메뉴 건너뛰기




Volumn 12, Issue 5-6, 2002, Pages 269-278

Single-channel currents of the permeability transition pore from the inner mitochondrial membrane of rat liver and of a human hepatoma cell line

Author keywords

Cyclosporin A; Inner mitochondrial membrane; Mitochondrial megachannel; Mitoplast; Patch clamp; Permeability transition pore

Indexed keywords

CALCIUM ION; CYCLOSPORIN A; EGTAZIC ACID; CALCIUM; CARRIER PROTEIN; CYCLOSPORIN; FAS ANTIGEN; ION CHANNEL; MITOCHONDRIAL PERMEABILITY TRANSITION PORE;

EID: 0036435713     PISSN: 10158987     EISSN: None     Source Type: Journal    
DOI: 10.1159/000067897     Document Type: Article
Times cited : (32)

References (44)
  • 1
    • 0023519987 scopus 로고
    • Patch-clamping of the inner mitochondrial membrane reveals a voltage-dependent ion channel
    • Sorgato MC, Keller BU, Stühmer W: Patch-clamping of the inner mitochondrial membrane reveals a voltage-dependent ion channel. Nature 1987;330:498-500.
    • (1987) Nature , vol.330 , pp. 498-500
    • Sorgato, M.C.1    Keller, B.U.2    Stühmer, W.3
  • 2
    • 0024431292 scopus 로고
    • Further investigation on the high-conductance ion channel of the inner membrane of mitochondria
    • Sorgato MC, Moran O, De Pinto V, Keller BU and Stuehmer W: Further investigation on the high-conductance ion channel of the inner membrane of mitochondria. J Bioenerg Biomembr 1989;21:485-496.
    • (1989) J Bioenerg Biomembr , vol.21 , pp. 485-496
    • Sorgato, M.C.1    Moran, O.2    De Pinto, V.3    Keller, B.U.4    Stuehmer, W.5
  • 3
    • 0025780245 scopus 로고
    • Inner mitochondrial membrane anion channel is present in brown adipocytes but is not identical with the uncoupling protein
    • Klitsch T, Siemen D: Inner mitochondrial membrane anion channel is present in brown adipocytes but is not identical with the uncoupling protein. J Membr Biol 1991;122:69-75.
    • (1991) J Membr Biol , vol.122 , pp. 69-75
    • Klitsch, T.1    Siemen, D.2
  • 4
    • 0026588320 scopus 로고
    • Properties of the inner membrane anion channel in intact mitochondria
    • Beavis AD: Properties of the inner membrane anion channel in intact mitochondria. J Bioenerg Biomembr 1992;24:77-90.
    • (1992) J Bioenerg Biomembr , vol.24 , pp. 77-90
    • Beavis, A.D.1
  • 5
    • 1842377980 scopus 로고    scopus 로고
    • 108-pS channel in brown fat mitochondria might be identical to the inner membrane anion channel
    • Borecky J, Jezek P, Siemen D: 108-pS channel in brown fat mitochondria might be identical to the inner membrane anion channel. J Biol Chem 1997;272:19282-19289.
    • (1997) J Biol Chem , vol.272 , pp. 19282-19289
    • Borecky, J.1    Jezek, P.2    Siemen, D.3
  • 6
    • 0024822215 scopus 로고
    • Blockade of a mitochondrial cationic channel by an addressing peptide: An electrophysiological study
    • Henry JP, Chich JF, Goldschmidt D, Thieffry M: Blockade of a mitochondrial cationic channel by an addressing peptide: An electrophysiological study. J Membr Biol 1989;112:139-147.
    • (1989) J Membr Biol , vol.112 , pp. 139-147
    • Henry, J.P.1    Chich, J.F.2    Goldschmidt, D.3    Thieffry, M.4
  • 7
    • 0025913049 scopus 로고
    • ATP-sensitive K+ channel in the mitochondrial inner membrane
    • Inoue I, Nagase H, Kishi K and Higuti T: ATP-sensitive K+ channel in the mitochondrial inner membrane. Nature 1991;352:244-247.
    • (1991) Nature , vol.352 , pp. 244-247
    • Inoue, I.1    Nagase, H.2    Kishi, K.3    Higuti, T.4
  • 8
    • 0030592185 scopus 로고    scopus 로고
