Inhibition of smooth muscle tension by cyclic AMP-dependent protein kinase

W. Glenn Kerrick, P. E. Hoar

Research output: Contribution to journalArticle

74 Citations (Scopus)

Abstract

β-adrenergic relaxation of smooth muscle by catecholamines has been associated with elevated levels of cyclic AMP. The question arises whether subsequent activation of cyclic AMP-dependent protein kinase has a role in the regulation of smooth muscle contraction. There is substantial evidence that a Ca2+-activated myosin light chain kinase/phosphatase system regulates smooth muscle contraction, and Adelstein et al. have shown that the catalytic subunit of cyclic ANP-dependent protein kinase plays a part in this regulation, by phosphorylation of the high molecular weight subunit of the light chain kinase, which results in a decrease in the activity of the kinase. Here we have shown for the first time that the catalytic subunit of the protein kinase inhibits Ca2+-activated tension in skinned smooth muscle fibre preparations.

Original languageEnglish
Pages (from-to)253-255
Number of pages3
JournalNature
Volume292
Issue number5820
StatePublished - Dec 1 1981

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Muscle Tonus
Cyclic AMP-Dependent Protein Kinases
Smooth Muscle
Muscle Contraction
Protein Kinases
Catalytic Domain
Phosphotransferases
Myosin-Light-Chain Phosphatase
Myosin-Light-Chain Kinase
Atrial Natriuretic Factor
Cyclic AMP
Adrenergic Agents
Catecholamines
Molecular Weight
Phosphorylation
Light

ASJC Scopus subject areas

  • General

Cite this

Inhibition of smooth muscle tension by cyclic AMP-dependent protein kinase. / Kerrick, W. Glenn; Hoar, P. E.

In: Nature, Vol. 292, No. 5820, 01.12.1981, p. 253-255.

Research output: Contribution to journalArticle

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