Publication List English

2019/10/15
C3orf70 Is Involved in Neural and Neurobehavioral Development

2019/09/22
Generation of a Triple-Transgenic Zebrafish Line for Assessment of Developmental Neurotoxicity during Neuronal Differentiation

2019/07/17
Aging-associated microstructural deterioration of vertebra in zebrafish

2019/03/18
Zebrafish yolk sac microinjection of thalidomide for assessment of developmental toxicology

2019/02/18
Toxicological Evaluation of SiO2 Nanoparticles by Zebrafish Embryo Toxicity Test

tRegulatory Mechanisms of Calponin Phosphorylation in Endothelin-1-induced Contraction of Porcine Coronary Artery.

                     
1999/01/01

Uhito Yuasa, Terumasa Mino, Michiko Naka, Isao Yada and Toshio Tanaka
J. Mol. Cell Cardiol. 31(6) 1281-1287 1999

Abstract

Calponin is an actin-associated protein that appears to play an auxiliary regulatory role in the contraction of smooth muscle. We report here on the mechanisms for regulation of calponin phosphorylation in the endothelin-1-induced contraction of porcine coronary artery. Treatment of strips of porcine artery with endothelin-1 increased calponin phosphorylation and contraction in a concentration-dependent manner. The time course of the phosphorylation was biphasic, with the response to endothelin-1. The extent of phosphorylation reached a maximum within 5 min of stimulation with 10(-7)M endothelin-1 and then it declined rapidly to reach a minimum at 20 min. A potent inhibitor of protein kinase C, GF109203X, inhibited both calponin phosphorylation and contraction that were induced by endothelin-1 at 5 min, without an inhibition for myosin light chain phosphorylation. Protein phosphatase inhibitor, okadaic acid, had no effect on the extent of phosphorylation at 5 min, but it significantly inhibited the subsequent decrease in calponin phosphorylation. In contrast, in PDBu-treated strips of coronary artery, okadaic acid caused a significant steady increase of the extent of calponin phosphorylation. Our results suggest that calponin phosphorylation might be regulated by protein kinase C and okadaic acid sensitive protein phosphatases, in the endothelin-1-induced contraction of porcine coronary artery.

Copyright 1999 Academic Press.

ŠΦ˜AƒŠƒ“ƒN

Pubmed