The relationship between ATP hydrolysis and active force in compressed and swollen skinned muscle fibers of the rabbit
- 1 February 1984
- journal article
- research article
- Published by Springer Nature in Pflügers Archiv - European Journal of Physiology
- Vol. 400 (2) , 160-165
- https://doi.org/10.1007/bf00585033
Abstract
We investigated whether the inhibition of force generation observed in compressed muscle fibers is accompanied by a coupled reduction in hydrolytic activity. Isometric force and rates of ATP hydrolysis (ATPase) were measured as functions of the relative width of chemically skinned skeletal muscle fiber segments immersed in relaxing (pCa>8) and activating (pCa 4.9) salt solutions. Osmotic radial compression of the fiber segment was produced (with little or no affect on striation spacing) by adding Dextran T500 to the bathing media. ADP as a product of ATP hydrolysis in fibers undergoing 10–15 min contractions was measured using high pressure liquid chromatography. Compression of the (initially swollen) fiber segment with dextran produced a slight (4%) increase in average active force and then, with further compression, a sharp decrease (with maximum around in situ width). With compression, the average ATPase of the fiber decreased monotonically, and with extreme compression (with 0.22 g dextran per ml), ATPase fell to a fifth of its level determined in dextran-free solution while force was abolished. The time course of active force development was described by the sum of two exponential functions, the faster of which characterized the rate of rise. Fiber compression (0.14 g dextran per ml) reduced the rate of rise of force ten-fold compared to that in dextran-free solution. Hindrance of cross movement is proposed to account for the inhibition of active force generation and (coupled) ATPase in compressed fibers.This publication has 16 references indexed in Scilit:
- Influence of temperature upon contractile activation and isometric force production in mechanically skinned muscle fibers of the frog.The Journal of general physiology, 1982
- Axial elastic modulus as a function of relative fiber width in relaxed skinned skeletal muscle fibersPflügers Archiv - European Journal of Physiology, 1982
- Influence of osmotic compression on calcium activation and tension in skinned muscle fibers of the rabbitPflügers Archiv - European Journal of Physiology, 1981
- Geometrical factors influencing muscle force development. I. The effect of filament spacing upon axial forcesBiophysical Journal, 1980
- Nonparallel isometric tension response of rabbit soleus skinned muscle fibers to magnesium adenosine triphosphate and magnesium inosine triphosphate.The Journal of general physiology, 1979
- Ca2+ dependence of tension and ADP production in segments of chemically skinned muscle fibersBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1976
- Mechanical Transients and the Origin of Muscular ForceCold Spring Harbor Symposia on Quantitative Biology, 1973
- Relaxation of glycerinated muscle: Low-angle X-ray diffraction studiesJournal of Molecular Biology, 1972
- Precision measurements of osmotic pressure in concentrated polymer solutionsEuropean Polymer Journal, 1971
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951