Calcium concentration in the myoplasm of skinned ferret ventricular muscle following changes in muscle length.
- 1 December 1988
- journal article
- research article
- Published by Wiley in The Journal of Physiology
- Vol. 407 (1) , 489-503
- https://doi.org/10.1113/jphysiol.1988.sp017427
Abstract
1. Ferret ventricular muscles were skinned by prolonged application of Triton X-100. Aequorin was allowed to diffuse into the myoplasmic space and the resulting light emission was used to monitor the myoplasmic [Ca2+]. The muscle was then activated with a lightly buffered Ca2+ solution and the changes in myoplasmic [Ca2+] and tension in response to length changes were investigated. 2. A sudden reduction in muscle length led to a rapid increase in myoplasmic [Ca2+] to a new level which was maintained as long as muscle length was reduced and which was reversed when the muscle was stretched back to the control length. The rate of increase of [Ca2+] when the muscle length was reduced was greater than the rate of decrease in [Ca2+] when the muscle was stretched. 3. Increasing the concentration of EGTA in the activating solution, so as to increase its Ca2+-buffering capacity, eliminated the changes in myoplasmic [Ca2+] in response to a length change but had little effect on developed tension. 4. On stretching the muscle there was a slow component of recovery of tension with a time course broadly similar to the rate of decrease of myoplasmic [Ca2+]. The time course of tension redevelopment and of the accompanying reduction in myoplasmic [Ca2+] both decreased to a similar extent when the [Ca2+] used to activate the muscle was increased. 5. Step reductions of length of increasing amplitude caused increases in myoplasmic [Ca2+] which were larger in proportion to the size of the step. 6. Step reductions of length of equal size but from different starting lengths caused changes in myoplasmic [Ca2+] the amplitude of which correlated with the change in tension rather than the change in length. 7. The increase in myoplasmic [Ca2+] when muscle length is reduced suggests that Ca2+ is released from a site in the muscle, probably troponin C. The time course and magnitude of the changes in myoplasmic [Ca2+] correlate more closely with the changes in developed tension than muscle length.This publication has 31 references indexed in Scilit:
- Rate of force generation in muscle: correlation with actomyosin ATPase activity in solution.Proceedings of the National Academy of Sciences, 1986
- The cellular basis of the length-tension relation in cardiac muscleJournal of Molecular and Cellular Cardiology, 1985
- Some characteristics of Ca2+- regulated force production in EGTA-treated muscles from rat heart.The Journal of general physiology, 1984
- A photomultiplier tube assembly for the detection of low light levelsPflügers Archiv - European Journal of Physiology, 1983
- A fluorescence stopped flow analysis of Ca2+ exchange with troponin C.Journal of Biological Chemistry, 1979
- The binding of calcium to glycerinated muscle fibers in rigor. The effect of filament overlapBiochimica et Biophysica Acta (BBA) - Protein Structure, 1977
- A reexamination of the influence of muscle length on myocardial performance.Circulation Research, 1977
- Sarcomere length-tension relations in living rat papillary muscle.Circulation Research, 1975
- Proceedings: Aequorin-light and tension responses from bundles of myofibrils following a sudden change in free calcium.1974
- The variation in isometric tension with sarcomere length in vertebrate muscle fibresThe Journal of Physiology, 1966