메뉴 건너뛰기




Volumn 224, Issue , 2003, Pages 29-55

Apoptosis and necrosis in health and disease: Role of mitochondria

Author keywords

Apoptosis; Cell death; Confocal microscopy; Membrane permeabilization; Membrane potential; Mitochondria; Necrosis

Indexed keywords

ADENOSINE TRIPHOSPHATE; CALCIUM; OXIDIZING AGENT;

EID: 0038076276     PISSN: 00747696     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0074-7696(05)24002-0     Document Type: Article
Times cited : (116)

References (117)
  • 4
    • 0034650523 scopus 로고    scopus 로고
    • Bax oligomerization is required for channel-forming activity in liposomes and to trigger cytochrome c release from mitochondria
    • Antonsson, B., Montessuit, S., Lauper, S., Eskes, R., and Martinou, J. C. (2000). Bax oligomerization is required for channel-forming activity in liposomes and to trigger cytochrome c release from mitochondria. Biochem. J. 345(Pt. 2), 271-278.
    • (2000) Biochem. J. , vol.345 , Issue.PART 2 , pp. 271-278
    • Antonsson, B.1    Montessuit, S.2    Lauper, S.3    Eskes, R.4    Martinou, J.C.5
  • 6
    • 0024237766 scopus 로고
    • Functional significance of mitochondrial bound hexokinase in tumor cell metabolism. Evidence for preferential phosphorylation of glucose by intramitochondrially generated ATP
    • Arora, K. K., and Pedersen, P. L. (1988). Functional significance of mitochondrial bound hexokinase in tumor cell metabolism. Evidence for preferential phosphorylation of glucose by intramitochondrially generated ATP. J. Biol. Chem. 263, 17422-17428.
    • (1988) J. Biol. Chem. , vol.263 , pp. 17422-17428
    • Arora, K.K.1    Pedersen, P.L.2
  • 8
    • 0028053663 scopus 로고
    • Recent progress on regulation of the mitochondrial permeability transition pore; a cyclosporin-sensitive pore in the inner mitochondrial membrane
    • Bernardi, P., Broekemeier, K. M., and Pfeiffer, D. R. (1994). Recent progress on regulation of the mitochondrial permeability transition pore; a cyclosporin-sensitive pore in the inner mitochondrial membrane. J. Bioenerg. Biomembr. 26, 509-517.
    • (1994) J. Bioenerg. Biomembr. , vol.26 , pp. 509-517
    • Bernardi, P.1    Broekemeier, K.M.2    Pfeiffer, D.R.3
  • 9
    • 0033568486 scopus 로고    scopus 로고
    • Mitochondria and cell death. Mechanistic aspects and methodological issues
    • Bernardi, P., Scorrano, L., Colonna, R., Petronilli, V., and Di Lisa, F. (1999). Mitochondria and cell death. Mechanistic aspects and methodological issues. Eur. J. Biochem. 264, 687-701.
    • (1999) Eur. J. Biochem. , vol.264 , pp. 687-701
    • Bernardi, P.1    Scorrano, L.2    Colonna, R.3    Petronilli, V.4    Di Lisa, F.5
  • 10
    • 0030569305 scopus 로고    scopus 로고
    • Complexes between kinases, mitochondrial porin and adenylate translocator in rat brain resemble the permeability transition pore
    • Beutner, G., Ruck, A., Riede, B., Welte, W., and Brdiczka, D. (1996). Complexes between kinases, mitochondrial porin and adenylate translocator in rat brain resemble the permeability transition pore. FEBS Lett. 396, 189-195.
    • (1996) FEBS Lett. , vol.396 , pp. 189-195
    • Beutner, G.1    Ruck, A.2    Riede, B.3    Welte, W.4    Brdiczka, D.5
  • 11
    • 0031772126 scopus 로고    scopus 로고
    • The mitochondrial permeability transition is required for tumor necrosis factor alpha-mediated apoptosis and cytochrome c release
    • Bradham, C. A., Qian, T., Streetz, K., Trautwein, C., Brenner, D. A., and Lemasters, J. J. (1998). The mitochondrial permeability transition is required for tumor necrosis factor alpha-mediated apoptosis and cytochrome c release. Mol. Cell Biol. 18, 6353-6364.
    • (1998) Mol. Cell Biol. , vol.18 , pp. 6353-6364
    • Bradham, C.A.1    Qian, T.2    Streetz, K.3    Trautwein, C.4    Brenner, D.A.5    Lemasters, J.J.6
  • 13
    • 0032899637 scopus 로고    scopus 로고
    • 2+ to the mitochondrial permeability transition induced by tert-butylhydroperoxide in rat hepatocytes
    • 2+ to the mitochondrial permeability transition induced by tert-butylhydroperoxide in rat hepatocytes. Hepatology 29, 1523-1531.
    • (1999) Hepatology , vol.29 , pp. 1523-1531
    • Byrne, A.M.1    Lemasters, J.J.2    Nieminen, A.L.3
  • 14
    • 0026584655 scopus 로고
    • 2+ increase by doxorubicin in cardiac myocytes
    • 2+ increase by doxorubicin in cardiac myocytes. Biochem. J. 281(Pt. 3), 871-878.
    • (1992) Biochem. J. , vol.281 , Issue.PART 3 , pp. 871-878
    • Chacon, E.1    Ulrich, R.2    Acosta, D.3
  • 15
    • 0018776894 scopus 로고
    • Hydroperoxide metabolism in mammalian organs
    • Chance, B., Sies, H., and Boveris, A. (1979). Hydroperoxide metabolism in mammalian organs. Physiol. Rev. 59, 527-605.
