The Cratylia mollis Seed Lectin Induces Membrane Permeability Transition in Isolated Rat Liver Mitochondria and a Cyclosporine A-Insensitive Permeability Transition in Trypanosoma cruzi Mitochondria

2014 ◽  
Vol 61 (4) ◽  
pp. 381-388 ◽  
Author(s):  
Mariana P. Fernandes ◽  
Ana C. R. Leite ◽  
Flavia F. B. Araújo ◽  
Sara T. O. Saad ◽  
M. O. Baratti ◽  
...  
Keyword(s):  
Trypanosoma Cruzi ◽  
Membrane Permeability ◽  
Cyclosporine A ◽  
Permeability Transition ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
Membrane Permeability Transition ◽  
Isolated Rat Liver ◽  
Cratylia Mollis ◽  
Isolated Rat

Suramin inhibits respiration and induces membrane permeability transition in isolated rat liver mitochondria

Toxicology ◽  
2001 ◽  
Vol 169 (1) ◽  
pp. 17-23 ◽  
Author(s):  
Celene F Bernardes ◽  
Marcia M Fagian ◽  
José R Meyer-Fernandes ◽  
Roger F Castilho ◽  
Anibal E Vercesi
Keyword(s):  
Membrane Permeability ◽  
Rat Liver ◽  
Permeability Transition ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
Membrane Permeability Transition ◽  
Isolated Rat Liver ◽  
Isolated Rat

Role of calcium and superoxide dismutase in sensitizing mitochondria to peroxynitrite-induced permeability transition

2004 ◽  
Vol 286 (1) ◽  
pp. H39-H46 ◽  
Author(s):  
Paul S. Brookes ◽  
Victor M. Darley-Usmar
Keyword(s):  
Superoxide Dismutase ◽  
Cytochrome C ◽  
Rat Liver ◽  
Permeability Transition ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
Isolated Rat Liver ◽  
Ptp Opening ◽  
Isolated Rat

The mitochondrial permeability transition pore (PTP) is a membrane protein complex assembled and opened in response to Ca2+ and oxidants such as peroxynitrite (ONOO–). Opening the PTP is mechanistically linked to the release of cytochrome c, which participates in downstream apoptotic signaling. However, the molecular basis of the synergistic interactions between oxidants and Ca2+ in promoting the PTP are poorly understood and are addressed in the present study. In isolated rat liver mitochondria, it was found that the timing of the exposure of the isolated rat liver mitochondria to Ca2+ was a critical factor in determining the impact of ONOO– on PTP. Specifically, addition of Ca2+ alone, or ONOO– and then Ca2+, elicited similar low levels of PTP opening, whereas ONOO– alone was ineffective. In contrast, addition of Ca2+ and then ONOO– induced extensive PTP opening and cytochrome c release. Interestingly, Cu/Zn-superoxide dismutase enhanced pore opening through a mechanism independent of its catalytic activity. These data are consistent with a model in which Ca2+ reveals a molecular target that is now reactive with ONOO–. As a test of this hypothesis, tyrosine nitration was determined in mitochondria exposed to ONOO– alone or to Ca2+ and then ONOO–, and mitochondrial membrane proteins were analyzed using proteomics. These studies suggest protein targets revealed by Ca2+ include dehydrogenases and CoA-containing enzymes. These data are discussed in the context of the role of mitochondria, Ca2+, and ONOO– in apoptotic signaling.

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