Crossref journal-article
American Association for the Advancement of Science (AAAS)
Science (221)
Abstract

The role of cyclic adenosine monophosphate-mediated phosphorylation of myosin light chain kinase in relaxing smooth muscle was examined. The kinase was immunoprecipitated from tissue extracts and the phosphate content was determined. The addition of forskolin to resting or methacholine-contracted muscles resulted in an increase in myosin light chain kinase phosphorylation and a relaxation of contracted muscles. These findings suggest that phosphorylation of myosin light chain kinase is one of the reactions in the process by which cyclic adenosine monophosphate causes relaxation of smooth muscle.

Bibliography

de Lanerolle, P., Nishikawa, M., Yost, D. A., & Adelstein, R. S. (1984). Increased Phosphorylation of Myosin Light Chain Kinase After an Increase in Cyclic AMP in Intact Smooth Muscle. Science, 223(4643), 1415–1417.

Authors 4
  1. Primal de Lanerolle (first)
  2. Masakatsu Nishikawa (additional)
  3. David A. Yost (additional)
  4. Robert S. Adelstein (additional)
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Dates
Type When
Created 18 years, 11 months ago (Oct. 5, 2006, 3:41 p.m.)
Deposited 1 year, 7 months ago (Jan. 14, 2024, 5 p.m.)
Indexed 1 day, 14 hours ago (Sept. 4, 2025, 10:26 a.m.)
Issued 41 years, 5 months ago (March 30, 1984)
Published 41 years, 5 months ago (March 30, 1984)
Published Print 41 years, 5 months ago (March 30, 1984)
Funders 0

None

@article{de_Lanerolle_1984, title={Increased Phosphorylation of Myosin Light Chain Kinase After an Increase in Cyclic AMP in Intact Smooth Muscle}, volume={223}, ISSN={1095-9203}, url={http://dx.doi.org/10.1126/science.6322302}, DOI={10.1126/science.6322302}, number={4643}, journal={Science}, publisher={American Association for the Advancement of Science (AAAS)}, author={de Lanerolle, Primal and Nishikawa, Masakatsu and Yost, David A. and Adelstein, Robert S.}, year={1984}, month=mar, pages={1415–1417} }