scholarly journals Toxicity of Pb2+ on rat liver mitochondria induced by oxidative stress and mitochondrial permeability transition

2017 ◽  
Vol 6 (6) ◽  
pp. 822-830 ◽  
Author(s):  
Long Ma ◽  
Jun-Yi Liu ◽  
Jia-Xin Dong ◽  
Qi Xiao ◽  
Jie Zhao ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Rat Liver ◽  
Mitochondrial Permeability Transition ◽  
Permeability Transition ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
Isolated Rat Liver ◽  
Mitochondrial Permeability ◽  
Isolated Rat

Toxicities and mechanisms of Pb2+ on isolated rat liver mitochondria.

Effect of progesterone and its synthetic analogues on the activity of mitochondrial permeability transition pore in isolated rat liver mitochondria

2009 ◽  
Vol 78 (8) ◽  
pp. 1060-1068 ◽  
Author(s):  
Nadezhda I. Fedotcheva ◽  
Vera V. Teplova ◽  
Tatiana A. Fedotcheva ◽  
Vladimir M. Rzheznikov ◽  
Nikolai L. Shimanovskii
Keyword(s):  
Rat Liver ◽  
Mitochondrial Permeability Transition Pore ◽  
Mitochondrial Permeability Transition ◽  
Permeability Transition Pore ◽  
Permeability Transition ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
Isolated Rat Liver ◽  
Mitochondrial Permeability ◽  
Isolated Rat

scholarly journals Toxicity of Evodiae fructus on Rat Liver Mitochondria: The Role of Oxidative Stress and Mitochondrial Permeability Transition

Molecules ◽  
2014 ◽  
Vol 19 (12) ◽  
pp. 21168-21182 ◽  
Author(s):  
Qingyan Cai ◽  
Jingjing Wei ◽  
Wei Zhao ◽  
Si Shi ◽  
Yu Zhang ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Rat Liver ◽  
Mitochondrial Permeability Transition ◽  
Permeability Transition ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
Mitochondrial Permeability

scholarly journals Closure of VDAC causes oxidative stress and accelerates the Ca2+-induced mitochondrial permeability transition in rat liver mitochondria

2010 ◽  
Vol 495 (2) ◽  
pp. 174-181 ◽  
Author(s):  
Andrey Tikunov ◽  
C. Bryce Johnson ◽  
Peter Pediaditakis ◽  
Nikolai Markevich ◽  
Jeffrey M. Macdonald ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Rat Liver ◽  
Mitochondrial Permeability Transition ◽  
Permeability Transition ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
Mitochondrial Permeability

scholarly journals Cd2+ -promoted mitochondrial permeability transition: a comparison with other heavy metals.

2004 ◽  
Vol 51 (2) ◽  
pp. 545-551 ◽  
Author(s):  
Elena A Belyaeva ◽  
Vadim V Glazunov ◽  
Sergey M Korotkov
Keyword(s):  
Heavy Metal Ions ◽  
Inhibitory Action ◽  
Mitochondrial Permeability Transition ◽  
Permeability Transition ◽  
Liver Mitochondria ◽  
Basal Respiration ◽  
Rat Liver Mitochondria ◽  
Isolated Rat Liver ◽  
Mitochondrial Permeability ◽  
Isolated Rat

We compared action of Cd(2+), Hg(2+), and Cu(2+) on isolated rat liver mitochondria in the absence of added Ca(2+) and P(i). The heavy-metal ions produced dose-dependently: (1) enhanced membrane permeabilization manifested in mitochondrial swelling and activation of basal respiration, (2) inhibition of uncoupler-stimulated respiration, and (3) membrane potential dissipation. Among the metals, Cu(2+) exhibited maximal stimulatory effect on basal respiration and minimal inhibitory action on DNP-uncoupled respiration whilst Cd(2+) promoted the strongest depression of uncoupled respiration and the largest swelling in NH(4)NO(3) medium. Dithiothreitol induced a basal respiration release if added after high [Cd(2+)] and [Hg(2+)], and the stimulation was CsA-insensitive.

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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