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


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1981-07

AUTHORS

W. Glenn L. Kerrick, Phyllis E. Hoar

ABSTRACT

β-adrenergic relaxation of smooth muscle by catecholamines has been associated with elevated levels of cyclic AMP1,2. The question arises whether subsequent activation of cyclic AMP-dependent protein kinase3,4 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 contraction5–15, and Adelstein et al.16,17 have shown that the catalytic subunit of cyclic AMP-dependent protein kinase3,4 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. More... »

PAGES

253-255

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/292253a0

DOI

http://dx.doi.org/10.1038/292253a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1026185646

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/6265788


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