The mitochondrial permeability transition

BioFactors

Volumn 8, Issue 3-4, 1998, Pages 273-281

  Bernardi, Paolo ^a,b   Colonna, Raffaele ^a   Costantini, Paola ^a   Eriksson, Ove ^a   Fontaine, Eric ^a   Ichas, François ^a   Massari, Stefano ^a   Nicolli, Annamaria ^a   Petronilli, Valeria ^a   Scorrano, Luca ^a  

^a UNIVERSITY OF PADUA MEDICAL SCHOOL   (Italy)

^b UNIVERSITY OF PADOVA   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

CYCLOSPORIN A;

BIOENERGY; CALCIUM HOMEOSTASIS; CELL DAMAGE; CELL DEATH; MEMBRANE PERMEABILITY; MITOCHONDRIAL MEMBRANE; PHOSPHOLIPID BILAYER; PRIORITY JOURNAL; REVIEW;

EID: 0032440436     PISSN: 09516433     EISSN: None     Source Type: Journal    
DOI: 10.1002/biof.5520080315     Document Type: Review

References (74)

1. M. Ankarcrona, J.M. Dypbukt, E. Bonfoco, B. Zhivotovsky, S. Orrenius, S.A. Lipton and P. Nicotera, Glutamate-induced neuronal death: a succession of necrosis or apoptosis depending on mitochondrial function, Neuron 15 (1995), 961-973.
2. 2+ network, J. Cell Biol. 136 (1997), 833-844.
3. 2+ by mitochondria, J. Biol. Chem. 255 (1980), 8663-8671.
4. P. Bernardi, Modulation of the mitochondrial cyclosporin A-sensitive permeability transition pore by the proton electrochemical gradient. Evidence that the pore can be opened by membrane depolarization, J. Biol. Chem. 267 (1992), 8834-8839.
5. P. Bernardi, K.M. Broekemeier and D.R. Pfeiffer, Recent progress on regulation of the mitochondrial permeability transition pore; a cyclosporin-sensitive pore in the inner mitochondrial membrane, J. Bioenerg. Biomembr. 26 (1994), 509-517.
6. P. Bernardi and V. Petronilli, The permeability transition pore as a mitochondrial calcium release channel: a critical appraisal, J. Bioenerg. Biomembr. 28 (1996), 131-138.
7. P. Bernardi, S. Vassanelli, P. Veronese, R. Colonna, I. Szabo and M. Zoratti, Modulation of the mitochondrial permeability transition pore. Effect of protons and divalent cations, J. Biol. Chem. 267 (1992), 2934-2939.
8. G. Beutner, A. Ruck, B. Riede, W. Weite and D. Brdiczka, Complexes between kinases, mitochondrial porin and adenylate translocator in rat brain resemble the permeability transition pore, FEBS Lett. 396 (1996), 189-195.
9. 2+ and oxidative stress, FEBS Lett. 304 (1992), 192-194.
10. K.M. Broekemeier, M.E. Dempsey and D.R. Pfeiffer, Cyclosporin A is a potent inhibitor of the inner membrane permeability transition in liver mitochondria, J. Biol. Chem. 264 (1989), 7826-7830.
11. K.M. Broekemeier and D.R. Pfeiffer, Inhibition of the mitochondrial permeability transition by cyclosporin A during long time frame experiments: relationship between pore opening and the activity of mitochondrial phospholipases, Biochemistry 34 (1995), 16440-16449.
12. 2+, Biochemistry 35 (1996), 8483-8488.
13. B.V. Chernyak and P. Bernardi, The mitochondrial permeability transition pore is modulated by oxidative agents through both pyridine nucleotides and glutathione at two separate sites, Eur. J. Biochem. 238 (1996), 623-630.
14. N.A. Clipstone and G.R. Crabtree, Identification of calcineurin as a key signalling enzyme in T-lymphocyte activation, Nature 357 (1992), 695-697.
15. 2+], Biochemistry 35 (1996), 8172-8180.
16. P. Costantini, B.V. Chernyak, V. Petronilli and P. Bernardi, Selective inhibition of the mitochondrial permeability transition pore at the oxidation-reduction sensitive dithiol by monobromobimane, FEBS Lett. 362 (1995), 239-242.
