High ionic strength and low pH detain activated skinned rabbit skeletal muscle crossbridges in a low force state.
Open Access
- 1 April 1993
- journal article
- Published by Rockefeller University Press in The Journal of general physiology
- Vol. 101 (4) , 487-511
- https://doi.org/10.1085/jgp.101.4.487
Abstract
The effects of varying pH and ionic strength on the force-velocity relations and tension transients of skinned rabbit skeletal muscle were studied at 1-2 degrees C. Both decreasing pH from 7.35 to 6.35 and raising ionic strength from 125 to 360 mM reduced isometric force by about half and decreased sarcomere stiffness by about one-fourth, so that the stiffness/force ratio was increased by half. Lowering pH also decreased maximum shortening velocity by approximately 29%, while increasing ionic strength had little effect on velocity. These effects on velocity were correlated with asymmetrical effects on stiffness. The increase in the stiffness/force ratio with both interventions was manifest as a greater relative force change associated with a sarcomere length step. This force difference persisted for a variable time after the step. At the high ionic strength the force difference was long-lasting after stretches but relaxed quickly after releases, suggesting that the structures responsible would not impose much resistance to steady-state shortening. The opposite was found in the low pH experiments. The force difference relaxed quickly after stretches but persisted for a long time after releases. Furthermore, this force difference reached a constant value of approximately 8% of isometric force with intermediate sizes of release, and was not increased with larger releases. This value was almost identical to the value of an internal load that would be sufficient to account for the reduction in maximum velocity seen at the low pH. The results are interpreted as showing that both low pH and high ionic strength inhibit the movement of crossbridges into the force-generating parts of their cycle after they have attached to the actin filaments, with very few other effects on the cycle. The two interventions are different, however, in that detained bridges can be detached readily by shortening when the detention is caused by high ionic strength but not when it is caused by low pH.Keywords
This publication has 41 references indexed in Scilit:
- Effects of fatigue and altered pH on isometric force and velocity of shortening at zero load in frog muscle fibresJournal of Muscle Research and Cell Motility, 1981
- Isotonic contraction of skinned muscle fibers on a slow time base: effects of ionic strength and calcium.The Journal of general physiology, 1981
- The relation between stiffness and filament overlap in stimulated frog muscle fibres.The Journal of Physiology, 1981
- Effects of calcium and ionic strength on shortening velocity and tension development in frog skinned muscle fibres.The Journal of Physiology, 1981
- A piezoelectric force transducer for single muscle cellsAmerican Journal of Physiology-Cell Physiology, 1978
- Swelling of Skinned Muscle Fibers of the FrogBiophysical Journal, 1977
- Tension responses to sudden length change in stimulated frog muscle fibres near slack lengthThe Journal of Physiology, 1977
- The effects of temperature and salts on myosin subfragment-1 and F-actin associationArchives of Biochemistry and Biophysics, 1977
- A note suggesting that the cross-bridge attachment during muscle contraction may take place in two stagesProceedings of the Royal Society of London. B. Biological Sciences, 1973
- X-ray diffraction studies on skinned single fibres of frog skeletal muscleJournal of Molecular Biology, 1972