    • (1979) Physiol. Rev. , vol.59 , pp. 527-605
    • Chance, B.1    Sies, H.2    Boveris, A.3
  • 16
    • 0030038762 scopus 로고    scopus 로고
    • The mitochondrial permeability transition pore is modulated by oxidative agents through both pyridine nucleotides and glutathione at two separate sites
    • Chernyak, B. V., and Bernardi, P. (1996). The mitochondrial permeability transition pore is modulated by oxidative agents through both pyridine nucleotides and glutathione at two separate sites. Eur. J. Biochem. 238, 623-630.
    • (1996) Eur. J. Biochem. , vol.238 , pp. 623-630
    • Chernyak, B.V.1    Bernardi, P.2
  • 17
    • 0037007227 scopus 로고    scopus 로고
    • Mitochondria are morphologically and functionally heterogeneous within cells
    • Collins, T. J., Berridge, M. J., Lipp, P., and Bootman, M. D. (2002). Mitochondria are morphologically and functionally heterogeneous within cells. EMBO J. 21, 1616-1627.
    • (2002) EMBO J. , vol.21 , pp. 1616-1627
    • Collins, T.J.1    Berridge, M.J.2    Lipp, P.3    Bootman, M.D.4
  • 18
    • 0029863399 scopus 로고    scopus 로고
    • Modulation of the mitochondrial permeability transition pore by pyridine nucleotides and dithiol oxidation at two separate sites
    • Costantini, P., Chernyak, B. V., Petronilli, V., and Bernardi, P. (1996). Modulation of the mitochondrial permeability transition pore by pyridine nucleotides and dithiol oxidation at two separate sites. J. Biol. Chem. 271, 6746-6751.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6746-6751
    • Costantini, P.1    Chernyak, B.V.2    Petronilli, V.3    Bernardi, P.4
  • 19
    • 0034642510 scopus 로고    scopus 로고
    • Oxidation of a critical thiol residue of the adenine nucleotide translocator enforces Bcl-2-independent permeability transition pore opening and apoptosis
    • Costantini, P., Belzacq, A. S., Vieira, H. L., Larochette, N., de Pablo, M. A., Zamzami, N., Susin, S. A., Brenner, C., and Kroemer, G. (2000). Oxidation of a critical thiol residue of the adenine nucleotide translocator enforces Bcl-2-independent permeability transition pore opening and apoptosis. Oncogene 19, 307-314.
    • (2000) Oncogene , vol.19 , pp. 307-314
    • Costantini, P.1    Belzacq, A.S.2    Vieira, H.L.3    Larochette, N.4    De Pablo, M.A.5    Zamzami, N.6    Susin, S.A.7    Brenner, C.8    Kroemer, G.9
  • 20
    • 0017716659 scopus 로고
    • The calcium-induced and sodium-induced effluxes of calcium from heart mitochondria. Evidence for a sodium-calcium carrier
    • Crompton, M., Kunzi, M., and Carafoli, E. (1977). The calcium-induced and sodium-induced effluxes of calcium from heart mitochondria. Evidence for a sodium-calcium carrier. Eur. J. Biochem. 79, 549-558.
    • (1977) Eur. J. Biochem. , vol.79 , pp. 549-558
    • Crompton, M.1    Kunzi, M.2    Carafoli, E.3
  • 21
    • 0017919178 scopus 로고
    • The interrelations between the transport of sodium and calcium in mitochondria of various mammalian tissues
    • Crompton, M., Moser, R., Ludi, H., and Carafoli, E. (1978). The interrelations between the transport of sodium and calcium in mitochondria of various mammalian tissues. Eur. J. Biochem. 82, 25-31.
    • (1978) Eur. J. Biochem. , vol.82 , pp. 25-31
    • Crompton, M.1    Moser, R.2    Ludi, H.3    Carafoli, E.4
  • 22
    • 0023821864 scopus 로고
    • 2+-dependent pore in heart mitochondria activated by inorganic phosphate and oxidative stress
    • 2+-dependent pore in heart mitochondria activated by inorganic phosphate and oxidative stress. Biochem. J. 255, 357-360.
    • (1988) Biochem. J. , vol.255 , pp. 357-360
    • Crompton, M.1    Ellinger, H.2    Costi, A.3
  • 23
    • 0027418625 scopus 로고
    • Mitochondria as a source of reactive oxygen species during reductive stress in rat hepatocytes
    • Dawson, T. L., Gores, G. J., Nieminen, A. L., Herman, B., and Lemasters, J. J. (1993). Mitochondria as a source of reactive oxygen species during reductive stress in rat hepatocytes. Am. J. Physiol. 264, C961-C967.
    • (1993) Am. J. Physiol. , vol.264
    • Dawson, T.L.1    Gores, G.J.2    Nieminen, A.L.3    Herman, B.4    Lemasters, J.J.5
  • 26
    • 0034616945 scopus 로고    scopus 로고
    • Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition
    • Du, C., Fang, M., Li, Y., Li, L., and Wang, X. (2000). Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition. Cell 102, 33-42.
    • (2000) Cell , vol.102 , pp. 33-42
    • Du, C.1    Fang, M.2    Li, Y.3    Li, L.4    Wang, X.5
  • 27
    • 0028882764 scopus 로고
    • Mitochondrial production of reactive oxygen species in cortical neurons following exposure to N-methyl-D-aspartate
    • Dugan, L. L., Sensi, S. L., Canzoniero, L. M., Handran, S. D., Rothman, S. M., Lin, T. S., Goldberg, M. P., and Choi, D. W. (1995). Mitochondrial production of reactive oxygen species in cortical neurons following exposure to N-methyl-D-aspartate. J. Neurosci. 15, 6377-6388.
