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Volumn 30, Issue 4, 1998, Pages 517-527

Mitochondrial permeability transition as induced by cross-linking of the adenine nucleotide translocase

Author keywords

Adenine nucleotide translocase; Calcium transport; Copper ortho phenanthroline; Membrane thiol groups; Mitochondria; Permeability transition; Protein cross linking

Indexed keywords

1,10 PHENANTHROLINE; 1,10 PHENANTHROLINE COPPER; ADENINE NUCLEOTIDE TRANSLOCASE; CALCIUM ION; CARBOXYATRACTYLOSIDE; COPPER; CYCLOSPORIN; DIMER; MALEIMIDE DERIVATIVE; MEMBRANE PROTEIN; MONOMER; THIOL GROUP;

EID: 0031745326     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1357-2725(97)00157-X     Document Type: Article
Times cited : (25)

References (45)
  • 1
    • 0017201717 scopus 로고
    • Safranine as a probe of the mitochondrial membrane potential
    • Akerman K.E.O., Wikström M.F.K. Safranine as a probe of the mitochondrial membrane potential. FEBS Lett. 68:1976;191-197.
    • (1976) FEBS Lett. , vol.68 , pp. 191-197
    • Akerman, K.E.O.1    Wikström, M.F.K.2
  • 3
    • 0017342852 scopus 로고
    • Effects of atractyloside and palmitoyl coenzyme A on calcium transport in cardiac mitochondria
    • Asimakis G.K., Sordhal L.A. Effects of atractyloside and palmitoyl coenzyme A on calcium transport in cardiac mitochondria. Arch. Biochem. Biophys. 179:1977;200-210.
    • (1977) Arch. Biochem. Biophys. , vol.179 , pp. 200-210
    • Asimakis, G.K.1    Sordhal, L.A.2
  • 4
    • 0024360271 scopus 로고
    • Cyclosporin A is a potent inhibitor of the inner membrane permeability transition in liver mitochondria
    • Broekemier K.M., Dempsey M.E., Pfeiffer D.R. Cyclosporin A is a potent inhibitor of the inner membrane permeability transition in liver mitochondria. J. Biol. Chem. 264:1989;7826-7830.
    • (1989) J. Biol. Chem. , vol.264 , pp. 7826-7830
    • Broekemier, K.M.1    Dempsey, M.E.2    Pfeiffer, D.R.3
  • 9
    • 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., Petronilli V., Bernardi P. Modulation of the mitochondrial permeability transition pore by pyridine nucleotides and dithiol oxidation at two separate sites. J. Biol. Chem. 271:1996;6746-6751.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6746-6751
    • Costantini, P.1    Chernyak, B.2    Petronilli, V.3    Bernardi, P.4
  • 10
    • 0023391047 scopus 로고
    • 2+-dependent pore activated by oxidative stress in heart mitochondria
    • 2+-dependent pore activated by oxidative stress in heart mitochondria. Biochem. J. 245:1987;915-918.
    • (1987) Biochem. J. , vol.245 , pp. 915-918
    • Crompton, M.1    Costi, A.2    Hayat, L.3
  • 12
    • 26744449473 scopus 로고
    • The mitochondrial/glutamate and ADP/ATP carrier switch from obligate counter exchange to unidirectional transport after modification by SH-reagents
    • Dierks T.H., Saletin A., Heberger C., Krämer R. The mitochondrial/glutamate and ADP/ATP carrier switch from obligate counter exchange to unidirectional transport after modification by SH-reagents. Biochim. Biophys. Acta. 1028:1990;280-288.
    • (1990) Biochim. Biophys. Acta , vol.1028 , pp. 280-288
    • Dierks, T.H.1    Saletin, A.2    Heberger, C.3    Krämer, R.4
  • 13
    • 49749177569 scopus 로고
    • A colorimetric method for determining low concentrations of mercaptans
    • Ellman G.L. A colorimetric method for determining low concentrations of mercaptans. Arch. Biochem. Biophys. 74:1958;443-447.
    • (1958) Arch. Biochem. Biophys. , vol.74 , pp. 443-447
    • Ellman, G.L.1
  • 15
    • 0023263612 scopus 로고
