Cytochrome c release and caspase-3 activation during colchicine-induced apoptosis of cerebellar granule cells

1999 ◽  
Vol 11 (3) ◽  
pp. 1067-1072 ◽  
Author(s):  
A. M. Gorman ◽  
E. Bonfoco ◽  
B. Zhivotovsky ◽  
S. Orrenius ◽  
S. Ceccatelli
Keyword(s):  
Cytochrome C ◽  
Caspase 3 ◽  
Granule Cells ◽  
Cerebellar Granule Cells ◽  
Cytochrome C Release ◽  
Cerebellar Granule ◽  
Induced Apoptosis

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.

scholarly journals The role of Bax and caspase-3 in doppel-induced apoptosis of cerebellar granule cells

Prion ◽  
2012 ◽  
Vol 6 (3) ◽  
pp. 309-316 ◽  
Author(s):  
Alessandro Didonna ◽  
Joshua Sussman ◽  
Federico Benetti ◽  
Giuseppe Legname
Keyword(s):  
Caspase 3 ◽  
Granule Cells ◽  
Cerebellar Granule Cells ◽  
Cerebellar Granule ◽  
Induced Apoptosis

scholarly journals Apoptosis of Growth Plate Chondrocytes Occurs through a Mitochondrial Pathway

2007 ◽  
Vol 77 (1) ◽  
pp. 129-134 ◽  
Author(s):  
Cristina C. Teixeira ◽  
Aida P. Padron Costas ◽  
Yelena Nemelivsky
Keyword(s):  
Cytochrome C ◽  
Growth Plate ◽  
Caspase 3 ◽  
Mitochondrial Pathway ◽  
Chondrocyte Apoptosis ◽  
Cytochrome C Release ◽  
Growth Plate Chondrocytes ◽  
Chondrocyte Viability ◽  
Induced Apoptosis ◽  
Free Media

Abstract Objective: To determine the role of mitochondria in chondrocyte apoptosis induced by inorganic phosphate (Pi). Materials and Methods: Chondrocytes isolated from the growth plates of chick embryo tibia were treated with Pi in serum-free media; chondrocyte viability, mitochondrial membrane potential, cytochrome c release from mitochondria, caspase 3 activity, endonuclease activity, and DNA fragmentation were investigated. Results: Exposure to Pi for 24 hours induced apoptosis in growth plate chondrocytes through a pathway that involved loss of mitochondrial function, release of cytochrome c into the cytoplasm, increases in caspase 3 and endonuclease activities, and fragmentation of DNA. Conclusions: This study suggests that mitochondria are important players in Pi-induced apoptosis.

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 Polyamine depletion prevents camptothecin-induced apoptosis by inhibiting the release of cytochromec

2002 ◽  
Vol 282 (6) ◽  
pp. C1290-C1297 ◽  
Author(s):  
Qing Yuan ◽  
Ramesh M. Ray ◽  
Leonard R. Johnson
Keyword(s):  
Cytochrome C ◽  
Mammalian Cells ◽  
Caspase 3 ◽  
Intestinal Epithelial ◽  
Caspase 9 ◽  
Cytochrome C Release ◽  
Polyamine Synthesis ◽  
Antiapoptotic Proteins ◽  
Induced Apoptosis ◽  
Rate Limiting

C1297, 2002; 10.1152/ajpcell.00351.2001.We have shown previously that depletion of polyamines delays apoptosis induced by camptothecin in rat intestinal epithelial cells (IEC-6). Mitochondria play an important role in the regulation of apoptosis in mammalian cells because apoptotic signals induce mitochondria to release cytochrome c. The latter interacts with Apaf-1 to activate caspase-9, which in turn activates downstream caspase-3. Bcl-2 family proteins are involved in the regulation of cytochrome c release from mitochondria. In this study, we examined the effects of polyamine depletion on the activation of the caspase cascade, release of cytochrome cfrom mitochondria, and expression and translocation of Bcl-2 family proteins. We inhibited ornithine decarboxylase, the first rate-limiting enzyme in polyamine synthesis, with α-difluoromethylornithine (DFMO) to deplete cells of polyamines. Depletion of polyamines prevented camptothecin-induced release of cytochrome c from mitochondria and decreased the activity of caspase-9 and caspase-3. The mitochondrial membrane potential was not disrupted when cytochrome c was released. Depletion of polyamines decreased translocation of Bax to mitochondria during apoptosis. The expression of antiapoptotic proteins Bcl-xL and Bcl-2 was increased in DFMO-treated cells. Caspase-8 activity and cleavage of Bid were decreased in cells depleted of polyamines. These results suggest that polyamine depletion prevents IEC-6 cells from apoptosis by preventing the translocation of Bax to mitochondria, thus preventing the release of cytochrome c.

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