Thermal dependence of maximum Ca2+-activated force in skinned muscle fibres of the toad Bufo marinus acclimated at different temperatures
Open Access
- 1 May 1987
- journal article
- research article
- Published by The Company of Biologists in Journal of Experimental Biology
- Vol. 129 (1) , 309-327
- https://doi.org/10.1242/jeb.129.1.309
Abstract
Mechanically skinned muscle fibres from the twitch region of the iliofibularis muscle of cool-(16 ± 1°C) and warm- (32 ± 1°C) acclimated cane toads (Bufo marinus) were activated maximally by Ca2+ in solutions of different pH and at different temperatures (approx. 1–35°C). Acclimation of up to 12 weeks at 16°C and up to 8 weeks at 32°C did not modify the marked thermal dependence of isometric force in the skeletal muscle fibres of the cane toad. The prominent decline of maximum Ca2+-activated force at lower temperatures, a property which is not characteristic of muscles from other anurans, was associated with an obvious decline in fibre stiffness at temperatures below about 20°C, regardless of the temperatures at which the toads were kept prior to experimentation. The results suggest that the decline of isometric force at lower temperatures is due both to a reduction in the number of cross-bridges and to a decrease in the force output per cross-bridge. The maximum Ca2+-activated force response increased when fibres were activated in solutions of increasing pH at all temperatures investigated. This trend is expected to have a compensatory effect on the thermal dependence of the maximum Ca2+-activated force under physiological conditions, because of the elevation of intracellular pH as temperature declines. 4.The isometric force did not depend on the concentration of the zwitterionic species of the pH buffer in solutions. 5.The skinned fibre preparation developed a Ca2+-insensitive residual force following maximal activation. The increment in residual force followed a linear relationship with the duration of activation at a given temperature and a power relationship of activation temperature for a given duration of activation. Fibres from warm-acclimated animals developed less residual force following activations at 15 °C than did fibres from cool-acclimated animals, suggesting that thermal acclimation may substantially reduce the magnitude of this phenomenon at temperatures below 20°C.This publication has 27 references indexed in Scilit:
- Evolutionary adaptation of muscle power output to environmental temperature: force-velocity characteristics of skinned fibres isolated from antarctic, temperate and tropical marine fishPflügers Archiv - European Journal of Physiology, 1985
- Stiffness, force, and sarcomere shortening during a twitch in frog semitendinosus muscle bundlesBiophysical Journal, 1984
- Muscular Contraction: Kinetics of Crossbridge Attachment Studied by High-Frequency Stiffness MeasurementsScience, 1982
- Isometric contractile properties and instantaneous stiffness of amphibian skeletal muscle in the temperature range from 0 to 20 °CCanadian Journal of Physiology and Pharmacology, 1981
- Role of creatine phosphokinase in cellular function and metabolismCanadian Journal of Physiology and Pharmacology, 1978
- Localization of creatine kinase isoenzymes in myofibrils. I. Chicken skeletal muscle.The Journal of cell biology, 1977
- Intracellular ph in cold-blooded vertebrates as a function of body temperatureRespiration Physiology, 1976
- Kinetics of reaction in calcium-activated skinned muscle fibresNature, 1976
- Ionic Strength and the Contraction Kinetics of Skinned Muscle FibersThe Journal of general physiology, 1974
- A Preliminary Review of the Thermal Requirements of AmphibiansEcology, 1963