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Volumn 21, Issue 2, 2015, Pages 206-214

Physiological and Pathological Roles of the Mitochondrial Permeability Transition Pore in the Heart

Author keywords

[No Author keywords available]

Indexed keywords

ADENINE NUCLEOTIDE TRANSLOCASE; BINDING PROTEIN; CARRIER PROTEIN; COMPLEMENT COMPONENT C1Q; COMPLEMENT COMPONENT C1Q BINDING PROTEIN; CYCLOPHILIN D; CYCLOPHILIN INHIBITOR; CYCLOSPORIN A; HEXOKINASE; MITOCHONDRIAL PERMEABILITY TRANSITION PORE; MITOCHONDRIAL PROTEIN; PHOSPHATE TRANSPORTER; PROTEIN BAK; PROTEIN BAX; PROTEIN TSPO; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; REACTIVE OXYGEN METABOLITE; UNCLASSIFIED DRUG; VOLTAGE DEPENDENT ANION CHANNEL; CALCIUM;

EID: 84922950911     PISSN: 15504131     EISSN: 19327420     Source Type: Journal    
DOI: 10.1016/j.cmet.2014.12.001     Document Type: Review
Times cited : (344)

References (117)
  • 1
    • 0022931338 scopus 로고
    • The reversible Ca2+-induced permeabilization of rat liver mitochondria
    • I. Al-Nasser, and M. Crompton The reversible Ca2+-induced permeabilization of rat liver mitochondria Biochem. J. 239 1986 19 29
    • (1986) Biochem. J. , vol.239 , pp. 19-29
    • Al-Nasser, I.1    Crompton, M.2
  • 3
    • 37849006735 scopus 로고    scopus 로고
    • A high-throughput screening for mammalian cell death effectors identifies the mitochondrial phosphate carrier as a regulator of cytochrome c release
    • S. Alcalá, M. Klee, J. Fernández, A. Fleischer, and F.X. Pimentel-Muiños A high-throughput screening for mammalian cell death effectors identifies the mitochondrial phosphate carrier as a regulator of cytochrome c release Oncogene 27 2008 44 54
    • (2008) Oncogene , vol.27 , pp. 44-54
    • Alcalá, S.1    Klee, M.2    Fernández, J.3    Fleischer, A.4    Pimentel-Muiños, F.X.5
  • 6
    • 34247895697 scopus 로고    scopus 로고
    • Voltage-dependent anion channels are dispensable for mitochondrial-dependent cell death
    • C.P. Baines, R.A. Kaiser, T. Sheiko, W.J. Craigen, and J.D. Molkentin Voltage-dependent anion channels are dispensable for mitochondrial-dependent cell death Nat. Cell Biol. 9 2007 550 555
    • (2007) Nat. Cell Biol. , vol.9 , pp. 550-555
    • Baines, C.P.1    Kaiser, R.A.2    Sheiko, T.3    Craigen, W.J.4    Molkentin, J.D.5
  • 8
    • 68649092333 scopus 로고    scopus 로고
    • The role of Ca(2+) signaling in the coordination of mitochondrial ATP production with cardiac work
    • R.S. Balaban The role of Ca(2+) signaling in the coordination of mitochondrial ATP production with cardiac work Biochim. Biophys. Acta 1787 2009 1334 1341
    • (2009) Biochim. Biophys. Acta , vol.1787 , pp. 1334-1341
    • Balaban, R.S.1
  • 9
    • 21244446551 scopus 로고    scopus 로고
    • Properties of the permeability transition pore in mitochondria devoid of Cyclophilin D
    • E. Basso, L. Fante, J. Fowlkes, V. Petronilli, M.A. Forte, and P. Bernardi Properties of the permeability transition pore in mitochondria devoid of Cyclophilin D J. Biol. Chem. 280 2005 18558 18561
    • (2005) J. Biol. Chem. , vol.280 , pp. 18558-18561
    • Basso, E.1    Fante, L.2    Fowlkes, J.3    Petronilli, V.4    Forte, M.A.5    Bernardi, P.6
  • 11
    • 0019332988 scopus 로고
    • The relationship between mitochondrial membrane permeability, membrane potential, and the retention of Ca2+ by mitochondria
    • M.C. Beatrice, J.W. Palmer, and D.R. Pfeiffer The relationship between mitochondrial membrane permeability, membrane potential, and the retention of Ca2+ by mitochondria J. Biol. Chem. 255 1980 8663 8671
    • (1980) J. Biol. Chem. , vol.255 , pp. 8663-8671
    • Beatrice, M.C.1    Palmer, J.W.2    Pfeiffer, D.R.3
  • 12
    • 84863206432 scopus 로고    scopus 로고
    • The permeability transition pore as a Ca(2+) release channel: New answers to an old question
    • P. Bernardi, and S. von Stockum The permeability transition pore as a Ca(2+) release channel: new answers to an old question Cell Calcium 52 2012 22 27
    • (2012) Cell Calcium , vol.52 , pp. 22-27
    • Bernardi, P.1    Von Stockum, S.2
  • 14
    • 79952007628 scopus 로고    scopus 로고
    • Adenine nucleotide translocase family: Four isoforms for apoptosis modulation in cancer
    • C. Brenner, K. Subramaniam, C. Pertuiset, and S. Pervaiz Adenine nucleotide translocase family: four isoforms for apoptosis modulation in cancer Oncogene 30 2011 883 895
    • (2011) Oncogene , vol.30 , pp. 883-895
    • Brenner, C.1    Subramaniam, K.2    Pertuiset, C.3    Pervaiz, S.4
  • 15
    • 0029953927 scopus 로고    scopus 로고
    • Mitochondrial ADP/ATP carrier can be reversibly converted into a large channel by Ca2+
