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In vitro studies of determinants of smooth muscle mechanics
J R Sellers1, S Umemoto, G Cuda
1Laboratory of Molecular Cardiology, National Heart, Lung, and Blood Institute, Bethesda, MD 20892.
Advances in Experimental Medicine and Biology
|January 1, 1993
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.