scholarly journals Inotropic Effects of Staurosporine, NA 0345 and H-7, Protein Kinase C Inhibitors, on Rabbit Ventricular Myocardium: Selective Inhibition of the Positive Inotropic Effect Mediated by α1-Adrenoceptors

1993 ◽  
Vol 63 (1) ◽  
pp. 17-26 ◽  
Author(s):  
Masao Endoh ◽  
Ikuo Norota ◽  
Masahiro Takanashi ◽  
Hideo Kasai
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Positive Inotropic Effect ◽  
Selective Inhibition ◽  
Ventricular Myocardium ◽  
Inotropic Effect ◽  
Inotropic Effects ◽  
Protein Kinase C Inhibitors ◽  
Kinase C ◽  
Rabbit Ventricular Myocardium

Positive inotropic effect of interleukin-2. Role of phospholipases and protein kinase C

1991 ◽  
Vol 13 (5) ◽  
pp. 509-515 ◽  
Author(s):  
Maria M. de E. de Bracco ◽  
Susana B. Fink ◽  
Marta R. Finiasz ◽  
Enri S. Borda ◽  
Leonor Sterin-Borda
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Positive Inotropic Effect ◽  
Interleukin 2 ◽  
Inotropic Effect ◽  
Kinase C

Protein kinase C is not involved in alpha 1-adrenoceptor-mediated positive inotropic effect

1991 ◽  
Vol 260 (1) ◽  
pp. H27-H36 ◽  
Author(s):  
M. Endou ◽  
Y. Hattori ◽  
N. Tohse ◽  
M. Kanno
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Positive Inotropic Effect ◽  
Negative Inotropic Effect ◽  
Inotropic Effect ◽  
Kinase C ◽  
Protein Kinase C Inhibitor ◽  
Prolongation Of Action Potential ◽  
Electrophysiological Effects

This study was performed to determine whether activation of protein kinase C is responsible for the positive inotropic effect of alpha 1-adrenoceptor stimulation in rat papillary muscle. In the presence of 1 microM propranolol, phenylephrine (10 microM) produced triphasic inotropic response that was accompanied by prolongation of action potential duration (APD) and hyperpolarization of membrane potential. Phorbol 12,13-dibutyrate (PDBu, 0.1 microM) abolished the negative inotropic effect of phenylephrine and apparently resulted in enhancement of the positive inotropic effect. PDBu also attenuated the phenylephrine-induced hyperpolarization without affecting the APD prolongation. However, such changes were not observed with 12-O-tetradecanoylphorbol-13-acetate (TPA, 0.1 microM). Neither PDBu nor TPA increased the force of contraction or prolonged APD similar to phenylephrine. The protein kinase C inhibitor 1-(5-isoquinolinylsulfonyl)-2-methyl-piperazine (H 7, 10 microM) did not suppress the changes induced by PDBu, and more importantly H 7 did not affect the inotropic and electrophysiological effects of phenylephrine. Both TPA and PDBu significantly inhibited the phenylephrine-induced phosphoinositide hydrolysis as measured by [3H]inositol monophosphate, and these inhibitory effects were eliminated in the presence of H 7. Our results provide an argument against a role of protein kinase C activation in the alpha 1-adrenoceptor-mediated inotropic and electrophysiological effects.

scholarly journals N-Acetylcysteine and α-cyano-4-hydroxycinnamic acid alter protein kinase C (PKC)-δ and PKC-ζ and diminish dysmorphogenesis in rat embryos cultured with high glucose in vitro

2007 ◽  
Vol 192 (1) ◽  
pp. 207-214 ◽  
Author(s):  
Mattias Gäreskog ◽  
Parri Wentzel
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
High Glucose ◽  
Culture Medium ◽  
Hydroxycinnamic Acid ◽  
Oxygen Species ◽  
Rat Embryos ◽  
Protein Kinase C Inhibitors ◽  
Kinase C

Malformations and growth disturbances are two- to threefold more common in infants of diabetic mothers than in offspring of non-diabetic pregnancy. Several suggestions have emerged to explain the reasons for diabetic embryopathy, including enhanced mitochondrial production of reactive oxygen species leading to altered activation of protein kinase C. This study aimed to evaluate the effect of α-cyano-4-hydroxycinnamic acid (CHC) and N-acetylcysteine (NAC) addition on morphology and activity of protein kinase C-δ and protein kinase C-ζ in rat embryos exposed to a high glucose concentration in vitro. Day 9 embryos from normal rats were cultured in 10 or 30 mM glucose concentrations with or without supplementation of CHC, NAC, or protein kinase C inhibitors specific for protein kinase C-δ and protein kinase C-ζ. Embryos were evaluated for malformations, crown rump length, and somite number. Protein kinase C-δ and protein kinase C-ζ activities were estimated by western blot by separating membranous and cytosolic fractions of the embryo. We found increased malformations and growth retardation in embryos cultured in high versus low glucose concentrations. These abnormalities were diminished when CHC and NAC or specific protein kinase C-inhibitors were added to the culture medium. The activities of embryonic protein kinase C-δ and protein kinase C-ζ were increased in the high glucose environment after 24-h culture, but were normalized by the addition of CHC and NAC as well as respective inhibitor to the culture medium. These findings suggest that mitochondrial overproduction of reactive oxygen species is involved in diabetic embryopathy. Furthermore, such overproduction may affect embryonic development, at least partly, by enhancing the activities of protein kinase C-δ and protein kinase C-ζ.

scholarly journals Protein kinase C inhibitors for immune disorders

2014 ◽  
Vol 19 (8) ◽  
pp. 1217-1221 ◽  
Author(s):  
Amnon Altman ◽  
Kok-Fai Kong
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Immune Disorders ◽  
Protein Kinase C Inhibitors ◽  
Kinase C
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