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- Title
Myosin phosphorylation, agonist concentration and contraction of tracheal smooth muscle.
- Authors
de Lanerolle, Primal; Condit, John R.; Tanenbaum, Mark; Adelstein, Robert S.
- Abstract
Myosin phosphorylation plays an important part in excitation-contraction coupling in smooth muscle. Phosphorylation by a Ca2+, calmodulin-dependent kinase stimulates the actin-activated Mg2+-ATPase activity of smooth muscle myosin1-5, suggesting that myosin phosphorylation regulates smooth muscle contraction (see refs 5, 6 for discussions of alternative hypotheses). This hypothesis is supported by evidence that myosin is phosphorylated during contraction and dephosphorylated during relaxation of intact smooth muscles stimulated with a single agonist concentration7-9. However, there is little information regarding the response to stimulation with various agonist concentrations. As the dose-response relationships for phosphorylation and tension should be similar if myosin phosphorylation does, in fact, regulate smooth muscle contraction, we studied myosin phosphorylation in tracheal smooth muscle stimulated with a broad range of concentrations of the cholinergic agonist, methacholine. The results of these experiments are consistent with the hypothesis that myosin phosphorylation regulates smooth muscle contraction but they indicate a relatively complex relationship between myosin phosphorylation and the generation of isometric tension.
- Publication
Nature, 1982, Vol 298, Issue 5877, p871
- ISSN
0028-0836
- Publication type
Article
- DOI
10.1038/298871a0