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2020/05/28
A novel orexin antagonist from a natural plant was discovered using zebrafish behavioural analysis

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

tPhosphorylation of Calponin Mediated by Protein Kinase C in Association with Contraction in Porcine Coronary Artery

                     
1995/03/08

Mino T, Yuasa U, Naka M, Tanaka T.
Biochem Biophys Res Commun. 1995 Mar 8;208(1):397-404.

Abstract

Calponin is an actin-associated regulatory protein in smooth muscle. We report that both endothelin-1 (ET-1) and phorbol 12, 13-dibutyrate (PDBu) caused a significant increase in phosphorylation of calponin during contraction of porcine coronary artery, while high levels of KCl were ineffective. This phosphorylation was predominantly catalyzed by activation of protein kinase C(PKC). In addition, the level of phosphorylation of calponin increased closely in association with the size of the contractile force induced by PDBu. Thus, the phosphorylation of calponin in vivo by PKC might modulate in part the contraction of smooth muscle that occurs in response to ET-1 or PDBu.

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