    • (1995) J. Neurosci. , vol.15 , pp. 6377-6388
    • Dugan, L.L.1    Sensi, S.L.2    Canzoniero, L.M.3    Handran, S.D.4    Rothman, S.M.5    Lin, T.S.6    Goldberg, M.P.7    Choi, D.W.8
  • 28
    • 0034254734 scopus 로고    scopus 로고
    • Caspase-independent commitment phase to apoptosis in activated blood T lymphocytes: Reversibility at low apoptotic insult
    • Dumont, C., Durrbach, A., Bidere, N., Rouleau, M., Kroemer, G., Bernard, G., Hirsch, F., Charpentier, B., Susin, S. A., and Senik, A. (2000). Caspase-independent commitment phase to apoptosis in activated blood T lymphocytes: Reversibility at low apoptotic insult. Blood 96, 1030-1038.
    • (2000) Blood , vol.96 , pp. 1030-1038
    • Dumont, C.1    Durrbach, A.2    Bidere, N.3    Rouleau, M.4    Kroemer, G.5    Bernard, G.6    Hirsch, F.7    Charpentier, B.8    Susin, S.A.9    Senik, A.10
  • 29
    • 0032885388 scopus 로고    scopus 로고
    • Mammalian caspases: Structure, activation, substrates, and functions during apoptosis
    • Earnshaw, W. C., Martins, L. M., and Kaufmann, S. H. (1999). Mammalian caspases: Structure, activation, substrates, and functions during apoptosis. Annu. Rev. Biochem. 68, 383-424.
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 383-424
    • Earnshaw, W.C.1    Martins, L.M.2    Kaufmann, S.H.3
  • 30
    • 0023928504 scopus 로고
    • Membrane potential can be determined in individual cells from the nernstian distribution of cationic dyes
    • Ehrenberg, B., Montana, V., Wei, M. D., Wuskell, J. P., and Loew, L. M. (1988). Membrane potential can be determined in individual cells from the nernstian distribution of cationic dyes. Biophys. J. 53, 785-794.
    • (1988) Biophys. J. , vol.53 , pp. 785-794
    • Ehrenberg, B.1    Montana, V.2    Wei, M.D.3    Wuskell, J.P.4    Loew, L.M.5
  • 32
    • 0035900312 scopus 로고    scopus 로고
    • Structural biology. Controlling the caspases
    • Fesik, S. W., and Shi, Y. (2001). Structural biology. Controlling the caspases. Science 294, 1477-1478.
    • (2001) Science , vol.294 , pp. 1477-1478
    • Fesik, S.W.1    Shi, Y.2
  • 34
    • 0023504596 scopus 로고
    • Purification and characterization of the voltage-dependent anion channel from the outer mitochondrial membrane of yeast
    • Forte, M., Adelsberger-Mangan, D., and Colombini, M. (1987). Purification and characterization of the voltage-dependent anion channel from the outer mitochondrial membrane of yeast. J. Membr. Biol. 99, 65-72.
    • (1987) J. Membr. Biol. , vol.99 , pp. 65-72
    • Forte, M.1    Adelsberger-Mangan, D.2    Colombini, M.3
  • 35
    • 0023263612 scopus 로고
    • Action of cyclosporine on mitochondrial calcium fluxes
    • Fournier, N., Ducet, G., and Crevat, A. (1987). Action of cyclosporine on mitochondrial calcium fluxes. J. Bioenerg. Biomembr. 19, 297-303.
    • (1987) J. Bioenerg. Biomembr. , vol.19 , pp. 297-303
    • Fournier, N.1    Ducet, G.2    Crevat, A.3
  • 36
    • 0028931989 scopus 로고
    • Hydroxyl radical generation during mitochondrial electron transfer and the formation of 8-hydroxydesoxyguanosine in mitochondrial DNA
    • Giulivi, C., Boveris, A., and Cadenas, E. (1995). Hydroxyl radical generation during mitochondrial electron transfer and the formation of 8-hydroxydesoxyguanosine in mitochondrial DNA. Arch. Biochem. Biophys. 316, 909-916.
    • (1995) Arch. Biochem. Biophys. , vol.316 , pp. 909-916
    • Giulivi, C.1    Boveris, A.2    Cadenas, E.3
  • 39
    • 0032528118 scopus 로고    scopus 로고
    • Enforced dimerization of BAX results in its translocation, mitochondrial dysfunction and apoptosis
    • Gross, A., Jockel, J., Wei, M. C., and Korsmeyer, S. J. (1998). Enforced dimerization of BAX results in its translocation, mitochondrial dysfunction and apoptosis. EMBO J. 17, 3878-3885.
    • (1998) EMBO J. , vol.17 , pp. 3878-3885
    • Gross, A.1    Jockel, J.2    Wei, M.C.3    Korsmeyer, S.J.4
  • 40
    • 0027945340 scopus 로고
    • Transport of calcium by mitochondria
    • Gunter, K. K., and Gunter, T. E. (1994). Transport of calcium by mitochondria. J. Bioenerg. Biomembr. 26, 471-485.
    • (1994) J. Bioenerg. Biomembr. , vol.26 , pp. 471-485
    • Gunter, K.K.1    Gunter, T.E.2
  • 41
    • 0035951886 scopus 로고    scopus 로고
    • Bcl-G, a novel pro-apoptotic member of the Bcl-2 family
    • Guo, B., Godzik, A., and Reed, J. C. (2001). Bcl-G, a novel pro-apoptotic member of the Bcl-2 family. J. Biol. Chem. 276, 2780-2785.
    • (2001) J. Biol. Chem. , vol.276 , pp. 2780-2785
    • Guo, B.1    Godzik, A.2    Reed, J.C.3
  • 42
    • 0014286720 scopus 로고
    • Ultrastructural bases for metabolically linked mechanical activity in mitochondria. II. Electron transport-linked ultrastructural transformations in mitochondria
    • Hackenbrock, C. R. (1968). Ultrastructural bases for metabolically linked mechanical activity in mitochondria. II. Electron transport-linked ultrastructural transformations in mitochondria. J. Cell Biol. 37, 345-369.
