Open AccessProtein Kinase Cδ but not PKCε Activity is Involved in Contractile Potentiation by Endothelin-1 in the Porcine Coronary Artery
Author(s) -
Kazuo Obara,
Masayo Koide,
Tomohisa Ishikawa,
Yuji Tanabe,
Koichi Nakayama
Publication year - 2000
Publication title -
journal of cardiovascular pharmacology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.762
H-Index - 100
eISSN - 1533-4023
pISSN - 0160-2446
DOI - 10.1097/00005344-200036051-00038
Subject(s) - protein kinase c , long term potentiation , myosin light chain kinase , cytosol , contraction (grammar) , medicine , endothelin 1 , myosin , endocrinology , endothelin receptor , phosphorylation , chemistry , biology , microbiology and biotechnology , biochemistry , enzyme , receptor
To clarify the mechanism of contractile strengthening by endothelin-1 (ET-1), we measured translocation of protein kinase C (PKC) from the cytosol to the membrane fraction in the porcine coronary artery. ET-1 potentiated the serotonin- (5-hydroxytryptamine, 5-HT) induced contraction without any additional increase in myosin light chain phosphorylation. Four PKC isoforms (alpha, beta1, delta, and zeta) were identified but not PKC epsilon. Only PKC delta was translocated from the cytosolic to the membrane fraction during the contractile potentiation by ET-1. Our results suggest that the activity of PKC delta but not PKC epsilon is involved in the contractile strengthening by ET-1 in the porcine coronary artery.