Dynamic actin interaction of cross-bridges during force generation: implications for cross-bridge action in muscle.
The force response of Ca(2+)-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 10(5) (nm/half-sarcomere)/s. At physiological ionic strength and at low temperature (5 degrees 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 ("stiffness-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.
Brenner
B
B
Department of General Physiology, University of Ulm, FRG.
D000199:Actins / Q000737:chemistry / Q000502:physiology*; D000818:Animals; D003432:Cross-Linking Reagents; D007537:Isometric Contraction / Q000502:physiology; D007551:Isotonic Contraction / Q000502:physiology; D009119:Muscle Contraction / Q000502:physiology; D009132:Muscles / Q000737:chemistry / Q000502:physiology*; D016658:Psoas Muscles / Q000737:chemistry / Q000502:physiology; D011817:Rabbits
D000199:Actins; D003432:Cross-Linking Reagents