    • (1968) J. Cell Biol. , vol.37 , pp. 345-369
    • Hackenbrock, C.R.1
  • 43
    • 0025193488 scopus 로고
    • Inhibition of Ca2(+)-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
    • Halestrap, A. P., and Davidson, A. M. (1990). Inhibition of Ca2(+)-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, 153-160.
    • (1990) Biochem. J. , vol.268 , pp. 153-160
    • Halestrap, A.P.1    Davidson, A.M.2
  • 44
    • 0031013623 scopus 로고    scopus 로고
    • Oxidative stress, thiol reagents, and membrane potential modulate the mitochondrial permeability transition by affecting nucleotide binding to the adenine nucleotide translocase
    • Halestrap, A. P., Woodfield, K. Y., and Connern, C. P. (1997). Oxidative stress, thiol reagents, and membrane potential modulate the mitochondrial permeability transition by affecting nucleotide binding to the adenine nucleotide translocase. J. Biol. Chem. 272, 3346-3354.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3346-3354
    • Halestrap, A.P.1    Woodfield, K.Y.2    Connern, C.P.3
  • 45
    • 0027960215 scopus 로고
    • Superoxide and peroxynitrite inactivate aconitases, but nitric oxide does not
    • Hausladen, A., and Fridovich, I. (1994). Superoxide and peroxynitrite inactivate aconitases, but nitric oxide does not. J. Biol. Chem. 269, 29405-29408.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29405-29408
    • Hausladen, A.1    Fridovich, I.2
  • 47
    • 0037070178 scopus 로고    scopus 로고
    • Regulated and unregulated mitochondrial permeability transition pores: A new paradigm of pore structure and function?
    • He, L., and Lemasters, J. J. (2002). Regulated and unregulated mitochondrial permeability transition pores: A new paradigm of pore structure and function? FEBS Lett. 512, 1-7.
    • (2002) FEBS Lett. , vol.512 , pp. 1-7
    • He, L.1    Lemasters, J.J.2
  • 49
    • 0033605376 scopus 로고    scopus 로고
    • Mitochondrial depolarization accompanies cytochrome c release during apoptosis in PC6 cells
    • Heiskanen, K. M., Bhat, M. B., Wang, H. W., Ma, J., and Nieminen, A. L. (1999). Mitochondrial depolarization accompanies cytochrome c release during apoptosis in PC6 cells. J. Biol. Chem. 274, 5654-5658.
    • (1999) J. Biol. Chem. , vol.274 , pp. 5654-5658
    • Heiskanen, K.M.1    Bhat, M.B.2    Wang, H.W.3    Ma, J.4    Nieminen, A.L.5
  • 51
    • 0023959131 scopus 로고
    • Irreversible injury in anoxic hepatocytes precipitated by an abrupt increase in plasma membrane permeability
    • Herman, B., Nieminen, A. L., Gores, G. J., and Lemasters, J. J. (1988). Irreversible injury in anoxic hepatocytes precipitated by an abrupt increase in plasma membrane permeability. FASEB J. 2, 146-151.
    • (1988) FASEB J. , vol.2 , pp. 146-151
    • Herman, B.1    Nieminen, A.L.2    Gores, G.J.3    Lemasters, J.J.4
  • 52
    • 0018332596 scopus 로고
    • 2+-induced membrane transition in mitochondria. I. The protective mechanisms
    • 2+-induced membrane transition in mitochondria. I. The protective mechanisms. Arch. Biochem. Biophys. 195, 453-459.
    • (1979) Arch. Biochem. Biophys. , vol.195 , pp. 453-459
    • Hunter, D.R.1    Haworth, R.A.2
  • 53
    • 0017089948 scopus 로고
    • Relationship between configuration, function, and permeability in calcium-treated mitochondria
    • Hunter, D. R., Haworth, R. A., and Southard, J. H. (1976). Relationship between configuration, function, and permeability in calcium-treated mitochondria. J. Biol. Chem. 251, 5069-5077.
    • (1976) J. Biol. Chem. , vol.251 , pp. 5069-5077
    • Hunter, D.R.1    Haworth, R.A.2    Southard, J.H.3
  • 54
    • 0027427670 scopus 로고
    • Mitochondrial and glycolytic dysfunction in lethal injury to hepatocytes by t-butylhydroperoxide: Protection by fructose, cyclosporin A and trifluoperazine
    • Imberti, R., Nieminen, A. L., Herman, B., and Lemasters, J. J. (1993). Mitochondrial and glycolytic dysfunction in lethal injury to hepatocytes by t-butylhydroperoxide: Protection by fructose, cyclosporin A and trifluoperazine. J. Pharmacol. Exp. Ther. 265, 392-400.
    • (1993) J. Pharmacol. Exp. Ther. , vol.265 , pp. 392-400
    • Imberti, R.1    Nieminen, A.L.2    Herman, B.3    Lemasters, J.J.4
  • 56
    • 0028963344 scopus 로고
    • The sodium-calcium antiport of heart mitochondria is not electroneutral
    • Jung, D. W., Baysal, K., and Brierley, G. P. (1995). The sodium-calcium antiport of heart mitochondria is not electroneutral. J. Biol. Chem. 270, 672-678.
    • (1995) J. Biol. Chem. , vol.270 , pp. 672-678
    • Jung, D.W.1    Baysal, K.2    Brierley, G.P.3
  • 58
    • 0035918260 scopus 로고    scopus 로고
    • Bcl-B, a novel Bcl-2 family member that differentially binds and regulates Bax and Bak
    • Ke, N., Godzik, A., and Reed, J. C. (2001). Bcl-B, a novel Bcl-2 family member that differentially binds and regulates Bax and Bak. J. Biol. Chem. 276, 12481-12484.
