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2018/01/18
EGF receptor kinase suppresses ciliogenesis through activation of USP8 deubiquitinase

2017/11/23
Chemokines protect vascular smooth muscle cells from cell death induced by cyclic mechanical stretch.

2017/07/29
New photic stimulating system with white light-emitting diodes to elicit electroretinograms from zebrafish larvae.

2017/03/09
Potential protective function of the sterol regulatory element binding factor 1-fatty acid desaturase 12 axis in early-stage age-related macular degeneration

2016/07/11
Activation of Sterol Regulatory Element Binding Factors by Fenofibrate and Gemfibrozil Stimulates Myelination in Zebrafish

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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