Mitochondrial dysfunction: A crucial event in okadaic acid (ICV) induced memory impairment and apoptotic cell death in rat brain

2011 ◽  
Vol 100 (2) ◽  
pp. 311-319 ◽  
Author(s):  
Pradeep K. Kamat ◽  
Santoshkumar Tota ◽  
Rakesh Shukla ◽  
Shakir Ali ◽  
Abul Kalam Najmi ◽  
...  
Keyword(s):  
Cell Death ◽  
Mitochondrial Dysfunction ◽  
Rat Brain ◽  
Okadaic Acid ◽  
Memory Impairment ◽  
Apoptotic Cell ◽  
Apoptotic Cell Death

scholarly journals Effect of Transient Maternal Hypotension on Apoptotic Cell Death in Foetal Rat Brain

2014 ◽  
Vol 33 (1) ◽  
pp. 88-94
Author(s):  
Hamit Ozyurek ◽  
Sibel Bayrak ◽  
Bilge Pehlivanoglu ◽  
Pergin Atilla ◽  
Zeynep Dicle Balkanci ◽  
...  
Keyword(s):  
Cell Death ◽  
Rat Brain ◽  
Apoptotic Cell ◽  
Apoptotic Cell Death ◽  
Foetal Rat

Protein Phosphatase 2A Inactivates Bcl2’s Antiapoptotic Function by Dephosphorylation and Up-Regulation of Bcl2-p53 Binding.

Blood ◽  
2006 ◽  
Vol 108 (11) ◽  
pp. 1436-1436
Author(s):  
Xingming Deng ◽  
Fengqin Gao ◽  
Tammy Flagg ◽  
W. Stratford May
Keyword(s):  
Cell Death ◽  
Cell Survival ◽  
Okadaic Acid ◽  
Protein Phosphatase ◽  
Apoptotic Cell ◽  
Protein Phosphatase 2A ◽  
Survival Function ◽  
Phosphorylation Site ◽  
Apoptotic Cell Death ◽  
Phosphatase 2A

Abstract DNA damage-induced p53/Bcl2 interaction at the outer mitochondrial membranes results in a Bcl2 conformational change and loss of its antiapoptotic function. Our data now indicate that either treatment of cells with the protein phosphatase 2A (PP2A) inhibitor, okadaic acid (10 nM), or specific disruption of PP2A activity by the expression of SV40 small tumor antigen enhances Bcl2 phosphorylation and suppresses the cisplatin-stimulated Bcl2-p53 interaction in association with prolonged cell survival. By contrast, C2-ceramide, a potent PP2A activator, reduces Bcl2 phosphorylation and increases Bcl2-p53 binding and promotes apoptotic cell death, suggesting that PP2A may function as a physiological regulator of Bcl2 by, at least in part, affecting its association with p53. Overexpression of the PP2A catalytic subunit (PP2A/C) suppresses Bcl2 phosphorylation in association with increased p53-Bcl2 binding and apoptotic cell death. By contrast, specific depletion of PP2A/C by RNA interference enhances Bcl2 phosphorylation, suppresses p53-Bcl2 interaction and prolongs cell survival. Purified PP2A can directly enhance the formation of the p53-Bcl2 complex in vitro in an okadaic acid-sensitive manner, supporting a direct mechanism. Importantly, PP2A directly interacts with Bcl2 at its BH4 domain which may function as the PP2A ‘docking site’ to potentially ‘bridge’ PP2A to the flexible loop domain which contains the physiological serine 70 phosphorylation site. Thus, PP2A may provide a double whammy to Bcl2’s survival function by both dephosphorylating and enhancing p53-Bcl2 binding. Therapeutically stimulating Bcl2 dephosphorylation and/or increasing Bcl2/p53 binding by activating PP2A may represent an efficient and novel antineoplastic approach.

scholarly journals N-Methyl-D-aspartate antagonists and apoptotic cell death triggered by head trauma in developing rat brain

1999 ◽  
Vol 96 (5) ◽  
pp. 2508-2513 ◽  
Author(s):  
D. Pohl ◽  
P. Bittigau ◽  
M. J. Ishimaru ◽  
D. Stadthaus ◽  
C. Hubner ◽  
...  
Keyword(s):  
Cell Death ◽  
Rat Brain ◽  
Head Trauma ◽  
Apoptotic Cell ◽  
Apoptotic Cell Death ◽  
Developing Rat

Lipopolysaccharide-induced fever is dissociated from apoptotic cell death in the rat brain

1998 ◽  
Vol 805 (1-2) ◽  
pp. 95-103 ◽  
Author(s):  
Abdeslam Mouihate ◽  
Quentin J Pittman
Keyword(s):  
Cell Death ◽  
Rat Brain ◽  
Apoptotic Cell ◽  
Apoptotic Cell Death
Sign in / Sign up

Export Citation Format

Share Document