17. P. Costantini, B.V. Chernyak, V. Petronilli and P. Bernardi, Modulation of the mitochondrial permeability transition pore by pyridine nucleotides and dithiol oxidation at two separate sites, J. Biol. Chem. 271 (1996), 6746-6751.
18. P. Costantini, R. Colonna and P. Bernardi, Induction of the mitochondrial permeability transition pore by N-ethyl-maleimide depends on secondary oxidation of critical thiol groups. Potentiation by copper-ortho-phenanthroline without dimerization of the adenine nucleotide translocase, Biochim. Biophys. Acta 1365 (1998), 385-392.
19. 2+-dependent pore in heart mitochondria activated by inorganic phosphate and oxidative stress, Biochem. J. 255 (1988), 357-360.
20. F. Di Lisa and P. Bernardi, Mitochondrial function as a determinant of recovery or death in cell response to injury, Mol. Cell Biochem. 184 (1998), 379-391.
21. M.R. Duchen, O. McGuinness, L.A. Brown and M. Crompton, On the involvement of a cyclosporin A-sensitive mitochondrial pore in myocardial reperfusion injury, Cardiovasc. Res. 27 (1993), 1790-1794.
22. O. Eriksson, E. Fontaine and P. Bernardi, Chemical modification of arginines by 2,3-butanedione and phenylglyoxal causes closure of the mitochondrial permeability transition pore, J. Biol. Chem. 273 (1998), 12 669-12 674.
23. O. Eriksson, E. Fontaine, V. Petronilli and P. Bernardi, Inhibition of the mitochondrial cyclosporin A-sensitive permeability transition pore by the arginine reagent phenylglyoxal, FEBS Lett. 409 (1997), 361-364.
24. 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, J. Biol. Chem. 273 (1998), 12 662-12 668.
25. N. Fournier, G. Ducet and A. Crevat, Action of cyclosporine on mitochondrial calcium fluxes, J. Bioenerg. Biomembr. 19 (1987), 297-303.
26. K.K. Gunter and T.E. Gunter, Transport of calcium by mitochondria, J. Bioenerg. Biomembr. 26 (1994), 471-485.
27. T.E. Gunter and D.R. Pfeiffer, Mechanisms by which mitochondria transport calcium, Am. J. Physiol. 258 (1990), C755-C786.
28. 2+-induced large-amplitude swelling of liver and heart mitochondria by cyclosporin is probably caused by the inhibitor binding to mitochondrial-matrix peptidyl-prolyl-cis-trans-isomerase and preventing it interacting with the adenine nucleotide translocase, Biochem. J. 268 (1990), 153-160.
29. 2+ trigger site, Arch. Biochem. Biophys. 195 (1979), 460-467.
30. J.B. Hoek, J.L. Farber, A.P. Thomas and X. Wang, Calcium ion-dependent signalling and mitochondrial dysfunction: mitochondrial calcium uptake during hormonal stimulation in intact liver cells and its implication for the mitochondrial permeability transition, Biochim. Biophys. Acta 1271 (1995), 93-102.
31. 2+-induced membrane transition in mitochondria. I. The protective mechanisms, Arch. Biochem. Biophys. 195 (1979), 453-459.
32. 2+ release, Arch. Biochem. Biophys. 195 (1979), 468-477.
33. F. Ichas, L.S. Jouaville and J.P. Mazat, Mitochondria are excitable organelles capable of generating and conveying electrical and calcium signals, Cell 89 (1997), 1145-1153.
34. F. Ichas, L.S. Jouaville, S.S. Sidash, J.P. Mazat and E.L. Holmuhamedov, Mitochondrial calcium spiking: a transduction mechanism based on calcium-induced permeability transition involved in cell calcium signalling, FEBS Lett. 348 (1994), 211-215.
35. F. Ichas and J.P. Mazat, From calcium signalling to cell death: two conformations for the mitochondrial permeability transition pore, Biochim. Biophys. Acta (1998) (in press).
36. 2+ binding site on the cytoplasmic side of the inner membrane, J. Biol. Chem. 263 (1988), 1405-1412.
37. 2+-requiring, cyclosporin-sensitive pathway, Biochem. Biophys. Res. Commun. 161 (1989), 619-625.
