scholarly journals GAPDH and Autophagy Preserve Survival after Apoptotic Cytochrome c Release in the Absence of Caspase Activation

Cell ◽  
2007 ◽  
Vol 130 (2) ◽  
pp. 385
Author(s):  
Anna Colell ◽  
Jean-Ehrland Ricci ◽  
Stephen Tait ◽  
Sandra Milasta ◽  
Ulrich Maurer ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Caspase Activation ◽  
Cytochrome C Release

scholarly journals Mouse mammary gland involution is associated with cytochrome c release and caspase activation

2001 ◽  
Vol 104 (1-2) ◽  
pp. 89-98 ◽  
Author(s):  
Andreas Marti ◽  
Philipp M. Ritter ◽  
Richard Jäger ◽  
Hedvika Lazar ◽  
Anna Baltzer ◽  
...  
Keyword(s):  
Mammary Gland ◽  
Cytochrome C ◽  
Mouse Mammary Gland ◽  
Caspase Activation ◽  
Cytochrome C Release ◽  
Mammary Gland Involution

Resistance of leukemic cells to 2-chlorodeoxyadenosine is due to a lack of calcium-dependent cytochrome c release

Blood ◽  
2002 ◽  
Vol 99 (2) ◽  
pp. 655-663 ◽  
Author(s):  
Joya Chandra ◽  
Emma Mansson ◽  
Vladimir Gogvadze ◽  
Scott H. Kaufmann ◽  
Freidoun Albertioni ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Dna Fragmentation ◽  
Cell Lines ◽  
Resistant Cell ◽  
Leukemic Cells ◽  
Caspase Activation ◽  
Cytochrome C Release ◽  
Deoxyguanosine Kinase ◽  
Induced Apoptosis ◽  
Resistant Cells

Abstract The purine nucleoside 2-chlorodeoxyadenosine (CdA) is often used in leukemia therapy. Its efficacy, however, is compromised by the emergence of resistant cells. In the present study, 3 CdA-resistant cell lines were generated and characterized. Their ability to accumulate 2-chloroadenosine triphosphate (CdATP) varied, reflecting differences in activities of deoxycytidine kinase (dCK) and deoxyguanosine kinase (dGK). Nonetheless, the selected lines were uniformly resistant to CdA-induced apoptosis, as assessed by caspase activation and DNA fragmentation. In contrast, cytosols from resistant cells were capable of robust caspase activation when incubated in the presence of cytochrome c and dATP. Moreover, replacement of dATP with CdATP also resulted in caspase activation in the parental and some of the resistant cell lines. Strikingly, CdA-induced decreases in mitochondrial transmembrane potential and release of cytochrome c from mitochondria were observed in the parental cells but not in any resistant lines. The lack of cytochrome c release correlated with an increased ability of mitochondria from resistant cells to sequester free Ca2+. Consistent with this enhanced Ca2+buffering capacity, an early increase in cytosolic Ca2+after CdA treatment of parental cells but not resistant cells was detected. Furthermore, CdA-resistant cells were selectively cross-resistant to thapsigargin but not to staurosporine- or Fas-induced apoptosis. In addition, CdA-induced caspase-3 activation and DNA fragmentation were inhibited by the Ca2+ chelator BAPTA-AM in sensitive cells. Taken together, the data indicate that the mechanism of resistance to CdA may be dictated by changes in Ca2+-sensitive mitochondrial events.

scholarly journals The role of cytochrome c in caspase activation in Drosophila melanogaster cells

2002 ◽  
Vol 156 (6) ◽  
pp. 1089-1098 ◽  
Author(s):  
Loretta Dorstyn ◽  
Stuart Read ◽  
Dimitrios Cakouros ◽  
Jun R. Huh ◽  
Bruce A. Hay ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Mammalian Cells ◽  
Significant Proportion ◽  
Ectopic Expression ◽  
Caspase Activation ◽  
Cytochrome C Release ◽  
Cell Extracts ◽  
Effector Caspase ◽  
Drosophila Cells

The release of cytochrome c from mitochondria is necessary for the formation of the Apaf-1 apoptosome and subsequent activation of caspase-9 in mammalian cells. However, the role of cytochrome c in caspase activation in Drosophila cells is not well understood. We demonstrate here that cytochrome c remains associated with mitochondria during apoptosis of Drosophila cells and that the initiator caspase DRONC and effector caspase DRICE are activated after various death stimuli without any significant release of cytochrome c in the cytosol. Ectopic expression of the proapoptotic Bcl-2 protein, DEBCL, also fails to show any cytochrome c release from mitochondria. A significant proportion of cellular DRONC and DRICE appears to localize near mitochondria, suggesting that an apoptosome may form in the vicinity of mitochondria in the absence of cytochrome c release. In vitro, DRONC was recruited to a >700-kD complex, similar to the mammalian apoptosome in cell extracts supplemented with cytochrome c and dATP. These results suggest that caspase activation in insects follows a more primitive mechanism that may be the precursor to the caspase activation pathways in mammals.

Involvement of cytochrome c release and caspase activation in toosendanin-induced PC12 cell apoptosis

Toxicology ◽  
2004 ◽  
Vol 201 (1-3) ◽  
pp. 31-38 ◽  
Author(s):  
Mian-Zhi Tang ◽  
Zhong-Feng Wang ◽  
Yu-Liang Shi
Keyword(s):  
Cytochrome C ◽  
Pc12 Cell ◽  
Cell Apoptosis ◽  
Caspase Activation ◽  
Cytochrome C Release

Apoptosis is induced by caspase activation and cytochrome c release in photodynamic therapy (PDT) of human hepatoteilular carcinoma cells

2001 ◽  
Vol 120 (5) ◽  
pp. A363
Author(s):  
Akihiko Okumura ◽  
Michael R. Hamblin ◽  
Tayaba Hasan ◽  
Tetsuya Ishikawa ◽  
Shinichi Kakumu ◽  
...  
Keyword(s):  
Photodynamic Therapy ◽  
Cytochrome C ◽  
Carcinoma Cells ◽  
Caspase Activation ◽  
Cytochrome C Release

scholarly journals Corrigendum to: Cytochrome c release and caspase activation in hydrogen peroxide- and tributyltin-induced apoptosis (FEBS 20394)

FEBS Letters ◽  
1998 ◽  
Vol 437 (1-2) ◽  
pp. 163-163 ◽  
Author(s):  
Hélène Stridh ◽  
Monica Kimland ◽  
Dean P. Jones ◽  
Sten Orrenius ◽  
Mark B. Hampton
Keyword(s):  
Hydrogen Peroxide ◽  
Cytochrome C ◽  
Caspase Activation ◽  
Cytochrome C Release ◽  
Induced Apoptosis
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