    • (2001) J. Biol. Chem. , vol.276 , pp. 12481-12484
    • Ke, N.1    Godzik, A.2    Reed, J.C.3
  • 59
    • 0024433994 scopus 로고
    • Mitochondrial channel activity studied by patch-clamping mitoplasts
    • Kinnally, K. W., Campo, M. L., and Tedeschi, H. (1989). Mitochondrial channel activity studied by patch-clamping mitoplasts. J. Bioenerg. Biomembr. 21, 497-506.
    • (1989) J. Bioenerg. Biomembr. , vol.21 , pp. 497-506
    • Kinnally, K.W.1    Campo, M.L.2    Tedeschi, H.3
  • 60
    • 0031037897 scopus 로고    scopus 로고
    • The release of cytochrome c from mitochondria: A primary site for Bcl-2 regulation of apoptosis
    • Kluck, R. M., Bossy-Wetzel, E., Green, D. R., and Newmeyer, D. D. (1997). The release of cytochrome c from mitochondria: A primary site for Bcl-2 regulation of apoptosis. Science 275, 1132-1136.
    • (1997) Science , vol.275 , pp. 1132-1136
    • Kluck, R.M.1    Bossy-Wetzel, E.2    Green, D.R.3    Newmeyer, D.D.4
  • 61
    • 0035956929 scopus 로고    scopus 로고
    • Increased mitochondrial oxidative stress in the Sod2 (+/-) mouse results in the age-related decline of mitochondrial function culminating in increased apoptosis
    • Kokoszka, J. E., Coskun, P., Esposito, L. A., and Wallace, D. C. (2001). Increased mitochondrial oxidative stress in the Sod2 (+/-) mouse results in the age-related decline of mitochondrial function culminating in increased apoptosis. Proc. Natl. Acad. Sci. USA 98, 2278-2283.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 2278-2283
    • Kokoszka, J.E.1    Coskun, P.2    Esposito, L.A.3    Wallace, D.C.4
  • 63
    • 0035861589 scopus 로고    scopus 로고
    • Photodynamic therapy-induced apoptosis in epidermoid carcinoma cells. Reactive oxygen species and mitochondrial inner membrane permeabilization
    • Lam, M., Oleinick, N. L., and Nieminen, A. L. (2001). Photodynamic therapy-induced apoptosis in epidermoid carcinoma cells. Reactive oxygen species and mitochondrial inner membrane permeabilization. J. Biol. Chem. 276, 47379-47386.
    • (2001) J. Biol. Chem. , vol.276 , pp. 47379-47386
    • Lam, M.1    Oleinick, N.L.2    Nieminen, A.L.3
  • 64
    • 0032608336 scopus 로고    scopus 로고
    • V. Necrapoptosis and the mitochondrial permeability transition: Shared pathways to necrosis and apoptosis
    • Lemasters, J. J. (1999). V. Necrapoptosis and the mitochondrial permeability transition: Shared pathways to necrosis and apoptosis. Am. J. Physiol. 276, G1-G6.
    • (1999) Am. J. Physiol. , vol.276
    • Lemasters, J.J.1
  • 67
    • 0035811496 scopus 로고    scopus 로고
    • Endonuclease G is an apoptotic DNase when released from mitochondria
    • Li, L. Y., Luo, X., and Wang, X. (2001). Endonuclease G is an apoptotic DNase when released from mitochondria. Nature 412, 95-99.
    • (2001) Nature , vol.412 , pp. 95-99
    • Li, L.Y.1    Luo, X.2    Wang, X.3
  • 68
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • Li, P., Nijhawan, D., Budihardjo, I., Srinivasula, S. M., Ahmad, M., Alnemri, E. S., and Wang, X. (1997). Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 91, 479-489.
    • (1997) Cell , vol.91 , pp. 479-489
    • Li, P.1    Nijhawan, D.2    Budihardjo, I.3    Srinivasula, S.M.4    Ahmad, M.5    Alnemri, E.S.6    Wang, X.7
  • 69
    • 0029981386 scopus 로고    scopus 로고
    • Activity of the mitochondrial multiple conductance channel is independent of the adenine nucleotide translocator
    • Lohret, T. A., Murphy, R. C., Drgon, T., and Kinnally, K. W. (1996). Activity of the mitochondrial multiple conductance channel is independent of the adenine nucleotide translocator. J. Biol. Chem. 271, 4846-4849.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4846-4849
    • Lohret, T.A.1    Murphy, R.C.2    Drgon, T.3    Kinnally, K.W.4
  • 74
    • 0022595453 scopus 로고
    • Hexokinase receptor complex in hepatoma mitochondria: Evidence from N,N′-dicyclohexylcarbodiimide-labeling studies for the involvement of the pore-forming protein VDAC
    • Nakashima, R. A., Mangan, P. S., Colombini, M., and Pedersen, P. L. (1986). Hexokinase receptor complex in hepatoma mitochondria: Evidence from N,N′-dicyclohexylcarbodiimide-labeling studies for the involvement of the pore-forming protein VDAC. Biochemistry 25, 1015-1021.
    • (1986) Biochemistry , vol.25 , pp. 1015-1021
    • Nakashima, R.A.1    Mangan, P.S.2    Colombini, M.3    Pedersen, P.L.4
  • 76
    • 0025267709 scopus 로고
    • Protection by acidotic pH and fructose against lethal injury to rat hepatocytes from mitochondrial inhibitors, ionophores and oxidant chemicals
    • Nieminen, A. L., Dawson, T. L., Gores, G. J., Kawanishi, T., Herman, B., and Lemasters, J. J. (1990). Protection by acidotic pH and fructose against lethal injury to rat hepatocytes from mitochondrial inhibitors, ionophores and oxidant chemicals. Biochem. Biophys. Res. Commun. 167, 600-606.
