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Okadaic acid uncouples myosin light chain phosphorylation and tension in smooth muscle.
Tansey, M G; Hori, M; Karaki, H; Kamm, K E; Stull, J T.
Afiliação
  • Tansey MG; Department of Physiology, University of Texas Southwestern Medical Center, Dallas 75235.
FEBS Lett ; 270(1-2): 219-21, 1990 Sep 17.
Article em En | MEDLINE | ID: mdl-2171992
Tracheal smooth muscle precontracted with carbachol relaxes upon the addition of 3 microM okadaic acid. 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.
Assuntos
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Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Miosinas / Fosfoproteínas Fosfatases / Éteres Cíclicos / Músculo Liso Limite: Animals Idioma: En Revista: FEBS Lett Ano de publicação: 1990 Tipo de documento: Article
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Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Miosinas / Fosfoproteínas Fosfatases / Éteres Cíclicos / Músculo Liso Limite: Animals Idioma: En Revista: FEBS Lett Ano de publicação: 1990 Tipo de documento: Article