Isotonic force modulates force redevelopment rate of intact frog muscle fibres: evidence for cross‐bridge induced thin filament activation
- 1 September 2002
- journal article
- Published by Wiley in The Journal of Physiology
- Vol. 543 (2) , 555-566
- https://doi.org/10.1113/jphysiol.2002.022673
Abstract
We tested the hypothesis that force‐velocity history modulates thin filament activation, as assessed by the rate of force redevelopment after shortening (+dF/dtR). The influence of isotonic force on +dF/dtR was assessed by imposing uniform amplitude (2.55 to 2.15 μm sarcomere−1) but different speed releases to intact frog muscle fibres during fused tetani. Each release consisted of a contiguous ramp‐ and step‐change in length. Ramp speed was changed from release to release to vary fibre shortening speed from 1.00 (2.76 ± 0.11 μm half‐sarcomere−1 s−1) to 0.30 of maximum unloaded shortening velocity (Vu), thereby modulating isotonic force from 0 to 0.34 Fo, respectively. The step zeroed force and allowed the fibre to shorten unloaded for a brief period of time prior to force redevelopment. Although peak force redevelopment after different releases was similar, +dF/dtR increased by 81 ± 6% (P < 0.05) as fibre shortening speed was reduced from 1.00 Vu. The +dF/dtR after different releases was strongly correlated with the preceding isotonic force (r= 0.99, P < 0.001). Results from additional experiments showed that the slope of slack test plots produced by systematically increasing the step size that followed each ramp were similar. Thus, isotonic force did not influence Vu (mean: 2.84 ± 0.10 μm half‐sarcomere−1 s−1, P < 0.05). We conclude that isotonic force modulates +dF/dtR independent of change in Vu, an outcome consistent with a cooperative influence of attached cross‐bridges on thin filament activation that increases cross‐bridge attachment rate without alteration to cross‐bridge detachment rate.Keywords
This publication has 41 references indexed in Scilit:
- Strong binding of myosin increases shortening velocity of rabbit skinned skeletal muscle fibres at low levels of Ca2+The Journal of Physiology, 2001
- Modulation of Contractile Activation in Skeletal Muscle by a Calcium-insensitive Troponin C MutantPublished by Elsevier ,2001
- Submillisecond changes in myosin lattice spacing resulting from rapid length changes 1 1Edited by M. F. MoodyJournal of Molecular Biology, 1999
- Effects of rapid shortening on rate of force regeneration and myoplasmic [Ca2+] in intact frog skeletal muscle fibresThe Journal of Physiology, 1998
- Mechanisms underlying reduced maximum shortening velocity during fatigue of intact, single fibres of mouse muscleThe Journal of Physiology, 1998
- Detection of Radial Crossbridge Force by Lattice Spacing Changes in Intact Single Muscle FibersScience, 1990
- Calcium-Sensitive Cross-Bridge Transitions in Mammalian Fast and Slow Skeletal Muscle FibersScience, 1990
- Reciprocal coupling between troponin C and myosin crossbridge attachmentBiochemistry, 1989
- Depression of mechanical performance by active shortening during twitch and tetanus of vertebrate muscle fibresActa Physiologica Scandinavica, 1980
- Variation of muscle stiffness with force at increasing speeds of shortening.The Journal of general physiology, 1975