scholarly journals The apoptosis/necrosis transition in cerebellar granule cells depends on the mutual relationship of the antioxidant and the proteolytic systems which regulate ROS production and cytochrome c release en route to death

2003 ◽  
Vol 84 (5) ◽  
pp. 960-971 ◽  
Author(s):  
Anna Atlante ◽  
Antonella Bobba ◽  
Pietro Calissano ◽  
Salvatore Passarella ◽  
Ersilia Marra
Keyword(s):  
Cytochrome C ◽  
Granule Cells ◽  
Cerebellar Granule Cells ◽  
Ros Production ◽  
Mutual Relationship ◽  
Cytochrome C Release ◽  
Cerebellar Granule ◽  
Relationship Of

Early release and subsequent caspase-mediated degradation of cytochrome c in apoptotic cerebellar granule cells

FEBS Letters ◽  
1999 ◽  
Vol 457 (1) ◽  
pp. 126-130 ◽  
Author(s):  
A. Bobba ◽  
A. Atlante ◽  
S. Giannattasio ◽  
G. Sgaramella ◽  
P. Calissano ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Granule Cells ◽  
Cerebellar Granule Cells ◽  
Cerebellar Granule ◽  
Early Release

scholarly journals Bid-induced Conformational Change of Bax Is Responsible for Mitochondrial Cytochrome c Release during Apoptosis

1999 ◽  
Vol 144 (5) ◽  
pp. 891-901 ◽  
Author(s):  
Solange Desagher ◽  
Astrid Osen-Sand ◽  
Anthony Nichols ◽  
Robert Eskes ◽  
Sylvie Montessuit ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Conformational Change ◽  
Granule Cells ◽  
Cerebellar Granule Cells ◽  
Tumor Cell Lines ◽  
Cytochrome C Release ◽  
Isolated Mitochondria ◽  
Bh3 Domain ◽  
Direct Binding ◽  
Induced Apoptosis

Here we report that in staurosporine-induced apoptosis of HeLa cells, Bid, a BH3 domain containing protein, translocates from the cytosol to mitochondria. This event is associated with a change in conformation of Bax which leads to the unmasking of its NH2-terminal domain and is accompanied by the release of cytochrome c from mitochondria. A similar finding is reported for cerebellar granule cells undergoing apoptosis induced by serum and potassium deprivation. The Bax-conformational change is prevented by Bcl-2 and Bcl-xL but not by caspase inhibitors. Using isolated mitochondria and various BH3 mutants of Bid, we demonstrate that direct binding of Bid to Bax is a prerequisite for Bax structural change and cytochrome c release. Bcl-xL can inhibit the effect of Bid by interacting directly with Bax. Moreover, using mitochondria from Bax-deficient tumor cell lines, we show that Bid- induced release of cytochrome c is negligible when Bid is added alone, but dramatically increased when Bid and Bax are added together. Taken together, our results suggest that, during certain types of apoptosis, Bid translocates to mitochondria and binds to Bax, leading to a change in conformation of Bax and to cytochrome c release from mitochondria.

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