    • Cation transport in mitochondria - The potassium cycle
    • Garlid KD: Cation transport in mitochondria - The potassium cycle. Biochim Biophys Acta 1996;1275:123-126.
    • (1996) Biochim Biophys Acta , vol.1275 , pp. 123-126
    • Garlid, K.D.1
  • 9
    • 0024433994 scopus 로고
    • Mitochondrial channel activity studied by patch-clamping mitoplasts
    • Kinnally KW, Campo ML, Tedeschi H: Mitochondrial channel activity studied by patch-clamping mitoplasts. J Bioenerg Biomembr 1989;21:497-506.
    • (1989) J Bioenerg Biomembr , vol.21 , pp. 497-506
    • Kinnally, K.W.1    Campo, M.L.2    Tedeschi, H.3
  • 10
    • 0027234336 scopus 로고
    • The mitochondrial permeability transition pore may comprise VDAC molecules. I. Binary structure and voltage dependence of the pore
    • Szabo I, Zoratti M: The mitochondrial permeability transition pore may comprise VDAC molecules. I. Binary structure and voltage dependence of the pore. FEBS Lett 1993;330:201-205.
    • (1993) FEBS Lett , vol.330 , pp. 201-205
    • Szabo, I.1    Zoratti, M.2
  • 11
    • 0027236162 scopus 로고
    • The mitochondrial permeability transition pore may comprise VDAC molecules. II. The electrophysiological properties of VDAC are compatible with those of the mitochondrial megachannel
    • Szabó I, De Pinto V, Zoratti M: The mitochondrial permeability transition pore may comprise VDAC molecules. II. The electrophysiological properties of VDAC are compatible with those of the mitochondrial megachannel. FEBS Lett 1993;330:206-210.
    • (1993) FEBS Lett , vol.330 , pp. 206-210
    • Szabó, I.1    De Pinto, V.2    Zoratti, M.3
  • 12
    • 0025905910 scopus 로고
    • The giant channel of the inner mitochondrial membrane is inhibited by cyclosporin A
    • Szabo I, Zoratti M: The giant channel of the inner mitochondrial membrane is inhibited by cyclosporin A. J Biol Chem 1991;266:3376-3379.
    • (1991) J Biol Chem , vol.266 , pp. 3376-3379
    • Szabo, I.1    Zoratti, M.2
  • 16
    • 0033290850 scopus 로고    scopus 로고
    • The mitochondrial permeability transition: Its molecular mechanism and role in reperfusion injury
    • Halestrap AP: The mitochondrial permeability transition: Its molecular mechanism and role in reperfusion injury. Biochem Soc Symp 1999;66:181-203.
    • (1999) Biochem Soc Symp , vol.66 , pp. 181-203
    • Halestrap, A.P.1
  • 17
    • 0034618269 scopus 로고    scopus 로고
    • Bax and bcl-xL independently regulate apoptotic changes of yeast mitochondria that require VDAC but not adenine nucleotide translocator
    • Shimizu S, Shinohara Y, Tsujimoto Y: Bax and bcl-xL independently regulate apoptotic changes of yeast mitochondria that require VDAC but not adenine nucleotide translocator. Oncogene 2000;19:4309-4318.
    • (2000) Oncogene , vol.19 , pp. 4309-4318
    • Shimizu, S.1    Shinohara, Y.2    Tsujimoto, Y.3
  • 19
    • 0032827410 scopus 로고    scopus 로고
    • Mitochondrial transport of cations: Channels, exchangers, and permeability transition
    • Bernardi P: Mitochondrial transport of cations: Channels, exchangers, and permeability transition. Physiol Rev 1999;79:1127-1155.
    • (1999) Physiol Rev , vol.79 , pp. 1127-1155
    • Bernardi, P.1
  • 20
    • 0033400223 scopus 로고    scopus 로고
    • Pathophysiology of mitochondrial cell death control
    • Vieira HLA, Kroemer G: Pathophysiology of mitochondrial cell death control. CMLS Cell Mol Life Sci 1999;56:971-976.
    • (1999) CMLS Cell Mol Life Sci , vol.56 , pp. 971-976
    • Vieira, H.L.A.1    Kroemer, G.2
