title: Cooperative interactions of myosin two heads in muscle force generation.
abstract: To investigate the possibility of cooperative interactions between the two myosin heads in muscle contraction, Ca2+-activated force development, K+-EDTA- and Mg2+-ATPase activities, muscle fiber stiffness, and the velocity of unloaded shortening were measured on partially p-PDM treated glycerinated muscle fibers, which contained a mixture of myosin molecules with zero, one and two of their heads inactivated. It was found that the magnitude of the Ca2+-activated isometric force development was proportional to the square of both K+-EDTA- and Mg2+-ATPase activities and also to the square of muscle fiber stiffness. If the two myosin heads in the glycerinated fibers are assumed to react independently with p-PDM, the above results strongly suggest that (i) each myosin molecule in the thick filaments can generate force only when its two heads do not react with p-PDM, (ii) muscle fiber stiffness is determined by the total number of native heads, and (iii) there is no cooperative interaction between the two myosin heads in catalyzing ATP hydrolysis.
authors.affiliation: Department of Physiology, School of Medicine, Teikyo University, Japan.
authors.forename: S
authors.initials: S
authors.lastname: Chaen
authors.forename: M
authors.initials: M
authors.lastname: Shimada
authors.forename: H
authors.initials: H
authors.lastname: Sugi
mesh_terms: D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000818:Animals; D017301:Ca(2+) Mg(2+)-ATPase / Q000378:metabolism; D002118:Calcium / Q000494:pharmacology; D066298:In Vitro Techniques; D007537:Isometric Contraction / Q000187:drug effects; D008954:Models, Biological; D009119:Muscle Contraction / Q000187:drug effects; D009132:Muscles / Q000502:physiology*; D009218:Myosins / Q000502:physiology*; D011817:Rabbits
chemical_list: D000251:Adenosine Triphosphatases; D017301:Ca(2+) Mg(2+)-ATPase; C026049:EDTA-ATPase; D009218:Myosins; D002118:Calcium