L. Bouchier-hayes, L. Lartigue, and D. Newmeyer, Mitochondria: pharmacological manipulation of cell death, Journal of Clinical Investigation, vol.115, issue.10, pp.2640-2647, 2005.
DOI : 10.1172/JCI26274DS1

S. Desagher and J. Martinou, Mitochondria as the central control point of apoptosis, Trends in Cell Biology, vol.10, issue.9, pp.369-377, 2000.
DOI : 10.1016/S0962-8924(00)01803-1

M. Duchen, Mitochondria and calcium: from cell signalling to cell death, The Journal of Physiology, vol.525, issue.1, pp.57-68, 2000.
DOI : 10.1111/j.1469-7793.2000.00057.x

X. Saelens, N. Festjens, V. Walle, L. Van-gurp, M. Van-loo et al., Toxic proteins released from mitochondria in cell death, Oncogene, vol.23, issue.16, pp.2861-2874, 2004.
DOI : 10.1038/sj.onc.1207523

P. Bernardi, A. Krauskopf, E. Basso, V. Petronilli, and E. Blachly-dyson, The mitochondrial permeability transition from in vitro artifact to disease target, FEBS Journal, vol.14, issue.10, pp.2077-2099, 2006.
DOI : 10.1093/hmg/7.13.2135

M. Zoratti and I. Szabo, The mitochondrial permeability transition, Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, vol.1241, issue.2, pp.139-176, 1995.
DOI : 10.1016/0304-4157(95)00003-A

C. Batandier, X. Leverve, and E. Fontaine, Opening of the Mitochondrial Permeability Transition Pore Induces Reactive Oxygen Species Production at the Level of the Respiratory Chain Complex I, Journal of Biological Chemistry, vol.279, issue.17, pp.17197-17204, 2004.
DOI : 10.1074/jbc.M310329200
URL : https://hal.archives-ouvertes.fr/inserm-00389920

S. Kantrow and C. Piantadosi, Release of Cytochrome c from Liver Mitochondria during Permeability Transition, Biochemical and Biophysical Research Communications, vol.232, issue.3, pp.669-671, 1997.
DOI : 10.1006/bbrc.1997.6353

D. Zorov, C. Filburn, L. Klotz, J. Zweier, and S. Sollott, Reactive Oxygen Species (Ros-Induced) Ros Release, The Journal of Experimental Medicine, vol.75, issue.7, pp.1001-1014, 2000.
DOI : 10.1016/0014-5793(93)81423-W

R. Haworth and D. Hunter, The Ca2+-induced membrane transition in mitochondria, Archives of Biochemistry and Biophysics, vol.195, issue.2, pp.460-467, 1979.
DOI : 10.1016/0003-9861(79)90372-2

E. Basso, L. Fante, J. Fowlkes, V. Petronilli, and M. Forte, Properties of the Permeability Transition Pore in Mitochondria Devoid of Cyclophilin D, Journal of Biological Chemistry, vol.280, issue.19, pp.18558-18561, 2005.
DOI : 10.1074/jbc.C500089200

M. Crompton, Mitochondrial intermembrane junctional complexes and their role in cell death, The Journal of Physiology, vol.90, issue.3, pp.11-21, 2000.
DOI : 10.1111/j.1469-7793.2000.00011.x

F. Ichas and J. Mazat, From calcium signaling to cell death: two conformations for the mitochondrial permeability transition pore. Switching from low- to high-conductance state, Biochimica et Biophysica Acta (BBA) - Bioenergetics, vol.1366, issue.1-2, pp.33-50, 1998.
DOI : 10.1016/S0005-2728(98)00119-4

G. Kroemer and J. Reed, Mitochondrial control of cell death, Nature Medicine, vol.6, issue.5, pp.513-519, 2000.
DOI : 10.1038/74994

C. Baines, R. Kaiser, N. Purcell, N. Blair, and H. Osinska, Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death, Nature, vol.65, issue.7033, pp.658-662, 2005.
DOI : 10.1038/sj.gt.3301048

T. Nakagawa, S. Shimizu, T. Watanabe, O. Yamaguchi, and K. Otsu, Cyclophilin D-dependent mitochondrial permeability transition regulates some necrotic but not apoptotic cell death, Nature, vol.12, issue.7033, pp.652-658, 2005.
DOI : 10.1084/jem.189.11.1699

A. Schinzel, O. Takeuchi, Z. Huang, J. Fisher, and Z. Zhou, Cyclophilin D is a component of mitochondrial permeability transition and mediates neuronal cell death after focal cerebral ischemia, Proceedings of the National Academy of Sciences, vol.102, issue.34, pp.12005-12010, 2005.
DOI : 10.1073/pnas.0505294102

C. Piot, P. Croisille, P. Staat, H. Thibault, and G. Rioufol, Effect of Cyclosporine on Reperfusion Injury in Acute Myocardial Infarction, New England Journal of Medicine, vol.359, issue.5, pp.473-481, 2008.
DOI : 10.1056/NEJMoa071142
URL : https://hal.archives-ouvertes.fr/hal-00428144

D. Oliveira, F. Chauvin, C. Ronot, X. Mousseau, M. Leverve et al., Effects of permeability transition inhibition and decrease in cytochrome c content on doxorubicin toxicity in K562 cells, Oncogene, vol.336, issue.18, pp.2646-2655, 2006.
DOI : 10.1038/sj.onc.1209293
URL : https://hal.archives-ouvertes.fr/inserm-00388731