    • N. Brustovetsky, and M. Klingenberg Mitochondrial ADP/ATP carrier can be reversibly converted into a large channel by Ca2+ Biochemistry 35 1996 8483 8488
    • (1996) Biochemistry , vol.35 , pp. 8483-8488
    • Brustovetsky, N.1    Klingenberg, M.2
  • 16
    • 0036771787 scopus 로고    scopus 로고
    • A large Ca2+-dependent channel formed by recombinant ADP/ATP carrier from Neurospora crassa resembles the mitochondrial permeability transition pore
    • N. Brustovetsky, M. Tropschug, S. Heimpel, D. Heidkämper, and M. Klingenberg A large Ca2+-dependent channel formed by recombinant ADP/ATP carrier from Neurospora crassa resembles the mitochondrial permeability transition pore Biochemistry 41 2002 11804 11811
    • (2002) Biochemistry , vol.41 , pp. 11804-11811
    • Brustovetsky, N.1    Tropschug, M.2    Heimpel, S.3    Heidkämper, D.4    Klingenberg, M.5
  • 17
    • 0035868944 scopus 로고    scopus 로고
    • Peripheral-type benzodiazepine receptor ligands: Mitochondrial permeability transition induction in rat cardiac tissue
    • B. Chelli, A. Falleni, F. Salvetti, V. Gremigni, A. Lucacchini, and C. Martini Peripheral-type benzodiazepine receptor ligands: mitochondrial permeability transition induction in rat cardiac tissue Biochem. Pharmacol. 61 2001 695 705
    • (2001) Biochem. Pharmacol. , vol.61 , pp. 695-705
    • Chelli, B.1    Falleni, A.2    Salvetti, F.3    Gremigni, V.4    Lucacchini, A.5    Martini, C.6
  • 19
    • 38349035719 scopus 로고    scopus 로고
    • Excessive reactive oxygen species induces apoptosis in fibroblasts: Role of mitochondrially accumulated hyaluronic acid binding protein 1 (HABP1/p32/gC1qR)
    • A.R. Chowdhury, I. Ghosh, and K. Datta Excessive reactive oxygen species induces apoptosis in fibroblasts: role of mitochondrially accumulated hyaluronic acid binding protein 1 (HABP1/p32/gC1qR) Exp. Cell Res. 314 2008 651 667
    • (2008) Exp. Cell Res. , vol.314 , pp. 651-667
    • Chowdhury, A.R.1    Ghosh, I.2    Datta, K.3
  • 20
    • 0037144409 scopus 로고    scopus 로고
    • Sanglifehrin A acts as a potent inhibitor of the mitochondrial permeability transition and reperfusion injury of the heart by binding to cyclophilin-D at a different site from cyclosporin A
    • S.J. Clarke, G.P. McStay, and A.P. Halestrap Sanglifehrin A acts as a potent inhibitor of the mitochondrial permeability transition and reperfusion injury of the heart by binding to cyclophilin-D at a different site from cyclosporin A J. Biol. Chem. 277 2002 34793 34799
    • (2002) J. Biol. Chem. , vol.277 , pp. 34793-34799
    • Clarke, S.J.1    McStay, G.P.2    Halestrap, A.P.3
  • 21
    • 0024271346 scopus 로고
    • Kinetic evidence for a heart mitochondrial pore activated by Ca2+, inorganic phosphate and oxidative stress. A potential mechanism for mitochondrial dysfunction during cellular Ca2+ overload
    • M. Crompton, and A. Costi Kinetic evidence for a heart mitochondrial pore activated by Ca2+, inorganic phosphate and oxidative stress. A potential mechanism for mitochondrial dysfunction during cellular Ca2+ overload Eur. J. Biochem. 178 1988 489 501
    • (1988) Eur. J. Biochem. , vol.178 , pp. 489-501
    • Crompton, M.1    Costi, A.2
  • 22
    • 0023821864 scopus 로고
    • Inhibition by cyclosporin A of a Ca2+-dependent pore in heart mitochondria activated by inorganic phosphate and oxidative stress
    • M. Crompton, H. Ellinger, and A. Costi Inhibition by cyclosporin A of a Ca2+-dependent pore in heart mitochondria activated by inorganic phosphate and oxidative stress Biochem. J. 255 1988 357 360
    • (1988) Biochem. J. , vol.255 , pp. 357-360
    • Crompton, M.1    Ellinger, H.2    Costi, A.3
  • 23
    • 0032401567 scopus 로고    scopus 로고
    • Cyclophilin-D binds strongly to complexes of the voltage-dependent anion channel and the adenine nucleotide translocase to form the permeability transition pore
    • M. Crompton, S. Virji, and J.M. Ward Cyclophilin-D binds strongly to complexes of the voltage-dependent anion channel and the adenine nucleotide translocase to form the permeability transition pore Eur. J. Biochem. 258 1998 729 735
    • (1998) Eur. J. Biochem. , vol.258 , pp. 729-735
    • Crompton, M.1    Virji, S.2    Ward, J.M.3
  • 24
    • 84901978868 scopus 로고    scopus 로고
    • The mitochondrial permeability transition pore is a dispensable element for mitochondrial calcium efflux
    • E. De Marchi, M. Bonora, C. Giorgi, and P. Pinton The mitochondrial permeability transition pore is a dispensable element for mitochondrial calcium efflux Cell Calcium 56 2014 1 13
    • (2014) Cell Calcium , vol.56 , pp. 1-13
    • De Marchi, E.1    Bonora, M.2    Giorgi, C.3    Pinton, P.4
  • 25
    • 80051936634 scopus 로고    scopus 로고