38. R. Imberti, A.L. Nieminen, B. Herman and J.J. Lemasters, Mitochondrial and glycolytic dysfunction in lethal injury to hepatocytes by t-butylhydroperoxide: protection by fructose, cyclosporin A and trifluoperazine, J. Pharmacol. Exp. Ther. 265 (1993), 392-400.
39. K.W. Kinnally, M.L. Campo and H. Tedeschi, Mitochondrial channel activity studied by patch-clamping mitoplasts, J. Bioenerg. Biomembr. 21 (1989), 497-506.
40. G. Kroemer, N. Zamzami and S.A. Susin, Mitochondrial control of apoptosis, Immunol. Today 18 (1997), 44-51.
41. R.G. Lapidus and P.M. Sokolove, Inhibition by spermine of the inner membrane permeability transition of isolated rat heart mitochondria, FEBS Lett. 313 (1992), 314-318.
42. R.G. Lapidus and P.M. Sokolove, Spermine inhibition of the permeability transition of isolated rat liver mitochondria: an investigation of mechanism, Arch. Biochem. Biophys. 306 (1993), 246-253.
43. M. Mancini, D.W. Nicholson, S. Roy, N.A. Thornberry, E.P. Peterson, R.L. Casciola and A. Rosen, The caspase-3 precursor has a cytosolic and mitochondrial distribution: implications for apoptotic signaling, J. Cell Biol. 140 (1998), 1485-1495.
44. S. Massari and G.F. Azzone, The equivalent pore radius of intact and damaged mitochondria and the mechanism of active shrinkage, Biochim. Biophys. Acta 283 (1972), 23-29.
45. A. Nicolli, E. Basso, V. Petronilli, R.M. Wenger and P. Bernardi, Interactions of cyclophilin with the mitochondrial inner membrane and regulation of the permeability transition pore, a cyclosporin A-sensitive channel, J. Biol. Chem. 271 (1996), 2185-2192.
46. A. Nicolli, V. Petronilli and P. Bernardi, Modulation of the mitochondrial cyclosporin A-sensitive permeability transition pore by matrix pH. Evidence that the pore open-closed probability is regulated by reversible histidine protonation, Biochemistry 32 (1993), 4461-4465.
47. J.G. Pastorino, J.W. Snyder, A. Serroni, J.B. Hoek and J.L. Farber, Cyclosporin and carnitine prevent the anoxic death of cultured hepatocytes by inhibiting the mitochondrial permeability transition, J. Biol. Chem. 268 (1993), 13 791-13 798.
48. 2+, J. Biol. Chem. 268 (1993), 1011-1016.
49. V. Petronilli, C. Cola, S. Massari, R. Colonna and P. Bernardi, Physiological effectors modify voltage sensing by the cyclosporin A-sensitive permeability transition pore of mitochondria, J. Biol. Chem. 268 (1993), 21 939-21 945.
50. V. Petronilli, P. Costantini, L. Scorrano, R. Colonna, S. Passamonti and P. Bernardi, The voltage sensor of the mitochondrial permeability transition pore is tuned by the oxidation-reduction state of vicinal thiols. Increase of the gating potential by oxidants and its reversal by reducing agents, J. Biol. Chem. 269 (1994), 16 638-16 642.
51. V. Petronilli, A. Nicolli, P. Costantini, R. Colonna and P. Bernardi, Regulation of the permeability transition pore, a voltage-dependent mitochondrial channel inhibited by cyclosporin A, Biochim. Biophys. Acta 1187 (1994), 255-259.
52. V. Petronilli, I. Szabo and M. Zoratti, The inner mitochondrial membrane contains ion-conducting channels similar to those found in bacteria, FEBS Lett. 259 (1989), 137-143.
53. 2+ plus N-ethylmaleimide on mitochondrial function, J. Biol. Chem. 254 (1979), 11 485-11 494.
54. M.P. Rigobello, E. Barzon, O. Marin and A. Bindoli, Effect of polycation peptides on mitochondrial permeability transition, Biochem. Biophys. Res. Commun. 217 (1995), 144-149.
55. 2+ homeostasis in intact cells, J. Cell Biol. 126 (1994), 1183-1194.