P. Klohn, M. Soriano, W. Irwin, D. Penzo, and L. Scorrano, Early resistance to cell death and to onset of the mitochondrial permeability transition during hepatocarcinogenesis with 2-acetylaminofluorene, Proceedings of the National Academy of Sciences, vol.100, issue.17, pp.10014-10019, 2003.
DOI : 10.1073/pnas.1633614100

J. Armstrong, Mitochondria: a target for cancer therapy, British Journal of Pharmacology, vol.124, issue.(Suppl 1), pp.239-248, 2006.
DOI : 10.1038/sj.bjp.0706556

E. Fontaine and P. Bernardi, Progress on the mitochondrial permeability transition pore: regulation by complex I and ubiquinone analogs, Journal of Bioenergetics and Biomembranes, vol.31, issue.4, pp.335-345, 1999.
DOI : 10.1023/A:1005475802350

E. Fontaine, F. Ichas, and P. Bernardi, A Ubiquinone-binding Site Regulates the Mitochondrial Permeability Transition Pore, Journal of Biological Chemistry, vol.273, issue.40, pp.25734-25740, 1998.
DOI : 10.1074/jbc.273.40.25734

L. Walter, H. Miyoshi, X. Leverve, P. Bernard, and E. Fontaine, Regulation of the Mitochondrial Permeability Transition Pore by Ubiquinone Analogs. A Progress Report, Free Radical Research, vol.36, issue.4, pp.405-412, 2002.
DOI : 10.1080/10715760290021252
URL : https://hal.archives-ouvertes.fr/inserm-00389972

L. Walter, V. Nogueira, X. Leverve, M. Heitz, and P. Bernardi, Three Classes of Ubiquinone Analogs Regulate the Mitochondrial Permeability Transition Pore through a Common Site, Journal of Biological Chemistry, vol.275, issue.38, pp.29521-29527, 2000.
DOI : 10.1074/jbc.M004128200
URL : https://hal.archives-ouvertes.fr/inserm-00390044

J. Armstrong, M. Whiteman, P. Rose, and D. Jones, The Coenzyme Q10 Analog Decylubiquinone Inhibits the Redox-activated Mitochondrial Permeability Transition: ROLE OF MITOCHONDRIAL RESPIRATORY COMPLEX III, Journal of Biological Chemistry, vol.278, issue.49, pp.49079-49084, 2003.
DOI : 10.1074/jbc.M307841200

E. Fontaine, O. Eriksson, F. Ichas, and P. Bernardi, Regulation of the Permeability Transition Pore in Skeletal Muscle Mitochondria: MODULATION BY ELECTRON FLOW THROUGH THE RESPIRATORY CHAIN COMPLEX I, Journal of Biological Chemistry, vol.273, issue.20, pp.12662-12668, 1998.
DOI : 10.1074/jbc.273.20.12662

A. Groen, H. Sips, R. Vervoorn, and J. Tager, Intracellular Compartment ation and Control of Alanine Metabolism in Rat Liver Parenchymal Cells, European Journal of Biochemistry, vol.5, issue.1, pp.87-93, 1982.
DOI : 10.1016/0006-3002(63)91800-6

C. Rousselle, M. Barbier, V. Comte, C. Alcouffe, and J. Clement-lacroix, INNOCUOUSNESS AND INTRACELLULAR DISTRIBUTION OF PKH67: A FLUORESCENT PROBE FOR CELL PROLIFERATION ASSESSMENT, In Vitro Cellular & Developmental Biology - Animal, vol.41, issue.10, pp.646-655, 2001.
DOI : 10.1290/1071-2690(2001)037<0646:IAIDOP>2.0.CO;2

V. Nogueira, D. A. Walter, L. Rigoulet, M. Leverve, and X. , Effects of Decreasing Mitochondrial Volume on the Regulation of the Permeability Transition Pore, Journal of Bioenergetics and Biomembranes, vol.1241, issue.1, pp.25-33, 2005.
DOI : 10.1007/s10863-005-4120-3
URL : https://hal.archives-ouvertes.fr/inserm-00388765

C. Chauvin, D. Oliveira, F. Ronot, X. Mousseau, M. Leverve et al., Rotenone Inhibits the Mitochondrial Permeability Transition-induced Cell Death in U937 and KB Cells, Journal of Biological Chemistry, vol.276, issue.44, pp.41394-41398, 2001.
DOI : 10.1074/jbc.M106417200
URL : https://hal.archives-ouvertes.fr/inserm-00389984

D. Detaille, B. Guigas, C. Chauvin, C. Batandier, and E. Fontaine, Metformin Prevents High-Glucose-Induced Endothelial Cell Death Through a Mitochondrial Permeability Transition-Dependent Process, Diabetes, vol.54, issue.7, pp.2179-2187, 2005.
DOI : 10.2337/diabetes.54.7.2179
URL : https://hal.archives-ouvertes.fr/inserm-00388755

B. Guigas, D. Detaille, C. Chauvin, C. Batandier, D. Oliveira et al., study, Biochemical Journal, vol.382, issue.3, pp.877-884, 2004.
DOI : 10.1042/BJ20040885
URL : https://hal.archives-ouvertes.fr/inserm-00387151