    • A forty-kilodalton protein of the inner membrane is the mitochondrial calcium uniporter
    • D. De Stefani, A. Raffaello, E. Teardo, I. Szabò, and R. Rizzuto A forty-kilodalton protein of the inner membrane is the mitochondrial calcium uniporter Nature 476 2011 336 340
    • (2011) Nature , vol.476 , pp. 336-340
    • De Stefani, D.1    Raffaello, A.2    Teardo, E.3    Szabò, I.4    Rizzuto, R.5
  • 26
    • 12744273967 scopus 로고    scopus 로고
    • A fourth ADP/ATP carrier isoform in man: Identification, bacterial expression, functional characterization and tissue distribution
    • V. Dolce, P. Scarcia, D. Iacopetta, and F. Palmieri A fourth ADP/ATP carrier isoform in man: identification, bacterial expression, functional characterization and tissue distribution FEBS Lett. 579 2005 633 637
    • (2005) FEBS Lett. , vol.579 , pp. 633-637
    • Dolce, V.1    Scarcia, P.2    Iacopetta, D.3    Palmieri, F.4
  • 27
    • 84876777712 scopus 로고    scopus 로고
    • Physiologic functions of cyclophilin D and the mitochondrial permeability transition pore
    • J.W. Elrod, and J.D. Molkentin Physiologic functions of cyclophilin D and the mitochondrial permeability transition pore Circ. J. 77 2013 1111 1122
    • (2013) Circ. J. , vol.77 , pp. 1111-1122
    • Elrod, J.W.1    Molkentin, J.D.2
  • 29
    • 80052465160 scopus 로고    scopus 로고
    • Imaging superoxide flash and metabolism-coupled mitochondrial permeability transition in living animals
    • H. Fang, M. Chen, Y. Ding, W. Shang, J. Xu, X. Zhang, W. Zhang, K. Li, Y. Xiao, and F. Gao Imaging superoxide flash and metabolism-coupled mitochondrial permeability transition in living animals Cell Res. 21 2011 1295 1304
    • (2011) Cell Res. , vol.21 , pp. 1295-1304
    • Fang, H.1    Chen, M.2    Ding, Y.3    Shang, W.4    Xu, J.5    Zhang, X.6    Zhang, W.7    Li, K.8    Xiao, Y.9    Gao, F.10
  • 30
    • 0023263612 scopus 로고
    • Action of cyclosporine on mitochondrial calcium fluxes
    • N. Fournier, G. Ducet, and A. Crevat Action of cyclosporine 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
  • 33
    • 33846018602 scopus 로고    scopus 로고
    • Cell death by necrosis: Towards a molecular definition
    • P. Golstein, and G. Kroemer Cell death by necrosis: towards a molecular definition Trends Biochem. Sci. 32 2007 37 43
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 37-43
    • Golstein, P.1    Kroemer, G.2
  • 34
    • 34548448546 scopus 로고    scopus 로고
    • Inhibition of mitochondrial permeability transition improves functional recovery and reduces mortality following acute myocardial infarction in mice
    • L. Gomez, H. Thibault, A. Gharib, J.M. Dumont, G. Vuagniaux, P. Scalfaro, G. Derumeaux, and M. Ovize Inhibition of mitochondrial permeability transition improves functional recovery and reduces mortality following acute myocardial infarction in mice Am. J. Physiol. Heart Circ. Physiol. 293 2007 H1654 H1661
    • (2007) Am. J. Physiol. Heart Circ. Physiol. , vol.293 , pp. H1654-H1661
    • Gomez, L.1    Thibault, H.2    Gharib, A.3    Dumont, J.M.4    Vuagniaux, G.5    Scalfaro, P.6    Derumeaux, G.7    Ovize, M.8
  • 35
    • 0031011211 scopus 로고    scopus 로고
    • A mouse model for mitochondrial myopathy and cardiomyopathy resulting from a deficiency in the heart/muscle isoform of the adenine nucleotide translocator
    • B.H. Graham, K.G. Waymire, B. Cottrell, I.A. Trounce, G.R. MacGregor, and D.C. Wallace A mouse model for mitochondrial myopathy and cardiomyopathy resulting from a deficiency in the heart/muscle isoform of the adenine nucleotide translocator Nat. Genet. 16 1997 226 234
    • (1997) Nat. Genet. , vol.16 , pp. 226-234
    • Graham, B.H.1    Waymire, K.G.2    Cottrell, B.3    Trounce, I.A.4    Macgregor, G.R.5    Wallace, D.C.6
  • 36
    • 0027761474 scopus 로고
    • Protection by Cyclosporin A of ischemia/reperfusion-induced damage in isolated rat hearts
    • E.J. Griffiths, and A.P. Halestrap Protection by Cyclosporin A of ischemia/reperfusion-induced damage in isolated rat hearts J. Mol. Cell. Cardiol. 25 1993 1461 1469
    • (1993) J. Mol. Cell. Cardiol. , vol.25 , pp. 1461-1469
    • Griffiths, E.J.1    Halestrap, A.P.2
  • 37
    • 0028968606 scopus 로고
    • Mitochondrial non-specific pores remain closed during cardiac ischaemia, but open upon reperfusion
    • E.J. Griffiths, and A.P. Halestrap Mitochondrial non-specific pores remain closed during cardiac ischaemia, but open upon reperfusion Biochem. J. 307 1995 93 98
    • (1995) Biochem. J. , vol.307 , pp. 93-98
    • Griffiths, E.J.1    Halestrap, A.P.2
  • 39
    • 67349117275 scopus 로고    scopus 로고
    • What is the mitochondrial permeability transition pore?
