Okadaic acid uncouples myosin light chain phosphorylation and tension in smooth muscle

M. G. Tansey, M. Hori, H. Karaki, K. E. Kamm, J. T. Stull

Research output: Contribution to journalArticle

60 Scopus citations

Abstract

Tracheal smooth muscle precontracted with carbachol relaxes upon the addition of 3 μM okadaic add. Although cytosolic Ca2+ concentrations decrease, myosin light chain remains highly phosphorylated (50%). In smooth muscle treated with carbachol alone or carbachol plus okadaic acid 32P is incorporated into a single peptide on myosin light chain which corresponds to the site phosphorylated by myosin light chain kinase. Treatment with okadaic acid alone does not result in myosin light chain phosphorylation or tension development. These results suggest that a cellular mechanism other than myosin light chain phosphorylation can regulate contractile tension.

Original languageEnglish (US)
Pages (from-to)219-221
Number of pages3
JournalFEBS Letters
Volume270
Issue number1-2
DOIs
StatePublished - Sep 17 1990

Keywords

  • Myosin light chain phosphorylation
  • Okadaic acid
  • Smooth muscle relaxation

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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