Phosphorylation of myosin light chain in skeletal and smooth muscles

J. T. Stull, P. J. Silver, J. R. Miller, D. K. Blumenthal, B. R. Botterman, G. A. Klug

Research output: Contribution to journalArticle

8 Scopus citations

Abstract

Significant differences in the properties of myosin light chain phosphorylation in skeletal and smooth muscles may be important in considering the role of myosin phosphorylation in contraction. Repetitive, low-frequency stimulation of fast-twitch skeletal muscle resulted in phosphorylation of myosin light chain. Some of the factors leading to phosphorylation under these conditions include partial activation of myosin light chain kinase with each stimulus, a slow rate (t(1/2) = 1 s) of inactivation of the kinase activity, and a very slow rate of dephosphorylation by myosin light chain phosphatase. Myosin light chain phosphorylation was correlated with potentiation of isometric twitch tension in posttetanic potentiation and staircase responses. Stimulation of contraction in bovine tracheal smooth muscle by the cholinergic agonist carbachol was correlated with phosphorylation of the myosin light chain. The initial rate and maximum extent of phosphorylation during the first minute of stimulation was dependent on the concentration of carbachol. Phosphate incorporation into light chain declined after 1 min whereas isometric tension was maintained. β-Adrenergic inhibition of tension development was accompanied by a decrease in the rate and extent of phosphorylatable myosin light chain phosphorylation but was not associated with reduced affinity of myosin light chain kinase for calcium-calmodulin.

Original languageEnglish (US)
Pages (from-to)21-26
Number of pages6
JournalFederation Proceedings
Volume42
Issue number1
StatePublished - 1983

ASJC Scopus subject areas

  • Medicine(all)

Fingerprint Dive into the research topics of 'Phosphorylation of myosin light chain in skeletal and smooth muscles'. Together they form a unique fingerprint.

Cite this