Endothelin-1-Induced Phosphorylation of the 20-kDa Myosin Light Chain and Caldesmon in Porcine Coronary Artery Smooth Muscle. | Zendy

Yoichiro Abe | Zendy; Yoshitoshi Kasuya | Zendy; Michiyo Kudo | Zendy; Kamejiro Yamashita | Zendy; Katsutoshi Goto | Zendy; Tomoh Masaki | Zendy; Yoh Takuwa | Zendy

Open Access

Endothelin-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,

Tomoh Masaki,

Yoh Takuwa

Publication year - 1991

Publication title -

the 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.

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