    • A.P. Halestrap What is the mitochondrial permeability transition pore? J. Mol. Cell. Cardiol. 46 2009 821 831
    • (2009) J. Mol. Cell. Cardiol. , vol.46 , pp. 821-831
    • Halestrap, A.P.1
  • 40
    • 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
    • A.P. Halestrap, and A.M. Davidson 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 1990 153 160
    • (1990) Biochem. J. , vol.268 , pp. 153-160
    • Halestrap, A.P.1    Davidson, A.M.2
  • 41
    • 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
    • A.P. Halestrap, K.Y. Woodfield, and C.P. Connern 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
  • 42
    • 1142273368 scopus 로고    scopus 로고
    • Mitochondrial permeability transition pore opening during myocardial reperfusion - A target for cardioprotection
    • A.P. Halestrap, S.J. Clarke, and S.A. Javadov Mitochondrial permeability transition pore opening during myocardial reperfusion - a target for cardioprotection Cardiovasc. Res. 61 2004 372 385
    • (2004) Cardiovasc. Res. , vol.61 , pp. 372-385
    • Halestrap, A.P.1    Clarke, S.J.2    Javadov, S.A.3
  • 43
    • 84925872846 scopus 로고    scopus 로고
    • The role of hexokinase in cardioprotection - Mechanism and potential for translation
    • Published online September 10, 2014
    • A.P. Halestrap, G.C. Pereira, and P. Pasdois The role of hexokinase in cardioprotection - mechanism and potential for translation Br. J. Pharmacol. 2014 10.1111/bph.12899 Published online September 10, 2014
    • (2014) Br. J. Pharmacol.
    • Halestrap, A.P.1    Pereira, G.C.2    Pasdois, P.3
  • 44
    • 0031680036 scopus 로고    scopus 로고
    • Role of mitochondrial calcium transport in the control of substrate oxidation
    • R.G. Hansford, and D. Zorov Role of mitochondrial calcium transport in the control of substrate oxidation Mol. Cell. Biochem. 184 1998 359 369
    • (1998) Mol. Cell. Biochem. , vol.184 , pp. 359-369
    • Hansford, R.G.1    Zorov, D.2
  • 45
    • 0026325774 scopus 로고
    • Control of mitochondrial ATP synthesis in the heart
    • D.A. Harris, and A.M. Das Control of mitochondrial ATP synthesis in the heart Biochem. J. 280 1991 561 573
    • (1991) Biochem. J. , vol.280 , pp. 561-573
    • Harris, D.A.1    Das, A.M.2
  • 46
    • 0018332597 scopus 로고
    • The Ca2+-induced membrane transition in mitochondria. II. Nature of the Ca2+ trigger site
    • R.A. Haworth, and D.R. Hunter The Ca2+-induced membrane transition in mitochondria. II. Nature of the Ca2+ trigger site Arch. Biochem. Biophys. 195 1979 460 467
    • (1979) Arch. Biochem. Biophys. , vol.195 , pp. 460-467
    • Haworth, R.A.1    Hunter, D.R.2
  • 47
    • 0034014265 scopus 로고    scopus 로고
    • Control of the mitochondrial permeability transition pore by high-affinity ADP binding at the ADP/ATP translocase in permeabilized mitochondria
    • R.A. Haworth, and D.R. Hunter Control of the mitochondrial permeability transition pore by high-affinity ADP binding at the ADP/ATP translocase in permeabilized mitochondria J. Bioenerg. Biomembr. 32 2000 91 96
    • (2000) J. Bioenerg. Biomembr. , vol.32 , pp. 91-96
    • Haworth, R.A.1    Hunter, D.R.2
  • 49
    • 0018332596 scopus 로고
    • The Ca2+-induced membrane transition in mitochondria. I. The protective mechanisms
    • D.R. Hunter, and R.A. Haworth The Ca2+-induced membrane 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
  • 50
    • 0018332598 scopus 로고
    • The Ca2+-induced membrane transition in mitochondria. III. Transitional Ca2+ release
    • D.R. Hunter, and R.A. Haworth The Ca2+-induced membrane transition in mitochondria. III. Transitional Ca2+ release Arch. Biochem. Biophys. 195 1979 468 477
    • (1979) Arch. Biochem. Biophys. , vol.195 , pp. 468-477
    • Hunter, D.R.1    Haworth, R.A.2
  • 51
    • 0032504717 scopus 로고    scopus 로고
    • From calcium signaling to cell death: Two conformations for the mitochondrial permeability transition pore. Switching from low- to high-conductance state
    • F. Ichas, and J.P. Mazat From calcium signaling to cell death: two conformations for the mitochondrial permeability transition pore. Switching from low- to high-conductance state Biochim. Biophys. Acta 1366 1998 33 50
    • (1998) Biochim. Biophys. Acta , vol.1366 , pp. 33-50
    • Ichas, F.1    Mazat, J.P.2
  • 52
    • 59449085388 scopus 로고    scopus 로고
    • Energy metabolism in heart failure and remodelling
    • J.S. Ingwall Energy metabolism in heart failure and remodelling Cardiovasc. Res. 81 2009 412 419