    • (1990) Biochem. Biophys. Res. Commun. , vol.167 , pp. 600-606
    • Nieminen, A.L.1    Dawson, T.L.2    Gores, G.J.3    Kawanishi, T.4    Herman, B.5    Lemasters, J.J.6
  • 78
    • 0028001390 scopus 로고
    • ATP depletion rather than mitochondrial depolarization mediates hepatocyte killing after metabolic inhibition
    • Nieminen, A. L., Saylor, A. K., Herman, B., and Lemasters, J. J. (1994). ATP depletion rather than mitochondrial depolarization mediates hepatocyte killing after metabolic inhibition. Am. J. Physiol. 267, C67-C74.
    • (1994) Am. J. Physiol. , vol.267
    • Nieminen, A.L.1    Saylor, A.K.2    Herman, B.3    Lemasters, J.J.4
  • 79
    • 0028923778 scopus 로고
    • Contribution of the mitochondrial permeability transition to lethal injury after exposure of hepatocytes to t-butylhydroperoxide
    • Nieminen, A. L., Saylor, A. K., Tesfai, S. A., Herman, B., and Lemasters, J. J. (1995). Contribution of the mitochondrial permeability transition to lethal injury after exposure of hepatocytes to t-butylhydroperoxide. Biochem. J. 307(Pt. 1), 99-106.
    • (1995) Biochem. J. , vol.307 , Issue.PART 1 , pp. 99-106
    • Nieminen, A.L.1    Saylor, A.K.2    Tesfai, S.A.3    Herman, B.4    Lemasters, J.J.5
  • 80
    • 0030963238 scopus 로고    scopus 로고
    • Mitochondrial permeability transition in hepatocytes induced by t-BuOOH: NAD(P)H and reactive oxygen species
    • Nieminen, A. L., Byrne, A. M., Herman, B., and Lemasters, J. J. (1997). Mitochondrial permeability transition in hepatocytes induced by t-BuOOH: NAD(P)H and reactive oxygen species. Am. J. Physiol. 272, C1286-C1294.
    • (1997) Am. J. Physiol. , vol.272
    • Nieminen, A.L.1    Byrne, A.M.2    Herman, B.3    Lemasters, J.J.4
  • 83
    • 0035421320 scopus 로고    scopus 로고
    • Propagation of the apoptotic signal by mitochondrial waves
    • Pacher, P., and Hajnoczky, G. (2001). Propagation of the apoptotic signal by mitochondrial waves. EMBO J. 20, 4107-4121.
    • (2001) EMBO J. , vol.20 , pp. 4107-4121
    • Pacher, P.1    Hajnoczky, G.2
  • 84
    • 0028306269 scopus 로고
    • Peroxynitrite causes calcium efflux from mitochondria which is prevented by cyclosporin A
    • Packer, M. A., and Murphy, M. P. (1994). Peroxynitrite causes calcium efflux from mitochondria which is prevented by cyclosporin A. FEBS Lett. 345, 237-240.
    • (1994) FEBS Lett. , vol.345 , pp. 237-240
    • Packer, M.A.1    Murphy, M.P.2
  • 85
    • 0030812638 scopus 로고    scopus 로고
    • The HtrA family of serine proteases
    • Pallen, M. J., and Wren, B. W. (1997). The HtrA family of serine proteases. Mol. Microbiol. 26, 209-221.
    • (1997) Mol. Microbiol. , vol.26 , pp. 209-221
    • Pallen, M.J.1    Wren, B.W.2
  • 86
    • 0035449164 scopus 로고    scopus 로고
    • tert-butylhydroperoxide induces peroxynitrite-dependent mitochondrial permeability transition leading PC12 cells to necrosis
    • Palomba, L., Sestili, P., and Cantoni, O. (2001). tert-Butylhydroperoxide induces peroxynitrite-dependent mitochondrial permeability transition leading PC12 cells to necrosis. J. Neurosci. Res. 65, 387-395.
    • (2001) J. Neurosci. Res. , vol.65 , pp. 387-395
    • Palomba, L.1    Sestili, P.2    Cantoni, O.3
  • 87
    • 0035811511 scopus 로고    scopus 로고
    • Mitochondrial endonuclease G is important for apoptosis in C. elegans
    • Parrish, J., Li, L., Klotz, K., Ledwich, D., Wang, X., and Xue, D. (2001). Mitochondrial endonuclease G is important for apoptosis in C. elegans. Nature 412, 90-94.
    • (2001) Nature , vol.412 , pp. 90-94
    • Parrish, J.1    Li, L.2    Klotz, K.3    Ledwich, D.4    Wang, X.5    Xue, D.6
  • 88
    • 0036510541 scopus 로고    scopus 로고
    • Mitochondrial binding of hexokinase II inhibits Bax-induced cytochrome c release and apoptosis
    • Pastorino, J. G., Shulga, N., and Hoek, J. B. (2002). Mitochondrial binding of hexokinase II inhibits Bax-induced cytochrome c release and apoptosis. J. Biol. Chem. 277, 7610-7618.
    • (2002) J. Biol. Chem. , vol.277 , pp. 7610-7618
    • Pastorino, J.G.1    Shulga, N.2    Hoek, J.B.3
  • 90
    • 0024787657 scopus 로고
    • The inner mitochondrial membrane contains ion-conducting channels similar to those found in bacteria
    • Petronilli, V., Szabo, I., and Zoratti, M. (1989). The inner mitochondrial membrane contains ion-conducting channels similar to those found in bacteria. FEBS Lett. 259, 137-143.
