Equilibrium muscle cross-bridge behavior. Theoretical considerations.
We have developed a model for the equilibrium attachment and detachment of myosin cross-bridges to actin that takes into account the possibility that a given cross-bridge can bind to one of a number of actin monomers, as seems likely, rather than to a site on only a single actin monomer, as is often assumed. The behavior of this multiple site model in response to constant velocity, as well as instantaneous stretches, was studied and the influence of system parameters on the force response explored. It was found that in the multiple site model the detachment rate constant has considerably greater influence on the mechanical response than the attachment rate constant. It is shown that one can obtain information about the detachment rate constants either by examining the relationship between the apparent stiffness and duration of stretch for constant velocity stretches or by examining the force-decay rate constants following an instantaneous stretch. The main effect of the attachment rate constant is to scale the mechanical response by influencing the number of attached cross-bridges. The significance of the modeling for the interpretation of experimental results is discussed.
D000199:Actins / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D002118:Calcium / Q000494:pharmacology; D046911:Macromolecular Substances; D008433:Mathematics; D008954:Models, Biological; D009126:Muscle Relaxation; D009132:Muscles / Q000187:drug effects / Q000502:physiology*; D009218:Myosins / Q000378:metabolism*; D013816:Thermodynamics
D000199:Actins; D046911:Macromolecular Substances; D000255:Adenosine Triphosphate; D009218:Myosins; D002118:Calcium