    • (2009) Cardiovasc. Res. , vol.81 , pp. 412-419
    • Ingwall, J.S.1
  • 53
    • 0025810599 scopus 로고
    • The cell biology of acute myocardial ischemia
    • R.B. Jennings, and K.A. Reimer The cell biology of acute myocardial ischemia Annu. Rev. Med. 42 1991 225 246
    • (1991) Annu. Rev. Med. , vol.42 , pp. 225-246
    • Jennings, R.B.1    Reimer, K.A.2
  • 54
    • 0033616764 scopus 로고    scopus 로고
    • Crystal structure of human p32, a doughnut-shaped acidic mitochondrial matrix protein
    • J. Jiang, Y. Zhang, A.R. Krainer, and R.M. Xu Crystal structure of human p32, a doughnut-shaped acidic mitochondrial matrix protein Proc. Natl. Acad. Sci. USA 96 1999 3572 3577
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 3572-3577
    • Jiang, J.1    Zhang, Y.2    Krainer, A.R.3    Xu, R.M.4
  • 55
    • 70349669093 scopus 로고    scopus 로고
    • Genome-wide RNAi screen identifies Letm1 as a mitochondrial Ca2+/H+ antiporter
    • D. Jiang, L. Zhao, and D.E. Clapham Genome-wide RNAi screen identifies Letm1 as a mitochondrial Ca2+/H+ antiporter Science 326 2009 144 147
    • (2009) Science , vol.326 , pp. 144-147
    • Jiang, D.1    Zhao, L.2    Clapham, D.E.3
  • 56
    • 77649200854 scopus 로고    scopus 로고
    • High-throughput assay to measure oxygen consumption in digitonin-permeabilized cells of patients with mitochondrial disorders
    • A.I. Jonckheere, M. Huigsloot, A.J. Janssen, A.J. Kappen, J.A. Smeitink, and R.J. Rodenburg High-throughput assay to measure oxygen consumption in digitonin-permeabilized cells of patients with mitochondrial disorders Clin. Chem. 56 2010 424 431
    • (2010) Clin. Chem. , vol.56 , pp. 424-431
    • Jonckheere, A.I.1    Huigsloot, M.2    Janssen, A.J.3    Kappen, A.J.4    Smeitink, J.A.5    Rodenburg, R.J.6
  • 60
    • 0024600466 scopus 로고
    • Molecular aspects of the adenine nucleotide carrier from mitochondria
    • M. Klingenberg Molecular aspects of the adenine nucleotide carrier from mitochondria Arch. Biochem. Biophys. 270 1989 1 14
    • (1989) Arch. Biochem. Biophys. , vol.270 , pp. 1-14
    • Klingenberg, M.1
  • 61
    • 52049113898 scopus 로고    scopus 로고
    • The ADP and ATP transport in mitochondria and its carrier
    • M. Klingenberg The ADP and ATP transport in mitochondria and its carrier Biochim. Biophys. Acta 1778 2008 1978 2021
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 1978-2021
    • Klingenberg, M.1
  • 62
    • 0037809232 scopus 로고    scopus 로고
    • Mitochondrial ATP synthasome. Cristae-enriched membranes and a multiwell detergent screening assay yield dispersed single complexes containing the ATP synthase and carriers for Pi and ADP/ATP
    • Y.H. Ko, M. Delannoy, J. Hullihen, W. Chiu, and P.L. Pedersen Mitochondrial ATP synthasome. Cristae-enriched membranes and a multiwell detergent screening assay yield dispersed single complexes containing the ATP synthase and carriers for Pi and ADP/ATP J. Biol. Chem. 278 2003 12305 12309
    • (2003) J. Biol. Chem. , vol.278 , pp. 12305-12309
    • Ko, Y.H.1    Delannoy, M.2    Hullihen, J.3    Chiu, W.4    Pedersen, P.L.5
  • 64
    • 0021136545 scopus 로고
    • Mitochondrial phosphate transport. Large scale isolation and characterization of the phosphate transport protein from beef heart mitochondria
    • H.V. Kolbe, D. Costello, A. Wong, R.C. Lu, and H. Wohlrab Mitochondrial phosphate transport. Large scale isolation and characterization of the phosphate transport protein from beef heart mitochondria J. Biol. Chem. 259 1984 9115 9120
    • (1984) J. Biol. Chem. , vol.259 , pp. 9115-9120
    • Kolbe, H.V.1    Costello, D.2    Wong, A.3    Lu, R.C.4    Wohlrab, H.5
  • 65
    • 80053392175 scopus 로고    scopus 로고
    • Protective role of transient pore openings in calcium handling by cardiac mitochondria
    • P. Korge, L. Yang, J.H. Yang, Y. Wang, Z. Qu, and J.N. Weiss Protective role of transient pore openings in calcium handling by cardiac mitochondria J. Biol. Chem. 286 2011 34851 34857
    • (2011) J. Biol. Chem. , vol.286 , pp. 34851-34857
    • Korge, P.1    Yang, L.2    Yang, J.H.3    Wang, Y.4    Qu, Z.5    Weiss, J.N.6
  • 66
    • 33845977959 scopus 로고    scopus 로고
    • Mitochondrial membrane permeabilization in cell death
    • G. Kroemer, L. Galluzzi, and C. Brenner Mitochondrial membrane permeabilization in cell death Physiol. Rev. 87 2007 99 163
    • (2007) Physiol. Rev. , vol.87 , pp. 99-163
    • Kroemer, G.1    Galluzzi, L.2    Brenner, C.3
  • 67
    • 84905042938 scopus 로고    scopus 로고
