Open AccessEndothelin-1-Induced Phosphorylation of the 20-kDa Myosin Light Chain and Caldesmon in Porcine Coronary Artery Smooth Muscle.
Author(s) -
Yoichiro Abe,
Yoshitoshi Kasuya,
Michiyo Kudo,
Kamejiro Yamashita,
Katsutoshi Goto,
Masaki Takao,
Yoh Takuwa
Publication year - 1991
Publication title -
japanese journal of pharmacology/japanese journal of pharmacology
Language(s) - English
Resource type - Journals
eISSN - 1347-3506
pISSN - 0021-5198
DOI - 10.1254/jjp.57.431
Subject(s) - caldesmon , myosin light chain kinase , phosphorylation , myosin , endothelin 1 , chemistry , smooth muscle , medicine , contraction (grammar) , endothelin receptor , endothelin 3 , endothelins , endocrinology , microbiology and biotechnology , biology , biochemistry , calmodulin , calcium , receptor
Endothelin-1 (ET), a potent vasoconstrictor, induces a sustained increase in the phosphorylation level of the 20-kDa myosin light chain (MLC) in porcine coronary artery strips. ET also induces late phosphorylation of caldesmon, which is mimicked by 12-deoxyphorbol 13-isobutyrate, but not by 60 mM KCl. Nitroglycerin, a vasorelaxant, completely reverses the ET-induced phosphorylation of MLC, but not that of caldesmon. These results suggest an important regulatory role of MLC phosphorylation in ET-induced contraction.