    • (1989) FEBS Lett. , vol.259 , pp. 137-143
    • Petronilli, V.1    Szabo, I.2    Zoratti, M.3
  • 91
    • 0033021780 scopus 로고    scopus 로고
    • Transient and long-lasting openings of the mitochondrial permeability transition pore can be monitored directly in intact cells by changes in mitochondrial calcein fluorescence
    • Petronilli, V., Miotto, G., Canton, M., Brini, M., Colonna, R., Bernardi, P., and Di Lisa, F. (1999). Transient and long-lasting openings of the mitochondrial permeability transition pore can be monitored directly in intact cells by changes in mitochondrial calcein fluorescence. Biophys. J. 76, 725-734.
    • (1999) Biophys. J. , vol.76 , pp. 725-734
    • Petronilli, V.1    Miotto, G.2    Canton, M.3    Brini, M.4    Colonna, R.5    Bernardi, P.6    Di Lisa, F.7
  • 93
    • 0033556544 scopus 로고    scopus 로고
    • The mitochondrial permeability transition mediates both necrotic and apoptotic death of hepatocytes exposed to Br-A23187
    • Qian, T., Herman, B., and Lemasters, J. J. (1999). The mitochondrial permeability transition mediates both necrotic and apoptotic death of hepatocytes exposed to Br-A23187. Toxicol. Appl. Pharmacol. 154, 117-125.
    • (1999) Toxicol. Appl. Pharmacol. , vol.154 , pp. 117-125
    • Qian, T.1    Herman, B.2    Lemasters, J.J.3
  • 94
    • 0028275459 scopus 로고
    • Inhibition of mitochondrial electron transport by peroxynitrite
    • Radi, R., Rodriguez, M., Castro, L., and Telleri, R. (1994). Inhibition of mitochondrial electron transport by peroxynitrite. Arch. Biochem. Biophys. 308, 89-95.
    • (1994) Arch. Biochem. Biophys. , vol.308 , pp. 89-95
    • Radi, R.1    Rodriguez, M.2    Castro, L.3    Telleri, R.4
  • 95
    • 0029064518 scopus 로고
    • Glutamate induces the production of reactive oxygen species in cultured forebrain neurons following NMDA receptor activation
    • Reynolds, I. J., and Hastings, T. G. (1995). Glutamate induces the production of reactive oxygen species in cultured forebrain neurons following NMDA receptor activation. J. Neurosci. 15, 3318-3327.
    • (1995) J. Neurosci. , vol.15 , pp. 3318-3327
    • Reynolds, I.J.1    Hastings, T.G.2
  • 96
    • 0032503058 scopus 로고    scopus 로고
    • Reconstituted adenine nucleotide translocase forms a channel for small molecules comparable to the mitochondrial permeability transition pore
    • Ruck, A., Dolder, M., Wallimann, T., and Brdiczka, D. (1998). Reconstituted adenine nucleotide translocase forms a channel for small molecules comparable to the mitochondrial permeability transition pore. FEBS Lett. 426, 97-101.
    • (1998) FEBS Lett. , vol.426 , pp. 97-101
    • Ruck, A.1    Dolder, M.2    Wallimann, T.3    Brdiczka, D.4
  • 97
    • 0029977549 scopus 로고    scopus 로고
    • 2+ release from intact rat liver mitochondria
    • 2+ release from intact rat liver mitochondria. Biochemistry 35, 4524-4528.
    • (1996) Biochemistry , vol.35 , pp. 4524-4528
    • Schweizer, M.1    Richter, C.2
  • 98
    • 0036007116 scopus 로고    scopus 로고
    • A distinct pathway remodels mitochondrial cristae and mobilizes cytochrome c during apoptosis
    • Scorrano, L., Ashiya, M., Buttle, K., Weiler, S., Oakes, S. A., Mannella, C. A., and Korsmeyer, S. J. (2002). A distinct pathway remodels mitochondrial cristae and mobilizes cytochrome c during apoptosis. Dev. Cell 2, 55-67.
    • (2002) Dev. Cell , vol.2 , pp. 55-67
    • Scorrano, L.1    Ashiya, M.2    Buttle, K.3    Weiler, S.4    Oakes, S.A.5    Mannella, C.A.6    Korsmeyer, S.J.7
  • 99
    • 0036205587 scopus 로고    scopus 로고
    • Mechanisms of caspase activation and inhibition during apoptosis
    • Shi, Y. (2002). Mechanisms of caspase activation and inhibition during apoptosis. Mol. Cell 9, 459-470.
    • (2002) Mol. Cell , vol.9 , pp. 459-470
    • Shi, Y.1
  • 100
    • 0033519705 scopus 로고    scopus 로고
    • Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC
    • Shimizu, S., Narita, M., and Tsujimoto, Y. (1999). Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC. Nature 399, 483-487.
    • (1999) Nature , vol.399 , pp. 483-487
    • Shimizu, S.1    Narita, M.2    Tsujimoto, Y.3
  • 101
    • 0033617146 scopus 로고    scopus 로고
    • A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein
    • Spiess, C., Beil, A., and Ehrmann, M. (1999). A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein. Cell 97, 339-347.
    • (1999) Cell , vol.97 , pp. 339-347
    • Spiess, C.1    Beil, A.2    Ehrmann, M.3
  • 103
    • 0034785591 scopus 로고    scopus 로고
    • A serine protease, HtrA2, is released from the mitochondria and interacts with XIAP, inducing cell death
    • Suzuki, Y., Imai, Y., Nakayama, H., Takahashi, K., Takio, K., and Takahashi, R. (2001). A serine protease, HtrA2, is released from the mitochondria and interacts with XIAP, inducing cell death. Mol. Cell 8, 613-621.
    • (2001) Mol. Cell , vol.8 , pp. 613-621
    • Suzuki, Y.1    Imai, Y.2    Nakayama, H.3    Takahashi, K.4    Takio, K.5    Takahashi, R.6
  • 104
    • 0025905910 scopus 로고
    • The giant channel of the inner mitochondrial membrane is inhibited by cyclosporin A
    • Szabo, I., and Zoratti, M. (1991). The giant channel of the inner mitochondrial membrane is inhibited by cyclosporin A. J. Biol. Chem. 266, 3376-3379.