    • Action of cyclosporin A on mitochondrial calcium fluxes
    • Fournier N., Ducet G., Crevat A. Action of cyclosporin A on mitochondrial calcium fluxes. J. Bioenerg. Biomembr. 19:1987;297-303.
    • (1987) J. Bioenerg. Biomembr. , vol.19 , pp. 297-303
    • Fournier, N.1    Ducet, G.2    Crevat, A.3
  • 16
    • 0025292743 scopus 로고
    • Mechanism by which mitochondria transport calcium
    • Gunter T.E., Pfeiffer D.R. Mechanism by which mitochondria transport calcium. Am. J. Physiol. 258:1990;C755-C786.
    • (1990) Am. J. Physiol. , vol.258
    • Gunter, T.E.1    Pfeiffer, D.R.2
  • 17
    • 0025193488 scopus 로고
    • 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
    • 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.
    • (1990) Biochem. J. , vol.268 , pp. 153-160
    • Halestrap, A.P.1    Davidson, A.M.2
  • 18
    • 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., Connern C.P. Oxidative stress, thiol reagents and membrane potential modulate the mitochondrial permeability transition by affecting nucleotide binding to the adenine nucleotide translocase. J. Biol. Chem. 272:1997;3346-3354.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3346-3354
    • Halestrap, A.P.1    Woodfield, K.Y.2    Connern, C.P.3
  • 19
    • 0019324933 scopus 로고
    • Production of thiol groups and retention of calcium ions by cardiac mitochondria
    • Harris E.J., Baum H. Production of thiol groups and retention of calcium ions by cardiac mitochondria. Biochem. J. 186:1980;725-732.
    • (1980) Biochem. J. , vol.186 , pp. 725-732
    • Harris, E.J.1    Baum, H.2
  • 20
    • 0018332596 scopus 로고
    • 2+-induced membrane permeability transition in mitochondria. I. The protective mechanisms
    • 2+-induced membrane permeability transition in mitochondria. I. The protective mechanisms. Arch. Biochem. Biophys. 195:1979;453-459.
    • (1979) Arch. Biochem. Biophys. , vol.195 , pp. 453-459
    • Hunter, D.R.1    Haworth, R.A.2
  • 21
    • 0023834932 scopus 로고
    • 2+ binding site on the cytoplasmic side of the inner membrane
    • 2+ binding site on the cytoplasmic side of the inner membrane. J. Biol. Chem. 263:1988;1405-1412.
    • (1988) J. Biol. Chem. , vol.263 , pp. 1405-1412
    • Igbavboa, U.1    Pfeiffer, D.R.2
  • 23
    • 0021679015 scopus 로고
    • 32Π -ATP exchange in bovine heart electron transport particles
    • 32Π -ATP exchange in bovine heart electron transport particles J. Biol. Chem. 259:1984;12742-12748.
    • (1984) J. Biol. Chem. , vol.259 , pp. 12742-12748
    • Joshi, S.1    Torok, K.2
  • 24
    • 0022273195 scopus 로고
    • Principles of carrier catalysis elucidated by comparing two similar membrane translocators from mitochondria, the ADP/ATP carrier and the uncoupling protein
    • in; G. Semenza, R. Kinne (Eds.)
    • M. Klingenberg, Principles of carrier catalysis elucidated by comparing two similar membrane translocators from mitochondria, the ADP/ATP carrier and the uncoupling protein, in; G. Semenza, R. Kinne (Eds.), Membrane Transport Driven by Ion Gradients, Ann. N. Y. Acad. Sci. 456 (1985) 279-288.
    • (1985) Membrane Transport Driven by Ion Gradients, Ann. N. Y. Acad. Sci. , vol.456 , pp. 279-288
    • Klingenberg, M.1
  • 25
    • 0025739622 scopus 로고
    • Phenylarsine oxide induces the cyclosporin A-sensitive membrane permeability transition in rat liver mitochondria
    • Lenartowicz E., Bernardi P., Azzone G.F. Phenylarsine oxide induces the cyclosporin A-sensitive membrane permeability transition in rat liver mitochondria. J. Bioenerg. Biomembr. 23:1991;679-688.
