ArticleThe Journal of physiology2001
Effect of temperature on elementary steps of the cross-bridge cycle in rabbit soleus slow-twitch muscle fibres.
Article in The Journal of physiology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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40 citing papers in PubMed, 67 citations in OpenAlex.
- Isometric slow- and fast-contracting skeletal muscle fibres have more similar cellular and molecular properties at 37°C than at 25°C in older adults.The Journal of physiology · 2026Article
- 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
- Temperature affects the torque-velocity relationship of the ankle plantar flexor muscles.Scientific reports · 2025Article
- The elementary step that generates force and sinusoidal analysis in striated muscle fibers.Journal of muscle research and cell motility · 2025Review
- Oscillatory work and the step that generates force in single myofibrils from rabbit psoas.Pflugers Archiv : European journal of physiology · 2024Article
- Myosin and tropomyosin-troponin complementarily regulate thermal activation of muscles.The Journal of general physiology · 2023Article
- Cross-bridge mechanics estimated from skeletal muscles' work-loop responses to impacts in legged locomotion.Scientific reports · 2021Article
- Myosin cross-bridge kinetics slow at longer muscle lengths during isometric contractions in intact soleus from mice.Proceedings. Biological sciences · 2021Article
- Evidence for Muscle Cell-Based Mechanisms of Enhanced Performance in Stretch-Shortening Cycle in Skeletal Muscle.Frontiers in physiology · 2020Review
- Phosphate increase during fatigue affects crossbridge kinetics in intact mouse muscle at physiological temperature.The Journal of physiology · 2017Article
- Myosin MgADP Release Rate Decreases as Sarcomere Length Increases in Skinned Rat Soleus Muscle Fibers.Biophysical journal · 2016Article
- Age-related maintenance of eccentric strength: a study of temperature dependence.Age (Dordrecht, Netherlands) · 2016Article
- Contribution of elastic tissues to the mechanics and energetics of muscle function during movement.The Journal of experimental biology · 2016Review
- Frequency dependence of power and its implications for contractile function of muscle fibers from the digital flexors of horses.Physiological reports · 2014Article
- Age-related slowing of myosin actin cross-bridge kinetics is sex specific and predicts decrements in whole skeletal muscle performance in humans.Journal of applied physiology (Bethesda, Md. : 1985) · 2013Article
- An embryonic myosin isoform enables stretch activation and cyclical power in Drosophila jump muscle.Biophysical journal · 2013Article
- The cross-bridge spring: can cool muscles store elastic energy?Science (New York, N.Y.) · 2013Article
- Contractile properties of muscle fibers from the deep and superficial digital flexors of horses.American journal of physiology. Regulatory, integrative and comparative physiology · 2010Article
- The role of tropomyosin isoforms and phosphorylation in force generation in thin-filament reconstituted bovine cardiac muscle fibres.Journal of muscle research and cell motility · 2010Article
- Tropomyosin period 3 is essential for enhancement of isometric tension in thin filament-reconstituted bovine myocardium.Journal of biophysics (Hindawi Publishing Corporation : Online) · 2009Article
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2 authors at 1 institution in 1 country.
Funding
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Abstract
1. Isometric tension, stiffness and the cross-bridge kinetics in rabbit soleus slow-twitch fibres (STFs) were studied in the temperature range 5-37 degrees C by sinusoidal analysis. 2. The effects of MgATP and phosphate (Pi) on the cross-bridge kinetics were studied, and the temperature dependence of the kinetic constants of elementary steps of the cross-bridge cycle was deduced in the range 20-37 degrees C. 3. The MgATP association constant (K1a) decreased when temperature was increased. The rate constants of the ATP-isomerization step (k1b and k-1b) and the cross-bridge detachment step (k2, and k(-2)) had Q10 values of 3-4, and hence their equilibrium constants (K1b and K2) changed little with temperature. 4. Q10 of the force generation step (k4) was the largest at 6.7; its reversal step (k(-4)) had a Q10 of 2.5, and hence its equilibrium constant (K4) increased significantly with temperature. The Pi association constant (K5) changed little with temperature. 5. The elementary steps of the cross-bridge cycle are more temperature sensitive in soleus STFs than in psoas, which are fast-twitch fibres. This is in accord with a higher temperature sensitivity of the apparent rate constants in STFs.T 6. The temperature dependence of the equilibrium constant of the force generation step (K4) was fitted to the modified Van't Hoff equation to deduce standard enthalpy change (DeltaH degrees; 70 +/- 20 kJ mol(-1)), standard entropy change (DeltaS degrees; 250 +/- 70 J mol(-1) K(-1)), and heat capacity change (DeltaCp; -12 +/- 5 kJ mol(-1) K(-1)). These results indicate that the force generation step is an entropy driven, endothermic reaction that accompanies a burial of large surface area. These observations are consistent with the hypothesis that hydrophobic interaction between residues of actin and myosin and between residues of the myosin head underlies the mechanism of force generation. 7. An increase of isometric tension with temperature is accounted for by the increased number of cross-bridges in tension generating states. Stiffness also increased with temperature, but to a lesser degree.
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