scholarly journals Altered regulation of glycogen metabolism by vasopressin and phenylephrine in hepatocytes from insulin-resistant obese (fa/fa) rats. Role of protein kinase C

1990 ◽  
Vol 269 (3) ◽  
pp. 795-799 ◽  
Author(s):  
G van de Werve ◽  
D Massillon
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Glycogen Synthase ◽  
Rat Hepatocytes ◽  
Glycogen Metabolism ◽  
Hormonal Control ◽  
Maximal Response ◽  
Insulin Resistant ◽  
Kinase C

The hormonal control of glycogen synthase and phosphorylase interconversion was investigated in hepatocytes isolated from lean and genetically obese (fa/fa) rats. In cells from obese animals, the inactivation of synthase by 4 β-phorbol 12 β-myristate 13 alpha-acetate (PMA), phospholipase C, vasopressin and the alpha 1-adrenergic agonist phenylephrine was markedly impaired, and the property of PMA to counteract phosphorylase activation by phenylephrine was attenuated. The maximal response of phosphorylase activation to phenylephrine and vasopressin was increased in obese-rat hepatocytes, but the sensitivity to these hormones was similar to that in lean-rat hepatocytes. These observations indicate that the defect in protein kinase C that we reported previously in heart of insulin-resistant fa/fa rats [van de Werve, Zaninetti, Lang, Vallotton & Jeanrenaud (1987) Diabetes 36, 310-319] is probably also expressed in liver.

Role of protein kinase C in the regulation of rat liver glycogen synthase

1987 ◽  
Vol 252 (1) ◽  
pp. 81-90 ◽  
Author(s):  
Hiroki Nakabayashi ◽  
Kai-Foon Jesse Chan ◽  
Kuo-Ping Huang
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Rat Liver ◽  
Glycogen Synthase ◽  
Liver Glycogen ◽  
Kinase C

The role of protein kinase C in the increased generation in isolated rat hepatocytes of the hydroxyl radical by puromycin aminonucleoside

2000 ◽  
Vol 32 (6) ◽  
pp. 487-496 ◽  
Author(s):  
Kazumasa Aoyagi ◽  
Siranoush Shahrzad ◽  
Yutaka Kuzure ◽  
Akio Koyama ◽  
Ko Nakamura ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Hydroxyl Radical ◽  
Rat Hepatocytes ◽  
Puromycin Aminonucleoside ◽  
Isolated Rat Hepatocytes ◽  
Kinase C ◽  
Isolated Rat

Role of protein kinase C in nonsensitized and passively sensitized human isolated bronchial smooth muscle

1995 ◽  
Vol 268 (6) ◽  
pp. L966-L971 ◽  
Author(s):  
M. Rossetti ◽  
J. P. Savineau ◽  
H. Crevel ◽  
R. Marthan
Keyword(s):  
Smooth Muscle ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Maximal Response ◽  
Bronchial Smooth Muscle ◽  
Kinase C ◽  
Passive Sensitization ◽  
Pkc Activation

To examine the role of protein kinase C (PKC) activation in the control of the mechanical activity of human isolated bronchial smooth muscle obtained at thoracotomy, the effect of the phorbol ester phorbol 12,13-dibutyrate (PDB) was evaluated. PDB produced slowly developing and sustained contractions that were reduced 1) by the PKC inhibitor staurosporine and 2) after long-term (12 h) exposure to PDB, which downregulates PKC. Moreover, the inactive phorbol ester 4 alpha-phorbol 12,13 didecanoate had no contractile effect. Removal of external Ca2+ or addition of the Ca(2+)-channel antagonist verapamil reduced the PDB-induced contraction. Passive sensitization of human isolated bronchial rings, i.e., incubation overnight of tissues in serum from atopic asthmatic patients, decreased the maximal response to PDB to 28.9 +/- 8% of the maximal response to acetylcholine (ACh) when compared with that of paired nonsensitized rings, i.e., tissues incubated overnight in serum from normal subjects (46.7 +/- 9.4% of the maximal response to ACh, n = 5, P < 0.05). The decrease in the response to PDB induced by either long-term preexposure to PDB or passive sensitization was reversed when both types of tissues were allowed to recover unstimulated for 3 h before PDB application. These results show that 1) PKC activation induces maintained contractions in human isolated airway smooth muscle that are largely dependent on extracellular calcium; 2) passive sensitization alters the PKC-mediated response in a way similar to that induced by prolonged stimulation of PKC.

scholarly journals The role of cytosolic Ca2+, protein kinase C, and protein kinase A in hormonal stimulation of phospholipase D in rat hepatocytes.

1994 ◽  
Vol 269 (2) ◽  
pp. 849-859
Author(s):  
L. Gustavsson ◽  
G. Moehren ◽  
M.E. Torres-Marquez ◽  
C. Benistant ◽  
R. Rubin ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Protein Kinase A ◽  
Phospholipase D ◽  
Rat Hepatocytes ◽  
Hormonal Stimulation ◽  
Kinase C ◽  
Kinase A ◽  
Stimulation Of

Role of protein kinase C in the regulation of steroidogenesis in the mouse Leydig cell

1986 ◽  
Vol 113 (1_Suppl) ◽  
pp. S63-S64
Author(s):  
A. K. MUKHOPADHYAY ◽  
H. G. BOHNET
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Leydig Cell ◽  
Kinase C ◽  
Mouse Leydig Cell

scholarly journals Dysregulation of protein kinase C in adult depression and suicide: evidence from postmortem brain studies

2021 ◽  
Author(s):  
Ghanshyam N Pandey ◽  
Anuradha Sharma ◽  
Hooriyah S Rizavi ◽  
Xinguo Ren
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Protein Expression ◽  
Mrna Expression ◽  
Postmortem Brain ◽  
Cortical Region ◽  
Cytosol Fraction ◽  
Kinase C ◽  
Pkc Isozymes

Abstract Background Several lines of evidence suggest the abnormalities of protein kinase C (PKC) signaling system in mood disorders and suicide based primarily on the studies of PKC and its isozymes in the platelets and postmortem brain of depressed and suicidal subjects. In this study we examined the role of PKC isozymes in depression and suicide. Methods We determined the protein and mRNA expression of various PKC isozymes in the prefrontal cortical region [Brodmann area 9 (BA9)] in 24 normal control (NC) subjects, 24 depressed suicide (DS) subjects and 12 depressed non-suicide (DNS) subjects. The levels of mRNA in the prefrontal cortex (PFC) were determined by qRT-PCR and the protein expression was determined by Western blotting. Results We observed a significant decrease in mRNA expression of PKCα, PKCβI, PKCδ and PKCε and decreased protein expression either in the membrane or the cytosol fraction of PKC isozymes - PKCα, PKCβI, PKCβII and PKCδ in DS and DNS subjects compared with NC subjects. Conclusions The current study provides detailed evidence of specific dysregulation of certain PKC isozymes in the postmortem brain of DS and DNS subjects and further supports earlier evidence for the role of PKC in the platelets and brain of adult and teenage depressed and suicidal population. This comprehensive study may lead to further knowledge of the involvement of PKC in the pathophysiology of depression and suicide.

scholarly journals Role of cadmium in activating nuclear protein kinase C and the enzyme binding to nuclear protein.

1992 ◽  
Vol 267 (28) ◽  
pp. 19824-19828
Author(s):  
C Block ◽  
S Freyermuth ◽  
D Beyersmann ◽  
A.N. Malviya
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Nuclear Protein ◽  
Enzyme Binding ◽  
Kinase C
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