Key result
Endothelin-1 induces sustained 20-kDa myosin light chain and late caldesmon phosphorylation in porcine coronary arteries.
The study suggests an important regulatory role of myosin light chain phosphorylation in Endothelin-1-induced contraction in porcine coronary arteries.
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 KC1. 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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Abe et al. (1991) studied this question. Endothelin-1 was evaluated on Phosphorylation level of the 20-kDa myosin light chain (MLC) and caldesmon. Endothelin-1 induces a sustained increase in the phosphorylation of the 20-kDa myosin light chain and late phosphorylation of caldesmon in porcine coronary artery strips.
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