Protein kinase C activity, translocation, and selective isoform subcellular redistribution in the rat cerebral cortex after in vitro ischemia

2002 ◽  
Vol 71 (1) ◽  
pp. 64-71 ◽  
Author(s):  
Rita Selvatici ◽  
Silvia Marino ◽  
Carmela Piubello ◽  
Donata Rodi ◽  
Lorenzo Beani ◽  
...  
Keyword(s):  
Cerebral Cortex ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Rat Cerebral Cortex ◽  
In Vitro Ischemia ◽  
Kinase C ◽  
Protein Kinase C Activity

Mitogen stimulation of Na+-H+ exchange: differential involvement of protein kinase C

1987 ◽  
Vol 253 (2) ◽  
pp. C219-C229 ◽  
Author(s):  
L. L. Muldoon ◽  
G. A. Jamieson ◽  
A. C. Kao ◽  
H. C. Palfrey ◽  
M. L. Villereal
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Cell Types ◽  
Intact Cells ◽  
Kinase C ◽  
Protein Kinase C Activity ◽  
Human Fibroblast Strains ◽  
Stimulation Of

The mitogen-induced activation of Na+-H+ exchange was investigated in two cultured human fibroblast strains (HSWP and WI-38 cells) that, based on previous studies, differed in their response to the tumor-promoting phorbol ester 12-O-tetradecanoylphorbol-13-acetate (TPA) (L. M. Vincentini and M. L. Villereal, Proc. Natl. Acad. Sci. USA 82: 8053-8056, 1985). The role of protein kinase C in the activation of Na+-H+ exchange was investigated by comparing the effects of TPA on Na+ influx, in vitro phosphorylation, and in vivo phosphorylation in both cell types. Although both cell types have significant quantities of protein kinase C activity that can be activated by TPA in intact cells, the addition of TPA to intact cells stimulates Na+ influx in WI-38 cells but not in HSWP cells, indicating that in HSWP cells the stimulation of protein kinase C is not sufficient to activate the Na+-H+ exchanger. Cells were then depleted of protein kinase C activity by chronic treatment with high doses of TPA. Both HSWP and WI-38 cells were rendered protein kinase C deficient by this treatment as determined by in vitro and in vivo phosphorylation studies. Protein kinase C-deficient HSWP cells lose the ability for TPA to inhibit the serum-induced activation of Na+-H+ exchange, but there is no reduction in the stimulation of Na+ influx by serum, bradykinin, vasopressin, melittin, or vanadate, indicating that protein kinase C activity is not necessary for the mitogen-induced activation of Na+-H+ exchange in HSWP cells by agents known to stimulate phosphatidylinositol turnover (G. A. Jamieson and M. Villereal. Arch. Biochem. Biophys. 252: 478-486, 1987). In contrast, depletion of protein kinase C activity in WI-38 cells significantly reduces both the TPA- and the serum-induced activation of the Na+-H+ exchange system, suggesting that protein kinase C activity is necessary for at least a portion of the mitogen-induced activation of the Na+-H+ exchanger in WI-38 cells. These results indicate that the mechanisms for regulating Na+-H+ exchange can differ dramatically between different types of fibroblasts.

Cognition stimulating drugs modulate protein kinase C activity in cerebral cortex and hippocampus of adult rats

Life Sciences ◽  
1993 ◽  
Vol 53 (24) ◽  
pp. 1821-1832 ◽  
Author(s):  
Laura Lucchi ◽  
Alessia Pascale ◽  
Fiorenzo Battaini ◽  
Stefano Govoni ◽  
Marco Trabucchi
Keyword(s):  
Cerebral Cortex ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Adult Rats ◽  
Kinase C ◽  
Protein Kinase C Activity

The Rap1A Protein Enhances Protein Kinase C Activity in Vitro

1993 ◽  
Vol 195 (3) ◽  
pp. 1321-1328 ◽  
Author(s):  
M.E. Labadia ◽  
G.M. Bokoch ◽  
C.K. Huang
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Kinase C ◽  
Protein Kinase C Activity
Sign in / Sign up

Export Citation Format

Share Document