Inhibition of smooth muscle tension by cyclic AMP-dependent protein kinase - PubMed (original) (raw)
. 1981 Jul 16;292(5820):253-5.
doi: 10.1038/292253a0.
- PMID: 6265788
- DOI: 10.1038/292253a0
Inhibition of smooth muscle tension by cyclic AMP-dependent protein kinase
W G Kerrick et al. Nature. 1981.
Abstract
beta-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 AMP-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 fiber preparations.
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