Faculty Opinions recommendation of Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition.

2001 ◽  
Author(s):  
Alun M Davies
Keyword(s):  
Cytochrome C ◽  
Mitochondrial Protein ◽  
Caspase Activation

scholarly journals Preservation of Mitochondrial Structure and Function after Bid- or Bax-Mediated Cytochrome c Release

2000 ◽  
Vol 150 (5) ◽  
pp. 1027-1036 ◽  
Author(s):  
Oliver von Ahsen ◽  
Christian Renken ◽  
Guy Perkins ◽  
Ruth M. Kluck ◽  
Ella Bossy-Wetzel ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Protein Import ◽  
Mitochondrial Protein ◽  
Intermembrane Space ◽  
Caspase Activation ◽  
Cytochrome C Release ◽  
Mitochondrial Protein Import ◽  
Inner Membrane ◽  
And Function

Proapoptotic members of the Bcl-2 protein family, including Bid and Bax, can activate apoptosis by directly interacting with mitochondria to cause cytochrome c translocation from the intermembrane space into the cytoplasm, thereby triggering Apaf-1–mediated caspase activation. Under some circumstances, when caspase activation is blocked, cells can recover from cytochrome c translocation; this suggests that apoptotic mitochondria may not always suffer catastrophic damage arising from the process of cytochrome c release. We now show that recombinant Bid and Bax cause complete cytochrome c loss from isolated mitochondria in vitro, but preserve the ultrastructure and protein import function of mitochondria, which depend on inner membrane polarization. We also demonstrate that, if caspases are inhibited, mitochondrial protein import function is retained in UV-irradiated or staurosporine-treated cells, despite the complete translocation of cytochrome c. Thus, Bid and Bax act only on the outer membrane, and lesions in the inner membrane occurring during apoptosis are shown to be secondary caspase-dependent events.

scholarly journals Smac, a Mitochondrial Protein that Promotes Cytochrome c–Dependent Caspase Activation by Eliminating IAP Inhibition

Cell ◽  
2000 ◽  
Vol 102 (1) ◽  
pp. 33-42 ◽  
Author(s):  
Chunying Du ◽  
Min Fang ◽  
Yucheng Li ◽  
Lily Li ◽  
Xiaodong Wang
Keyword(s):  
Cytochrome C ◽  
Mitochondrial Protein ◽  
Caspase Activation

scholarly journals Conformational change and human cytochrome c function: mutation of residue 41 modulates caspase activation and destabilizes Met-80 coordination

2013 ◽  
Vol 18 (3) ◽  
pp. 289-297 ◽  
Author(s):  
Tracy M. Josephs ◽  
Matthew D. Liptak ◽  
Gillian Hughes ◽  
Alexandra Lo ◽  
Rebecca M. Smith ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Conformational Change ◽  
Caspase Activation ◽  
Human Cytochrome ◽  
Human Cytochrome C

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

Posttranscriptional regulation of cytochrome c expression during the developmental cycle of Trypanosoma brucei

1988 ◽  
Vol 8 (11) ◽  
pp. 4625-4633
Author(s):  
A F Torri ◽  
S L Hajduk
Keyword(s):  
Steady State ◽  
Cytochrome C ◽  
Trypanosoma Brucei ◽  
Posttranscriptional Regulation ◽  
Mitochondrial Protein ◽  
Developmental Cycle ◽  
Mrna Levels ◽  
Developmentally Regulated ◽  
Partial Cdna ◽  
Steady State Levels

We examined the expression of a nucleus-encoded mitochondrial protein, cytochrome c, during the life cycle of Trypanosoma brucei. The bloodstream forms of T. brucei, the long slender and short stumpy trypanosomes, have inactive mitochondria with no detectable cytochrome-mediated respiration. The insect form of T. brucei, the procyclic trypanosomes, has fully functional mitochondria. Cytochrome c is spectrally undetectable in the bloodstream forms of trypanosomes, but during differentiation to the procyclic form, spectrally detected holo-cytochrome c accumulates rapidly. We have purified T. brucei cytochrome c and raised antibodies that react to both holo- and apo-cytochrome c. In addition, we isolated a partial cDNA to trypanosome cytochrome c. An examination of protein expression and steady-state mRNA levels in T. brucei indicated that bloodstream trypanosomes did not express cytochrome c but maintained significant steady-state levels of cytochrome c mRNA. The results suggest that in T. brucei, cytochrome c is developmentally regulated by a posttranscriptional mechanism which prevents either translation or accumulation of cytochrome c in the bloodstream trypanosomes.

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