title: The myosin motor: muscle contraction and in vitro movement.
abstract: The molecular mechanism of in vitro movement is assumed, by most investigators, to be identical to that of muscle contraction. We discuss this view, which raises various problems. We believe there are mechanisms for muscle contraction (in this case considerable forces are developed, with small displacements) and other mechanisms for in vitro movement (giving large displacements, without necessarily generating substantial forces). Hybrid models may explain muscle contraction. The traditional swinging-crossbridge model may explain in vitro movement. For muscle contraction, movement may result partly from the swinging-crossbridge mechanism and partly from other factors. Comparisons of different fibres at different moments of the Mg-ATPase cycle suggest that both the value of the isometric force in muscle and in vitro and that of the Mg-ATPase activity used in vitro need to be reconsidered. The recently reported dependence of the isometric active tension of smooth skinned fibres on temperature appears to be weaker than predicted by the swinging-crossbridge theory alone. This recent observation is compatible with the existence of other forces (electrostatic repulsions) decreasing with temperature as has been known for some years. From recent experimental data, we think the biochemistry of myosin and actomyosin should be reassessed, to try to find new details of the mechanisms of muscle contraction and in vitro motility.
authors.affiliation: Laboratoire de Biologie, Ecole Centrale de Paris, Grande Voie des Vignes, 92295, Châtenay-Malabry, France.
authors.forename: J M
authors.initials: JM
authors.lastname: Morel
authors.forename: N
authors.initials: N
authors.lastname: D'Hahan
mesh_terms: D000818:Animals; D017301:Ca(2+) Mg(2+)-ATPase / Q000378:metabolism; D007537:Isometric Contraction; D009218:Myosins / Q000502:physiology*
chemical_list: D017301:Ca(2+) Mg(2+)-ATPase; D009218:Myosins