    • (1991) J. Bioenerg. Biomembr. , vol.23 , pp. 679-688
    • Lenartowicz, E.1    Bernardi, P.2    Azzone, G.F.3
  • 26
    • 0023759935 scopus 로고
    • Involvement of the ADP/ATP carrier in calcium-induced perturbations of the mitochondrial inner membrane permeability: Importance of the orientation of the nucleotide binding site
    • LeQuoc K., LeQuoc D. Involvement of the ADP/ATP carrier in calcium-induced perturbations of the mitochondrial inner membrane permeability: Importance of the orientation of the nucleotide binding site. Arch. Biochem. Biophys. 265:1988;249-257.
    • (1988) Arch. Biochem. Biophys. , vol.265 , pp. 249-257
    • Lequoc, K.1    Lequoc, D.2
  • 28
    • 0028064745 scopus 로고
    • Importance of loops of mitochondrial ADP/ATP carrier for its transport activity deduced from reactivities of its cysteine residues with the sulfhydryl reagent eosin-5-maleimide
    • Majima M., Shinohara Y., Yamaguchi N., Hong Y.M., Terada H. Importance of loops of mitochondrial ADP/ATP carrier for its transport activity deduced from reactivities of its cysteine residues with the sulfhydryl reagent eosin-5-maleimide. Biochemistry. 33:1994;9530-9535.
    • (1994) Biochemistry , vol.33 , pp. 9530-9535
    • Majima, M.1    Shinohara, Y.2    Yamaguchi, N.3    Hong, Y.M.4    Terada, H.5
  • 29
    • 0028840853 scopus 로고
    • Translocation of loops regulates transport activity of mitochondrial ADP/ATP carrier deduced from formation of a specific intermolecular disulfide bridge catalyzed by copper-o-phenanthroline
    • Majima E., Ikawa K., Takeda M., Hashimoto M., Shinohara Y., Terada H. Translocation of loops regulates transport activity of mitochondrial ADP/ATP carrier deduced from formation of a specific intermolecular disulfide bridge catalyzed by copper-o-phenanthroline. J. Biol. Chem. 270:1995;29548-29554.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29548-29554
    • Majima, E.1    Ikawa, K.2    Takeda, M.3    Hashimoto, M.4    Shinohara, Y.5    Terada, H.6
  • 31
    • 0021356527 scopus 로고
    • Rotational diffusion of the ADP/ATP translocator in the inner membrane of mitochondria and in proteoliposomes
    • Müller M., Krebs J.J.R., Cherry R.J., Kawato S. Rotational diffusion of the ADP/ATP translocator in the inner membrane of mitochondria and in proteoliposomes. J. Biol. Chem. 259:1984;3037-3043.
    • (1984) J. Biol. Chem. , vol.259 , pp. 3037-3043
    • Müller, M.1    Krebs, J.J.R.2    Cherry, R.J.3    Kawato, S.4
  • 32
    • 0023245601 scopus 로고
    • Ion permeability induction by the SH cross-linking reagents in rat liver mitochondria is inhibited by the free radical scavenger, buthylhydroperoxytoluene
    • Novgorodov S.A., Kultayeva E.V., Yaguzhinsky L.S., Lemeshko V.V. Ion permeability induction by the SH cross-linking reagents in rat liver mitochondria is inhibited by the free radical scavenger, buthylhydroperoxytoluene. J. Bioenerg. Biomembr. 19:1987;191-202.
    • (1987) J. Bioenerg. Biomembr. , vol.19 , pp. 191-202
    • Novgorodov, S.A.1    Kultayeva, E.V.2    Yaguzhinsky, L.S.3    Lemeshko, V.V.4
  • 33
    • 0025679160 scopus 로고
    • Effect of ADP/ATP antiporter conformational state on the suppression of the non-specific permeability of the inner mitochondrial membrane
    • Novgorodov S.A., Gudz T.I., Kushnareva Y.E., Zorov D.B., Kudrjashov Y.B. Effect of ADP/ATP antiporter conformational state on the suppression of the non-specific permeability of the inner mitochondrial membrane. FEBS Lett. 277:1990;123-126.
    • (1990) FEBS Lett. , vol.277 , pp. 123-126