    • Genetic deletion of the mitochondrial phosphate carrier desensitizes the mitochondrial permeability transition pore and causes cardiomyopathy
    • J.Q. Kwong, J. Davis, C.P. Baines, M.A. Sargent, J. Karch, X. Wang, T. Huang, and J.D. Molkentin Genetic deletion of the mitochondrial phosphate carrier desensitizes the mitochondrial permeability transition pore and causes cardiomyopathy Cell Death Differ. 21 2014 1209 1217
    • (2014) Cell Death Differ. , vol.21 , pp. 1209-1217
    • Kwong, J.Q.1    Davis, J.2    Baines, C.P.3    Sargent, M.A.4    Karch, J.5    Wang, X.6    Huang, T.7    Molkentin, J.D.8
  • 68
    • 0034960785 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in cardiac disease: Ischemia - Reperfusion, aging, and heart failure
    • E.J. Lesnefsky, S. Moghaddas, B. Tandler, J. Kerner, and C.L. Hoppel Mitochondrial dysfunction in cardiac disease: ischemia - reperfusion, aging, and heart failure J. Mol. Cell. Cardiol. 33 2001 1065 1089
    • (2001) J. Mol. Cell. Cardiol. , vol.33 , pp. 1065-1089
    • Lesnefsky, E.J.1    Moghaddas, S.2    Tandler, B.3    Kerner, J.4    Hoppel, C.L.5
  • 69
    • 55549091082 scopus 로고    scopus 로고
    • The mitochondrial phosphate carrier interacts with cyclophilin D and may play a key role in the permeability transition
    • A.W. Leung, P. Varanyuwatana, and A.P. Halestrap The mitochondrial phosphate carrier interacts with cyclophilin D and may play a key role in the permeability transition J. Biol. Chem. 283 2008 26312 26323
    • (2008) J. Biol. Chem. , vol.283 , pp. 26312-26323
    • Leung, A.W.1    Varanyuwatana, P.2    Halestrap, A.P.3
  • 70
    • 33847341092 scopus 로고    scopus 로고
    • Peripheral benzodiazepine receptor ligand, PK11195 induces mitochondria cytochrome c release and dissipation of mitochondria potential via induction of mitochondria permeability transition
    • J. Li, J. Wang, and Y. Zeng Peripheral benzodiazepine receptor ligand, PK11195 induces mitochondria cytochrome c release and dissipation of mitochondria potential via induction of mitochondria permeability transition Eur. J. Pharmacol. 560 2007 117 122
    • (2007) Eur. J. Pharmacol. , vol.560 , pp. 117-122
    • Li, J.1    Wang, J.2    Zeng, Y.3
  • 71
    • 84863229709 scopus 로고    scopus 로고
    • Superoxide flashes reveal novel properties of mitochondrial reactive oxygen species excitability in cardiomyocytes
    • K. Li, W. Zhang, H. Fang, W. Xie, J. Liu, M. Zheng, X. Wang, W. Wang, W. Tan, and H. Cheng Superoxide flashes reveal novel properties of mitochondrial reactive oxygen species excitability in cardiomyocytes Biophys. J. 102 2012 1011 1021
    • (2012) Biophys. J. , vol.102 , pp. 1011-1021
    • Li, K.1    Zhang, W.2    Fang, H.3    Xie, W.4    Liu, J.5    Zheng, M.6    Wang, X.7    Wang, W.8    Tan, W.9    Cheng, H.10
  • 72
    • 34447507839 scopus 로고    scopus 로고
    • Preconditioning and postconditioning: The essential role of the mitochondrial permeability transition pore
    • S.Y. Lim, S.M. Davidson, D.J. Hausenloy, and D.M. Yellon Preconditioning and postconditioning: the essential role of the mitochondrial permeability transition pore Cardiovasc. Res. 75 2007 530 535
    • (2007) Cardiovasc. Res. , vol.75 , pp. 530-535
    • Lim, S.Y.1    Davidson, S.M.2    Hausenloy, D.J.3    Yellon, D.M.4
  • 74
    • 84883592437 scopus 로고    scopus 로고
    • 2+ handling in heart failure
    • 2+ handling in heart failure Circ. Res. 113 2013 690 708
    • (2013) Circ. Res. , vol.113 , pp. 690-708
    • Luo, M.1    Anderson, M.E.2
  • 75
    • 67649811029 scopus 로고    scopus 로고
    • The mitochondrial permeability transition pore in motor neurons: Involvement in the pathobiology of ALS mice
    • L.J. Martin, B. Gertz, Y. Pan, A.C. Price, J.D. Molkentin, and Q. Chang The mitochondrial permeability transition pore in motor neurons: involvement in the pathobiology of ALS mice Exp. Neurol. 218 2009 333 346
    • (2009) Exp. Neurol. , vol.218 , pp. 333-346
    • Martin, L.J.1    Gertz, B.2    Pan, Y.3    Price, A.C.4    Molkentin, J.D.5    Chang, Q.6
  • 78
    • 0026591024 scopus 로고
    • Isolation of the mitochondrial benzodiazepine receptor: Association with the voltage-dependent anion channel and the adenine nucleotide carrier
    • M.W. McEnery, A.M. Snowman, R.R. Trifiletti, and S.H. Snyder Isolation of the mitochondrial benzodiazepine receptor: association with the voltage-dependent anion channel and the adenine nucleotide carrier Proc. Natl. Acad. Sci. USA 89 1992 3170 3174
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 3170-3174
