Dynamic Actin Interaction of Cross-Bridges During Force Generation: Implications for Cross-Bridge Action in Muscle
The force response of Ca2+ -activated, permeabilized segments of rabbit psoas muscle fibers to stretches and releases was studied. These length changes were imposed (i) during isometric steady state contraction, (ii) as a restretch at the end of a ramp-shaped prerelease, and (iii) during isotonic steady state shortening. The speed of the stretches/releases was varied between about 10 and 105 (nm/halfsarcomere)/s. At physiological ionic strength and at low temperature (5°C), the force response to stretches apparently is neither affected by cross-bridges that occupy weak-binding states nor by redistribution among various attached force-generating states. Plots of force vs. imposed length change (“T-plots”) and plots of apparent fiber stiffness vs. speed of the imposed length change (“stiffhess-speed relations”) recorded under all these conditions suggest that cross-bridges, even during force-generation, dissociate and reassociate from and to actin on a time scale that is fast compared to active cross-bridge cycling (> 50- 1000s-1 vs. 1-10s-1). This rapid dissociation/reassociation of force-generating cross-bridges may provide a mechanism to account for the unexpectedly low ATPase activity during high-speed shortening and for filament sliding exceeding 10–20nm while a cross-bridge passes through the force-generating states.
KeywordsEDTA Propionate Cardiol Creatine Glutaraldehyde
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