    • Novgorodov, S.A.1    Gudz, T.I.2    Kushnareva, Y.E.3    Zorov, D.B.4    Kudrjashov, Y.B.5
  • 34
    • 0025934444 scopus 로고
    • The nonspecific inner membrane pore of liver mitochondria: Modulation of cyclosporin sensitivity by ADP at carboxyatractyloside-sensitive and insensitive sites
    • Novgorodov S.A., Gudz T.I., Jung D.W., Brierley G.P. The nonspecific inner membrane pore of liver mitochondria: Modulation of cyclosporin sensitivity by ADP at carboxyatractyloside-sensitive and insensitive sites. Biochem. Biophys. Res. Commun. 180:1991;33-38.
    • (1991) Biochem. Biophys. Res. Commun. , vol.180 , pp. 33-38
    • Novgorodov, S.A.1    Gudz, T.I.2    Jung, D.W.3    Brierley, G.P.4
  • 35
    • 0028340683 scopus 로고
    • Magnesium ion modulates the sensitivity of the mitochondrial permeability transition pore to cyclosporin A and ADP
    • Novgorodov S.A., Gudz T.I., Brierley G.P., Pfeiffer D.R. Magnesium ion modulates the sensitivity of the mitochondrial permeability transition pore to cyclosporin A and ADP. Arch. Biochem. Biophys. 311:1994;219-228.
    • (1994) Arch. Biochem. Biophys. , vol.311 , pp. 219-228
    • Novgorodov, S.A.1    Gudz, T.I.2    Brierley, G.P.3    Pfeiffer, D.R.4
  • 37
    • 0028239794 scopus 로고
    • 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
    • Petronilli V., Costantini P., Scorrano L., Colonna R., Passamonti S., Bernardi P. 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;16638-16642.
    • (1994) J. Biol. Chem. , vol.269 , pp. 16638-16642
    • Petronilli, V.1    Costantini, P.2    Scorrano, L.3    Colonna, R.4    Passamonti, S.5    Bernardi, P.6
  • 38
    • 0016734199 scopus 로고
    • Solubilization of the carboxy-atractyloside binding protein from mitochondria
    • Riccio P., Aquila H., Klingenberg M. Solubilization of the carboxy-atractyloside binding protein from mitochondria. FEBS Lett. 56:1975;133-138.
    • (1975) FEBS Lett. , vol.56 , pp. 133-138
    • Riccio, P.1    Aquila, H.2    Klingenberg, M.3
  • 41
    • 0020535504 scopus 로고
    • On the relationship between calcium and phosphate transport, transmembrane potential and acetoacetate-induced oxidation of pyridine nucleotides in rat-liver mitochondria
    • Siliprandi D., Siliprandi N., Toninello A. On the relationship between calcium and phosphate transport, transmembrane potential and acetoacetate-induced oxidation of pyridine nucleotides in rat-liver mitochondria. Eur J. Biochem. 130:1983;173-175.
    • (1983) Eur J. Biochem. , vol.130 , pp. 173-175
    • Siliprandi, D.1    Siliprandi, N.2    Toninello, A.3
  • 44
    • 0027436057 scopus 로고
    • The participation of reactive oxygen species and protein thiols in the mechanism of mitochondrial inner membrane permeabilization by calcium plus prooxidants
    • Valle V.G.R., Fagian M.M., Parentoni L.S., Meinicke A.R., Vercesi A.E. The participation of reactive oxygen species and protein thiols in the mechanism of mitochondrial inner membrane permeabilization by calcium plus prooxidants. Arch. Biochem. Biophys. 307:1993;1-7.
    • (1993) Arch. Biochem. Biophys. , vol.307 , pp. 1-7
    • Valle, V.G.R.1    Fagian, M.M.2    Parentoni, L.S.3    Meinicke, A.R.4    Vercesi, A.E.5
  • 45
    • 0029116916 scopus 로고
    • The mitochondrial permeability transition
    • 176
    • Zoratti M., Szabò I. The mitochondrial permeability transition. Biochim. Biophys. Acta. 1241:1995;139-176.
    • (1995) Biochim. Biophys. Acta , vol.1241
    • Zoratti, M.1    Szabò, I.2


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