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.
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Kerrick, W., Hoar, P. Inhibition of smooth muscle tension by cyclic AMP-dependent protein kinase. Nature 292, 253–255 (1981). https://doi.org/10.1038/292253a0
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DOI: https://doi.org/10.1038/292253a0
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