The Role of Ca2+ and Protein Kinase C in Regulation of Phosphatidylserine Synthesis in Glioma C6 Cells

1997 ◽  
pp. 1011-1018
Author(s):  
J. Barańska ◽  
M. Czarny ◽  
P. Sabała ◽  
M. Wiktorek
1999 ◽  
Vol 46 (1) ◽  
pp. 99-106 ◽  
Author(s):  
A Dygas ◽  
M Sidorko ◽  
M Bobeszko ◽  
J Barańska

In the present study we investigate the effect of exogenous sphingosine, sphingosine 1-phosphate and sphingosylphosphorylcholine on phospholipase D (PLD) activity in glioma C6 cells. The cells were prelabeled with [1-14C]palmitic acid and PLD-mediated synthesis of [14C]phosphatidylethanol was measured. Sphingosine 1-phosphate and sphingosylphosphorylcholine did not stimulate [14C]phosphatidylethanol formation either at low (0.1-10 microM) or high (25-100 microM) concentrations. On the other hand, sphingosine at concentrations of 100-250 microM strongly stimulated PLD activity as compared to the effect of phorbol ester, 12-O-tetradecanoylphorbol 13-acetate (TPA), known as a PLD activator. The effect of TPA on PLD is linked to the activation of protein kinase C. The present study also shows that sphingosine additively enhances TPA-mediated PLD activity. This is in contrast to the postulated role of sphingosine as a protein kinase C inhibitor. These results demonstrate that in glioma C6 cells sphingosine not only affects PLD independently of its effect on protein kinase C, but also is unable to block TPA-mediated PLD activity.


Neuropeptides ◽  
1998 ◽  
Vol 32 (2) ◽  
pp. 185-189 ◽  
Author(s):  
R Kaufmann ◽  
H Schafberg ◽  
M Zieger ◽  
P Henklein ◽  
G Nowak

2005 ◽  
Vol 30 (3) ◽  
pp. 349-354 ◽  
Author(s):  
Magdalena Zielińska ◽  
Barbara Zabłocka ◽  
Anna Dybel ◽  
Jan Albrecht

2000 ◽  
Vol 28 (5) ◽  
pp. A445-A445
Author(s):  
Marta Bobeszko ◽  
Anna Dygas ◽  
Irena Nalepa ◽  
Jolanta Barańska

1986 ◽  
Vol 113 (1_Suppl) ◽  
pp. S63-S64
Author(s):  
A. K. MUKHOPADHYAY ◽  
H. G. BOHNET

Author(s):  
Ghanshyam N Pandey ◽  
Anuradha Sharma ◽  
Hooriyah S Rizavi ◽  
Xinguo Ren

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.


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