    • McEnery, M.W.1    Snowman, A.M.2    Trifiletti, R.R.3    Snyder, S.H.4
  • 79
    • 79551482697 scopus 로고    scopus 로고
    • Complement 1q-binding protein inhibits the mitochondrial permeability transition pore and protects against oxidative stress-induced death
    • A.M. McGee, and C.P. Baines Complement 1q-binding protein inhibits the mitochondrial permeability transition pore and protects against oxidative stress-induced death Biochem. J. 433 2011 119 125
    • (2011) Biochem. J. , vol.433 , pp. 119-125
    • McGee, A.M.1    Baines, C.P.2
  • 80
    • 84873119884 scopus 로고    scopus 로고
    • CypD(-/-) hearts have altered levels of proteins involved in Krebs cycle, branch chain amino acid degradation and pyruvate metabolism
    • S. Menazza, R. Wong, T. Nguyen, G. Wang, M. Gucek, and E. Murphy CypD(-/-) hearts have altered levels of proteins involved in Krebs cycle, branch chain amino acid degradation and pyruvate metabolism J. Mol. Cell. Cardiol. 56 2013 81 90
    • (2013) J. Mol. Cell. Cardiol. , vol.56 , pp. 81-90
    • Menazza, S.1    Wong, R.2    Nguyen, T.3    Wang, G.4    Gucek, M.5    Murphy, E.6
  • 83
    • 42049108814 scopus 로고    scopus 로고
    • Mechanisms underlying acute protection from cardiac ischemia-reperfusion injury
    • E. Murphy, and C. Steenbergen Mechanisms underlying acute protection from cardiac ischemia-reperfusion injury Physiol. Rev. 88 2008 581 609
    • (2008) Physiol. Rev. , vol.88 , pp. 581-609
    • Murphy, E.1    Steenbergen, C.2
  • 86
    • 0032422488 scopus 로고    scopus 로고
    • Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria
    • M. Narita, S. Shimizu, T. Ito, T. Chittenden, R.J. Lutz, H. Matsuda, and Y. Tsujimoto Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria Proc. Natl. Acad. Sci. USA 95 1998 14681 14686
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 14681-14686
    • Narita, M.1    Shimizu, S.2    Ito, T.3    Chittenden, T.4    Lutz, R.J.5    Matsuda, H.6    Tsujimoto, Y.7
  • 87
    • 78651386544 scopus 로고    scopus 로고
    • Adenine nucleotide translocase 1 deficiency results in dilated cardiomyopathy with defects in myocardial mechanics, histopathological alterations, and activation of apoptosis
    • N. Narula, M.V. Zaragoza, P.P. Sengupta, P. Li, N. Haider, J. Verjans, K. Waymire, M. Vannan, and D.C. Wallace Adenine nucleotide translocase 1 deficiency results in dilated cardiomyopathy with defects in myocardial mechanics, histopathological alterations, and activation of apoptosis JACC Cardiovasc. Imaging 4 2011 1 10
    • (2011) JACC Cardiovasc. Imaging , vol.4 , pp. 1-10
    • Narula, N.1    Zaragoza, M.V.2    Sengupta, P.P.3    Li, P.4    Haider, N.5    Verjans, J.6    Waymire, K.7    Vannan, M.8    Wallace, D.C.9
  • 88
    • 1242317666 scopus 로고    scopus 로고
    • The mitochondrial transporter family (SLC25): Physiological and pathological implications
    • F. Palmieri The mitochondrial transporter family (SLC25): physiological and pathological implications Pflugers Arch. 447 2004 689 709
    • (2004) Pflugers Arch. , vol.447 , pp. 689-709
    • Palmieri, F.1
  • 91
    • 0027960574 scopus 로고
    • Protoporphyrin IX, an endogenous ligand of the peripheral benzodiazepine receptor, potentiates induction of the mitochondrial permeability transition and the killing of cultured hepatocytes by rotenone
    • J.G. Pastorino, G. Simbula, E. Gilfor, J.B. Hoek, and J.L. Farber Protoporphyrin IX, an endogenous ligand of the peripheral benzodiazepine receptor, potentiates induction of the mitochondrial permeability transition and the killing of cultured hepatocytes by rotenone J. Biol. Chem. 269 1994 31041 31046
    • (1994) J. Biol. Chem. , vol.269 , pp. 31041-31046
    • Pastorino, J.G.1    Simbula, G.2    Gilfor, E.3    Hoek, J.B.4    Farber, J.L.5
  • 93
    • 77958542380 scopus 로고    scopus 로고
    • Superoxide flashes in mouse skeletal muscle are produced by discrete arrays of active mitochondria operating coherently
    • S. Pouvreau Superoxide flashes in mouse skeletal muscle are produced by discrete arrays of active mitochondria operating coherently PLoS ONE 5 2010 5
    • (2010) PLoS ONE , vol.5 , pp. 5
    • Pouvreau, S.1
  • 94
    • 78651285839 scopus 로고    scopus 로고
    • Cyclophilin D deficiency protects against acetaminophen-induced oxidant stress and liver injury
    • A. Ramachandran, M. Lebofsky, C.P. Baines, J.J. Lemasters, and H. Jaeschke Cyclophilin D deficiency protects against acetaminophen-induced oxidant stress and liver injury Free Radic. Res. 45 2011 156 164
