We have provided evidence that mitochondrial membrane permeability transition induced by inorganic phosphate, uncouplers or prooxidants such as t-butyl hydroperoxide and diamide is caused by a Ca2+-stimulated production of reactive oxygen species (ROS) by the respiratory chain, at the level of the coenzyme Q. The ROS attack to membrane protein thiols produces cross-linkage reactions, that may open membrane pores upon Ca2+ binding. Studies with submitochondrial particles have demonstrated that the binding of Ca2+ to these particles (possibly to cardiolipin) induces lipid lateral phase separation detected by electron paramagnetic resonance experiments exploying stearic acids spin labels. This condition leads to a disorganization of respiratory chain components, favoring ROS production and consequent protein and lipid oxidation.
The Role of Reactive Oxygen Species in Mitochondrial Permeability Transition
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Anibal E. Vercesi, Alicia J. Kowaltowski, Mercedes T. Grijalba, André R. Meinicke, Roger F. Castilho; The Role of Reactive Oxygen Species in Mitochondrial Permeability Transition. Biosci Rep 1 February 1997; 17 (1): 43–52. doi: https://doi.org/10.1023/A:1027335217774
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