ArticleThe Journal of physiology2002
The elementary force generation process probed by temperature and length perturbations in muscle fibres from the rabbit.
Article in The Journal of physiology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed.
- The elementary step that generates force and sinusoidal analysis in striated muscle fibers.Journal of muscle research and cell motility · 2025Review
- The Mechanism of Modulation of Cardiac Force by Temperature.International journal of molecular sciences · 2025Article
- The N-Terminal Mutations of cMyBP-C Affect Calcium Regulation, Kinetics, and Force of Muscle Contraction.International journal of molecular sciences · 2024Article
- Oscillatory work and the step that generates force in single myofibrils from rabbit psoas.Pflugers Archiv : European journal of physiology · 2024Article
- Dependence of thick filament structure in relaxed mammalian skeletal muscle on temperature and interfilament spacing.The Journal of general physiology · 2021Article
- The likely effects of thermal climate change on vertebrate skeletal muscle mechanics with possible consequences for animal movement and behaviour.Conservation physiology · 2019Review
- Temperature Effects on Force and Actin⁻Myosin Interaction in Muscle: A Look Back on Some Experimental Findings.International journal of molecular sciences · 2018Review
- Kinetic coupling of phosphate release, force generation and rate-limiting steps in the cross-bridge cycle.Journal of muscle research and cell motility · 2017Review
- Force Responses and Sarcomere Dynamics of Cardiac Myofibrils Induced by Rapid Changes in [PBiophysical journal · 2017Article
- The endothermic ATP hydrolysis and crossbridge attachment steps drive the increase of force with temperature in isometric and shortening muscle.The Journal of physiology · 2015Article
- Why muscle is an efficient shock absorber.PloS one · 2014Article
- A review of the thermal sensitivity of the mechanics of vertebrate skeletal muscle.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2013Review
- The effects of Ca2+ and MgADP on force development during and after muscle length changes.PloS one · 2013Article
- ATP binding and cross-bridge detachment steps during full Ca²⁺ activation: comparison of myofibril and muscle fibre mechanics by sinusoidal analysis.The Journal of physiology · 2012Article
- The fraction of myosin motors that participate in isometric contraction of rabbit muscle fibers at near-physiological temperature.Biophysical journal · 2011Article
- Force and power generating mechanism(s) in active muscle as revealed from temperature perturbation studies.The Journal of physiology · 2010Review
- Myosin heads contribute to the maintenance of filament order in relaxed rabbit muscle.Biophysical journal · 2010Article
- Effect of phosphate and temperature on force exerted by white muscle fibres from dogfish.Journal of muscle research and cell motility · 2010Article
- Temperature jump induced force generation in rabbit muscle fibres gets faster with shortening and shows a biphasic dependence on velocity.The Journal of physiology · 2010Article
- Temperature change as a probe of muscle crossbridge kinetics: a review and discussion.Proceedings. Biological sciences · 2009Review
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Single chemically permeabilized fibres from rabbit psoas muscle were activated maximally at 5-6 degrees C and then exposed to a rapid temperature increase ('T-jump') up to 37 degrees C by passing a high-voltage pulse (40 kHz AC, 0.15 ms duration) through the fibre length. Fibre cooling after the T-jump was compensated by applying a warming (40 kHz AC, 200 ms) pulse. Tension and changes in sarcomere length induced by the T-jumps and by fast length step perturbations of the fibres were monitored. In some experiments sarcomere length feedback control was used. After T-jumps tension increased from approximately 55 kN m(-2) at 5-6 degrees C to approximately 270 kN m(-2) at 36-37 degrees C, while stiffness rose by approximately 15 %, suggesting that at a higher temperature the myosin head generates more force. The temperature-tension relation became less steep at temperatures above 25 degrees C, but was not saturated even at near-physiological temperature. Comparison of tension transients induced by the T-jump and length steps showed that they are different. The T-jump transients were several times slower than fast partial tension recovery following length steps at low and high temperature (phase 2). The kinetics of the tension rise after the T-jumps was independent of the preceding length changes. When the length steps were applied during the tension rise induced by the T-jump, the observed complex tension transient was simply the sum of two separate responses to the mechanical and temperature perturbations. This demonstrates the absence of interaction between these processes. The data suggest that tension transients induced by the T-jumps and length steps are caused by different processes in myosin cross-bridges.
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