge cycle in rabbit soleus slow-twitch muscle fibres.The Journal of physiology · 2001Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The temperature dependence of sliding force, velocity, and unbinding force was studied on actin filaments when they were placed on heavy meromyosin (HMM) attached to a glass surface. A fluorescently labeled actin filament was attached to the gelsolin-coated surface of a 1-microm polystyrene bead. The bead was trapped by optical tweezers, and HMM-actin interaction was performed at 20-35 degrees C to examine whether force is altered by the temperature change. Our experiments demonstrate that sliding force increased moderately with temperature (Q(10) = 1.6 +/- 0.2, +/-SEM, n = 9), whereas the velocity increased significantly (Q(10) = 2.9 +/- 0.4, n = 10). The moderate increase in force is caused by the increased number of available cross-bridges for actin interaction, because the cross-bridge number similarly increased with temperature (Q(10) = 1. 5 +/- 0.2, n = 3) when measured during rigor induction. We further found that unbinding force measured during the rigor condition did not differ with temperature. These results indicate that the amount of force each cross-bridge generates is fixed, and it does not change with temperature. We found that the above generalization was not modified in the presence of 1 mM MgADP or 8 mM phosphate.
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