56. B. Scherer and M. Klingenberg, Demonstration of the relationship between the adenine nucleotide carrier and the structural changes of mitochondria as induced by adenosine-5′-diphosphate, Biochemistry 13 (1974), 161-170.
57. A.F. Schinder, E.C. Olson, N.C. Spitzer and M. Montal, Mitochondrial dysfunction is a primary event in glutamate neurotoxicity, J. Neurosci. 16 (1996), 6125-6133.
58. H.P. Schultheiss and M. Klingenberg, Immunochemical characterization of the adenine nucleotide translocator. Organ specificity and conformation specificity, Eur. J. Biochem. 143 (1984), 599-605.
59. L. Scorrano, A. Nicolli, E. Basso, V. Petronilli and P. Bernardi, Two modes of activation of the permeability transition pore: the role of mitochondrial cyclophilin, Mol. Cell Biochem. 174 (1997), 181-184.
60. L. Scorrano, V. Petronilli and P. Bernardi, On the voltage dependence of the mitochondrial permeability transition pore. A critical appraisal, J. Biol. Chem. 272 (1997), 12295-12299.
61. G.C. Sparagna, K.K. Gunter, S.S. Sheu and T.E. Gunter, Mitochondrial calcium uptake from physiological-type pulses of calcium. A description of the rapid uptake mode, J. Biol. Chem. 270 (1995), 27 510-27 515.
62. S.A. Susin, N. Zamzami, M. Castedo, T. Hirsch, P. Marchetti, A. Macho, E. Daugas, M. Geuskens and G. Kroemer, Bcl-2 inhibits the mitochondrial release of an apoptogenic protease, J. Exp. Med. 184 (1996), 1331-1341.
63. I. Szabo, P. Bernardi and M. Zoratti, Modulation of the mitochondrial megachannel by divalent cations and protons, J. Biol. Chem. 267 (1992), 2940-2946.
64. I. Szabo and M. Zoratti, The giant channel of the inner mitochondrial membrane is inhibited by cyclosporin A, J. Biol. Chem. 266 (1991), 3376-3379.
65. I. Szabo and M. Zoratti, The mitochondrial megachannel is the permeability transition pore, J. Bioenerg. Biomembr. 24 (1992), 111-117.
66. I. Szabo and M. Zoratti, The mitochondrial permeability transition pore may comprise VDAC molecules. I. Binary structure and voltage dependence of the pore, FEBS Lett. 330 (1993), 201-205.
67. 2+ release and pore formation by prooxidants, Biochem. Pharmacol. 47 (1994), 2147-2156.
68. K.Y. Woodfield, N.T. Price and A.P. Halestrap, cDNA cloning of rat mitochondrial cyclophilin, Biochim. Biophys. Acta 1351 (1997), 27-30.
69. N. Zamzami, P. Marchetti, M. Castedo, D. Decaudin, A. Macho, T. Hirsch, S.A. Susin, P.X. Petit, B. Mignotte and G. Kroemer, Sequential reduction of mitochondrial transmembrane potential and generation of reactive oxygen species in early programmed cell death, J. Exp. Med. 182 (1995), 367-377.
70. N. Zamzami, P. Marchetti, M. Castedo, T. Hirsch, S.A. Susin, B. Masse and G. Kroemer, Inhibitors of permeability transition interfere with the disruption of the mitochondrial transmembrane potential during apoptosis, FEBS Lett. 384 (1996), 53-57.
71. N. Zamzami, P. Marchetti, M. Castedo, C. Zanin, J.L. Vayssiere, P.X. Petit and G. Kroemer, Reduction in mitochondrial potential constitutes an early irreversible step of programmed lymphocyte death in vivo, J. Exp. Med. 181 (1995), 1661-1672.
72. M. Zoratti and I. Szabo, The mitochondrial permeability transition, Biochim. Biophys. Acta 1241 (1995), 139-176.
73. H. Zou, W.J. Henzel, X. Liu, A. Lutschg and X. Wang, Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3, Cell 90 (1997), 405-413.
74. V. Petronilli, G. Miotto, M. Canton, R. Colonna, P. Bernardi and F. Di Lisa, Imaging the mitochondrial permeability transition pore in intact cells, BioFactors 8 (1998), 263-272.