Phosphorylation-dependent activated tension in skinned gizzard muscle fibers in the absence of Ca2+.

M. P. Walsh, R. Bridenbaugh, D. J. Hartshorne, W. Glenn Kerrick

Research output: Contribution to journalArticle

47 Citations (Scopus)

Abstract

A Ca2+-insensitive myosin light chain kinase was prepared and used in experiments with skinned gizzard fibers. In the absence of Ca2+, this kinase activated isometric force development. The force development was associated with phosphorylation of the 20,000-dalton myosin light chains and addition of Ca2+ did not activate the fibers further. Pretreatment of the fibers with Ca2+-insensitive myosin light chain kinase and adenosine 5'-O-(3-thiotriphosphate) in the absence of Ca2+ caused thiophosphorylation of the light chains and, on the addition of ATP, an activation of isometric tension was observed. The subsequent addition of Ca2+ did not increase force development. A comparison of Ca2+-activated tension in the skinned gizzard muscle fibers with Ca2+-insensitive myosin light chain kinase-activated tension suggests that the phosphorylation of the myosin light chains is the dominant factor in the development of tension in smooth muscle.

Original languageEnglish
Pages (from-to)5987-5990
Number of pages4
JournalJournal of Biological Chemistry
Volume257
Issue number11
StatePublished - Jun 10 1982
Externally publishedYes

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Myosin-Light-Chain Kinase
Phosphorylation
Muscle
Myosin Light Chains
Muscles
Fibers
Smooth Muscle
Phosphotransferases
Adenosine Triphosphate
Light
Chemical activation
Experiments

ASJC Scopus subject areas

  • Biochemistry

Cite this

Phosphorylation-dependent activated tension in skinned gizzard muscle fibers in the absence of Ca2+. / Walsh, M. P.; Bridenbaugh, R.; Hartshorne, D. J.; Kerrick, W. Glenn.

In: Journal of Biological Chemistry, Vol. 257, No. 11, 10.06.1982, p. 5987-5990.

Research output: Contribution to journalArticle

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