The influence of doubly attached crossbridges on the mechanical behavior of skeletal muscle fibers under equilibrium conditions.
A simple model of a double-headed crossbridge is introduced to explain the retardation of force decay after an imposed stretch in skeletal muscle fibers under equilibrium conditions. The critical assumption in the model is that once one of the heads of a crossbridge is attached to one of the available actin sites, the attachment of the second head will be restricted to a level of strain determined by the attachment of the first head. The crossbridge structure, namely the connection of both heads of a crossbridge to the same tail region, is assumed to impose this constraint on the spatial configurations of crossbridge heads. The unique feature of the model is the prediction that, in the presence of a ligand (PPi, ADP, AMP-PNP) and absence of Ca2+, the halftime of force decay is many times larger than the inverse rate of detachment of a crossbridge head measured in solution. This prediction is in agreement with measured values of half-times of force decay in fibers under similar conditions (Schoenberg, M., and E. Eisenberg. 1985. Biophys. J. 48:863-871f). It is predicted that a crossbridge head is more likely to re-attach to its previously strained position than remain unattached while the other head is attached, leading to the slow decay of force. Our computations also show that the apparent cooperativity in crossbridge binding observed in experiments (Brenner, B., L. C. Yu, L. E. Greene, E. Eisenberg, and M. Schoenberg. 1986. Biophys. J. 50:1101-1108) can be partially accounted by the double-headed crossbridge attachment. Our model predictions fit the aforementioned data best when the crossbridge stiffness does not change significantly with the dissociation of one of the two attached heads. This observation suggests that crossbridge stiffness is determined either by the extensibility (flexibility) of the double helical tail region or its junction to the thick filament backbone.
Tozeren
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Department of Mechanical Engineering, Catholic University of America, Washington, DC 20064.
D008841:Actin Cytoskeleton / Q000502:physiology; D000199:Actins / Q000502:physiology*; D000266:Adenylyl Imidodiphosphate / Q000494:pharmacology; D000818:Animals; D007700:Kinetics; D008433:Mathematics; D008954:Models, Biological; D009119:Muscle Contraction; D009132:Muscles / Q000502:physiology*; D010710:Phosphates / Q000494:pharmacology
D000199:Actins; D010710:Phosphates; D000266:Adenylyl Imidodiphosphate