Florence Verrier

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Bcl-2 is a prosurvival factor that reportedly prevents the nonspecific permeabilization of mitochondrial membranes, yet enhances specific ADP/ATP exchange by these organelles. Here, we show that Bcl-2 enhances the ADP/ATP exchange in proteoliposomes containing the purified adenine nucleotide translocase (ANT) in isolated mitochondria and mitoplasts, as well(More)
The mitochondrial permeability transition pore complex (PTPC) is involved in the control of the mitochondrial membrane permeabilization during apoptosis, necrosis and autophagy. Indeed, the adenine nucleotide translocator (ANT) and the voltage-dependent anion channel (VDAC), two major components of PTPC, are the targets of a variety of proapoptotic(More)
The permeability transition pore complex (PTPC), a mitochondrial polyprotein complex, has been previously described to be involved in the control of mitochondrial membrane permeabilization (MMP) during chemotherapy-induced apoptosis. PTPC may contain proteins from both mitochondrial membranes [e.g., voltage-dependent anion channel (VDAC), PRAX-1, peripheral(More)
Abbreviations: 4-hydroxynonenal, (HNE); 4-methylumbelliferone, (MU); 4-methylumbelliferyl phosphate, (MUP); adenine nucleotide translocator, (ANT); apoptosis inducing factor, (AIF); bongkrekic acid, (BA); cyclosporin A, (CsA); inner membrane, (IM); lonidamine, (LND); methyl-valine cyclosporin A, (m-val-CsA); mitochondrial membrane permeabilization, (MMP);(More)
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