title: In vitro studies of determinants of smooth muscle mechanics.
abstract: Smooth muscle contraction is dependent upon phosphorylation of the 20,000 Da light chain subunits of myosin. Whereas the kinetics of the hydrolysis of MgATP by smooth muscle myosin suggest a simple phosphorylation-dependent "on-off" mechanism, the contractile response in smooth muscle tissue is complex. Experiments to unravel this complexity have been performed in vitro using a combination of motility assays and kinetic techniques. Some insight into this complexity is obtained, but the mechanism and the regulation of smooth muscle contraction is still not completely known.
authors.affiliation: Laboratory of Molecular Cardiology, National Heart, Lung, and Blood Institute, Bethesda, MD 20892.
authors.forename: J R
authors.initials: JR
authors.lastname: Sellers
authors.forename: S
authors.initials: S
authors.lastname: Umemoto
authors.forename: G
authors.initials: G
authors.lastname: Cuda
mesh_terms: D000818:Animals; D006801:Humans; D009130:Muscle, Smooth / Q000737:chemistry / Q000502:physiology*; D009218:Myosins / Q000737:chemistry / Q000502:physiology*
chemical_list: D009218:Myosins