  • 21
    • 0035897408 scopus 로고    scopus 로고
    • Cytochrome c maintains mitochondrial transmembrane potential and ATP generation after outer mitochondrial membrane permeabilization during the apoptotic process
    • Waterhouse, NJ, Goldstein JC, von Ahsen O, Schuler M, Newmeyer DD, Green DR: Cytochrome c maintains mitochondrial transmembrane potential and ATP generation after outer mitochondrial membrane permeabilization during the apoptotic process. J Cell Biol 2001;153:319-328.
    • (2001) J Cell Biol , vol.153 , pp. 319-328
    • Waterhouse, N.J.1    Goldstein, J.C.2    Von Ahsen, O.3    Schuler, M.4    Newmeyer, D.D.5    Green, D.R.6
  • 22
    • 0034668791 scopus 로고    scopus 로고
    • Mitochondrial intermembrane junctional complexes and their role in cell death
    • Crompton M: Mitochondrial intermembrane junctional complexes and their role in cell death. J Physiol 2000;529:11-21.
    • (2000) J Physiol , vol.529 , pp. 11-21
    • Crompton, M.1
  • 23
    • 0029245289 scopus 로고
    • A potential role for apoptosis in neurodegeneration and Alzheimer's disease
    • Cotman CW, Anderson AJ: A potential role for apoptosis in neurodegeneration and Alzheimer's disease. Mol Neurobiol 1995;10:19-45.
    • (1995) Mol Neurobiol , vol.10 , pp. 19-45
    • Cotman, C.W.1    Anderson, A.J.2
  • 24
    • 0033286594 scopus 로고    scopus 로고
    • Mitochondria, NO and neurodegeneration
    • Beal MF: Mitochondria, NO and neurodegeneration. Biochem Soc Symp 1999;66:43-54.
    • (1999) Biochem Soc Symp , vol.66 , pp. 43-54
    • Beal, M.F.1
  • 25
    • 0032842038 scopus 로고    scopus 로고
    • Dopamine oxidation alters mitochondrial respiration and induces permeability transition in brain mitochondria: Implications for Parkinson's disease
    • Berman SB and Hastings TG: Dopamine oxidation alters mitochondrial respiration and induces permeability transition in brain mitochondria: Implications for Parkinson's disease. J Neurochem 1999;73:1127-1137.
    • (1999) J Neurochem , vol.73 , pp. 1127-1137
    • Berman, S.B.1    Hastings, T.G.2
  • 27
    • 0031587822 scopus 로고    scopus 로고
    • Mitochondria are excitable organelles capable of generating and conveying electrical and calcium signals
    • Ichas F, Jouaville LS, Mazat JP: Mitochondria are excitable organelles capable of generating and conveying electrical and calcium signals. Cell 1997;89:1145-1153.
    • (1997) Cell , vol.89 , pp. 1145-1153
    • Ichas, F.1    Jouaville, L.S.2    Mazat, J.P.3
  • 28
    • 0025292743 scopus 로고
    • Mechanisms by which mitochondria transport calcium
    • Gunter TE, Pfeiffer DR: Mechanisms by which mitochondria transport calcium. Am J Physiol 1990;258:C755-C786.
    • (1990) Am J Physiol , vol.258
    • Gunter, T.E.1    Pfeiffer, D.R.2
  • 30
    • 0035499826 scopus 로고    scopus 로고
    • How cells choose to die
    • Lane D: How cells choose to die. Nature 2001;414:25-26.
    • (2001) Nature , vol.414 , pp. 25-26
    • Lane, D.1
  • 31
    • 0024388778 scopus 로고
    • Long-chain fatty acids act as protonophoric uncouplers of oxidative phosphorylation in rat liver mitochondria
    • Schönfeld P, Schild L, Kunz W: Long-chain fatty acids act as protonophoric uncouplers of oxidative phosphorylation in rat liver mitochondria. Biochim Biophys Acta 1989;977:266-272.
    • (1989) Biochim Biophys Acta , vol.977 , pp. 266-272
    • Schönfeld, P.1    Schild, L.2    Kunz, W.3
  • 32
    • 0026531719 scopus 로고
    • Bound and determined: A computer program for making buffers of defined ion concentrations