    • (1991) J. Biol. Chem. , vol.266 , pp. 3376-3379
    • Szabo, I.1    Zoratti, M.2
  • 106
    • 0032575750 scopus 로고    scopus 로고
    • Caspases: Enemies within
    • Thornberry, N. A., and Lazebnik, Y. (1998). Caspases: Enemies within. Science 281, 1312-1316.
    • (1998) Science , vol.281 , pp. 1312-1316
    • Thornberry, N.A.1    Lazebnik, Y.2
  • 107
    • 0034191826 scopus 로고    scopus 로고
    • Quantitative analysis of Pc 4 localization in mouse lymphoma (LY-R) cells via double-label confocal fluorescence microscopy
    • Trivedi, N. S., Wang, H. W., Nieminen, A. L., Oleinick, N. L., and Izatt, J. A. (2000). Quantitative analysis of Pc 4 localization in mouse lymphoma (LY-R) cells via double-label confocal fluorescence microscopy. Photochem. Photobiol. 71, 634-639.
    • (2000) Photochem. Photobiol. , vol.71 , pp. 634-639
    • Trivedi, N.S.1    Wang, H.W.2    Nieminen, A.L.3    Oleinick, N.L.4    Izatt, J.A.5
  • 108
    • 0013818771 scopus 로고
    • Studies of necrosis in vitro of mouse hepatic parenchymal cells. Ultrastructural alterations in endoplasmic reticulum, Golgi apparatus, plasma membrane, and lipid droplets
    • Trump, B. F., Goldblatt, P. J., and Stowell, R. E. (1965). Studies of necrosis in vitro of mouse hepatic parenchymal cells. Ultrastructural alterations in endoplasmic reticulum, Golgi apparatus, plasma membrane, and lipid droplets. Lab. Invest. 14, 2000-2028.
    • (1965) Lab. Invest. , vol.14 , pp. 2000-2028
    • Trump, B.F.1    Goldblatt, P.J.2    Stowell, R.E.3
  • 109
    • 0033942613 scopus 로고    scopus 로고
    • BNIP3 and genetic control of necrosis-like cell death through the mitochondrial permeability transition pore
    • Vande, V. C., Cizeau, J., Dubik, D., Alimonti, J., Brown, T., Israels, S., Hakem, R., and Greenberg, A. H. (2000). BNIP3 and genetic control of necrosis-like cell death through the mitochondrial permeability transition pore. Mol. Cell. Biol. 20, 5454-5468.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 5454-5468
    • Vande, V.C.1    Cizeau, J.2    Dubik, D.3    Alimonti, J.4    Brown, T.5    Israels, S.6    Hakem, R.7    Greenberg, A.H.8
  • 110
    • 0034616942 scopus 로고    scopus 로고
    • Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins
    • Verhagen, A. M., Ekert, P. G., Pakusch, M., Silke, J., Connolly, L. M., Reid, G. E., Moritz, R. L., Simpson, R. J., and Vaux, D. L. (2000). Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins. Cell 102, 43-53.
    • (2000) Cell , vol.102 , pp. 43-53
    • Verhagen, A.M.1    Ekert, P.G.2    Pakusch, M.3    Silke, J.4    Connolly, L.M.5    Reid, G.E.6    Moritz, R.L.7    Simpson, R.J.8    Vaux, D.L.9
  • 112
    • 0025058739 scopus 로고
    • NADH-linked substrate dependence of peroxide-induced respiratory inhibition and calcium efflux in isolated renal mitochondria
    • Vlessis, A. A. (1990). NADH-linked substrate dependence of peroxide-induced respiratory inhibition and calcium efflux in isolated renal mitochondria. J. Biol. Chem. 265, 1448-1453.
    • (1990) J. Biol. Chem. , vol.265 , pp. 1448-1453
    • Vlessis, A.A.1
  • 113
    • 0026587335 scopus 로고
    • Mitochondrial genetics: A paradigm for aging and degenerative diseases?
    • Wallace, D. C. (1992). Mitochondrial genetics: A paradigm for aging and degenerative diseases? Science 256, 628-632.
    • (1992) Science , vol.256 , pp. 628-632
    • Wallace, D.C.1
  • 115
    • 0031036872 scopus 로고    scopus 로고
    • Prevention of apoptosis by Bcl-2: Release of cytochrome c from mitochondria blocked
    • Yang, J., Liu, X., Bhalla, K., Kim, C. N., Ibrado, A. M., Cai, J., Peng, T. I., Jones, D. P., and Wang, X. (1997). Prevention of apoptosis by Bcl-2: Release of cytochrome c from mitochondria blocked. Science 275, 1129-1132.
    • (1997) Science , vol.275 , pp. 1129-1132
    • Yang, J.1    Liu, X.2    Bhalla, K.3    Kim, C.N.4    Ibrado, A.M.5    Cai, J.6    Peng, T.I.7    Jones, D.P.8    Wang, X.9
  • 116
    • 0029116916 scopus 로고
    • The mitochondrial permeability transition
    • Zoratti, M., and Szabo, I. (1995). The mitochondrial permeability transition. Biochim. Biophys. Acta 1241, 139-176.
    • (1995) Biochim. Biophys. Acta , vol.1241 , pp. 139-176
    • Zoratti, M.1    Szabo, I.2
  • 117
    • 0030745646 scopus 로고    scopus 로고
    • Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3
    • Zou, H., Henzel, W. J., Liu, X., Lutschg, A., and Wang, X. (1997). Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3. Cell 90, 405-413.
    • (1997) Cell , vol.90 , pp. 405-413
    • Zou, H.1    Henzel, W.J.2    Liu, X.3    Lutschg, A.4    Wang, X.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.