    • Brooks SP, Storey KB: Bound and determined: A computer program for making buffers of defined ion concentrations. Anal Biochem 1992;201:119-126.
    • (1992) Anal Biochem , vol.201 , pp. 119-126
    • Brooks, S.P.1    Storey, K.B.2
  • 34
    • 0026703122 scopus 로고
    • Modulation of the mitochondrial megachannel by divalent cations and protons
    • Szabó I, Bernardi P, Zoratti M: Modulation of the mitochondrial megachannel by divalent cations and protons. J Biol Chem 1992;267:2940-2946.
    • (1992) J Biol Chem , vol.267 , pp. 2940-2946
    • Szabó, I.1    Bernardi, P.2    Zoratti, M.3
  • 37
    • 0019230323 scopus 로고
    • Allosteric inhibition of the Ca2+-activated hydrophilic channel of the mitochondrial inner membrane by nucleotides
    • Haworth RA, Hunter DR: Allosteric inhibition of the Ca2+-activated hydrophilic channel of the mitochondrial inner membrane by nucleotides. J Membr Biol 1980;54:231-236.
    • (1980) J Membr Biol , vol.54 , pp. 231-236
    • Haworth, R.A.1    Hunter, D.R.2
  • 38
    • 0033002854 scopus 로고    scopus 로고
    • Manganese and calcium transport in mitochondria: Implications for manganese toxicity
    • Gavin CE, Gunter KK, Gunter TE: Manganese and calcium transport in mitochondria: Implications for manganese toxicity. Neurotoxicology 1999;20:445-453.
    • (1999) Neurotoxicology , vol.20 , pp. 445-453
    • Gavin, C.E.1    Gunter, K.K.2    Gunter, T.E.3
  • 39
    • 0033016172 scopus 로고    scopus 로고
    • Increased vulnerability of hippocampal neurons to excitotoxic necrosis in presenilin-1 mutant knock-in mice
    • Guo Q, Fu W, Sopher BL, Miller MW, Ware CB, Martin GM, Mattson MP: Increased vulnerability of hippocampal neurons to excitotoxic necrosis in presenilin-1 mutant knock-in mice. Nat Med 1999;5:101-106.
    • (1999) Nat Med , vol.5 , pp. 101-106
    • Guo, Q.1    Fu, W.2    Sopher, B.L.3    Miller, M.W.4    Ware, C.B.5    Martin, G.M.6    Mattson, M.P.7
  • 40
    • 0026687312 scopus 로고
    • Modulation of the mitochondrial permeability transition pore. Effect of protons and divalent cations
    • Bernardi P, Vassanelli S, Veronese P, Colonna R, Szabo I, Zoratti M: Modulation of the mitochondrial permeability transition pore. Effect of protons and divalent cations. J Biol Chem 1992;267:2934-2939.
    • (1992) J Biol Chem , vol.267 , pp. 2934-2939
    • Bernardi, P.1    Vassanelli, S.2    Veronese, P.3    Colonna, R.4    Szabo, I.5    Zoratti, M.6
  • 41
    • 0035853721 scopus 로고    scopus 로고
    • The mitochondrial permeability transition, release of cytochrome c and cell death. Correlation with the duration of pore openings in situ
    • Petronilli V, Penzo D, Scorrano L, Bernardi P, Di Lisa F: The mitochondrial permeability transition, release of cytochrome c and cell death. Correlation with the duration of pore openings in situ. J Biol Chem 2001;276:12030-12034.
    • (2001) J Biol Chem , vol.276 , pp. 12030-12034
    • Petronilli, V.1    Penzo, D.2    Scorrano, L.3    Bernardi, P.4    Di Lisa, F.5
  • 42
    • 0034068601 scopus 로고    scopus 로고
    • Mitochondrial control of cell death
    • Kroemer G, Reed JC: Mitochondrial control of cell death. Nat Med 2000;6:513-519.
    • (2000) Nat Med , vol.6 , pp. 513-519
    • Kroemer, G.1    Reed, J.C.2
  • 44
    • 0003443746 scopus 로고
    • Sinauer Assoc., Sunderland, MA
    • nd Edn., Sinauer Assoc., Sunderland, MA 1991.
    • (1991) nd Edn.
    • Hille, B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.