    • (2011) Free Radic. Res. , vol.45 , pp. 156-164
    • Ramachandran, A.1    Lebofsky, M.2    Baines, C.P.3    Lemasters, J.J.4    Jaeschke, H.5
  • 95
    • 0032503058 scopus 로고    scopus 로고
    • Reconstituted adenine nucleotide translocase forms a channel for small molecules comparable to the mitochondrial permeability transition pore
    • A. Rück, M. Dolder, T. Wallimann, and D. Brdiczka Reconstituted adenine nucleotide translocase forms a channel for small molecules comparable to the mitochondrial permeability transition pore FEBS Lett. 426 1998 97 101
    • (1998) FEBS Lett. , vol.426 , pp. 97-101
    • Rück, A.1    Dolder, M.2    Wallimann, T.3    Brdiczka, D.4
  • 96
    • 1842333844 scopus 로고    scopus 로고
    • The reversible antiport-uniport conversion of the phosphate carrier from yeast mitochondria depends on the presence of a single cysteine
    • A. Schroers, R. Krämer, and H. Wohlrab The reversible antiport-uniport conversion of the phosphate carrier from yeast mitochondria depends on the presence of a single cysteine J. Biol. Chem. 272 1997 10558 10564
    • (1997) J. Biol. Chem. , vol.272 , pp. 10558-10564
    • Schroers, A.1    Krämer, R.2    Wohlrab, H.3
  • 99
    • 84901008605 scopus 로고    scopus 로고
    • Regulation of the mitochondrial permeability transition pore by the outer membrane does not involve the peripheral benzodiazepine receptor (Translocator Protein of 18 kDa (TSPO))
    • J. Šileikytė, E. Blachly-Dyson, R. Sewell, A. Carpi, R. Menabò, F. Di Lisa, F. Ricchelli, P. Bernardi, and M. Forte Regulation of the mitochondrial permeability transition pore by the outer membrane does not involve the peripheral benzodiazepine receptor (Translocator Protein of 18 kDa (TSPO)) J. Biol. Chem. 289 2014 13769 13781
    • (2014) J. Biol. Chem. , vol.289 , pp. 13769-13781
    • Šileikyte, J.1    Blachly-Dyson, E.2    Sewell, R.3    Carpi, A.4    Menabò, R.5    Di Lisa, F.6    Ricchelli, F.7    Bernardi, P.8    Forte, M.9
  • 101
    • 77956322223 scopus 로고    scopus 로고
    • The molecular identity of the mitochondrial Ca2+ sequestration system
    • A.A. Starkov The molecular identity of the mitochondrial Ca2+ sequestration system FEBS J. 277 2010 3652 3663
    • (2010) FEBS J. , vol.277 , pp. 3652-3663
    • Starkov, A.A.1
  • 102
    • 0026550587 scopus 로고
    • The mitochondrial megachannel is the permeability transition pore
    • I. Szabó, and M. Zoratti The mitochondrial megachannel is the permeability transition pore J. Bioenerg. Biomembr. 24 1992 111 117
    • (1992) J. Bioenerg. Biomembr. , vol.24 , pp. 111-117
    • Szabó, I.1    Zoratti, M.2
  • 103
    • 0027234336 scopus 로고
    • The mitochondrial permeability transition pore may comprise VDAC molecules. I. Binary structure and voltage dependence of the pore
    • I. Szabó, 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
    • (1993) FEBS Lett. , vol.330 , pp. 201-205
    • Szabó, I.1    Zoratti, M.2
  • 104
    • 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
    • I. Szabó, V. De Pinto, and M. Zoratti 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. 330 1993 206 210
    • (1993) FEBS Lett. , vol.330 , pp. 206-210
    • Szabó, I.1    De Pinto, V.2    Zoratti, M.3
  • 105
    • 77956095537 scopus 로고    scopus 로고
    • Mitochondria and cell death: Outer membrane permeabilization and beyond
    • S.W. Tait, and D.R. Green Mitochondria and cell death: outer membrane permeabilization and beyond Nat. Rev. Mol. Cell Biol. 11 2010 621 632
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 621-632
    • Tait, S.W.1    Green, D.R.2
  • 106
    • 0027244336 scopus 로고
    • The mitochondrial DNA mutation at 8993 associated with NARP slows the rate of ATP synthesis in isolated lymphoblast mitochondria
    • Y. Tatuch, and B.H. Robinson The mitochondrial DNA mutation at 8993 associated with NARP slows the rate of ATP synthesis in isolated lymphoblast mitochondria Biochem. Biophys. Res. Commun. 192 1993 124 128
    • (1993) Biochem. Biophys. Res. Commun. , vol.192 , pp. 124-128
    • Tatuch, Y.1    Robinson, B.H.2
  • 107
    • 84891378488 scopus 로고    scopus 로고
    • Functional reconstitution of the mitochondrial Ca2+/H+ antiporter Letm1
    • M.F. Tsai, D. Jiang, L. Zhao, D. Clapham, and C. Miller Functional reconstitution of the mitochondrial Ca2+/H+ antiporter Letm1 J. Gen. Physiol. 143 2014 67 73
    • (2014) J. Gen. Physiol. , vol.143 , pp. 67-73
    • Tsai, M.F.1    Jiang, D.2    Zhao, L.3    Clapham, D.4    Miller, C.5
  • 109
    • 84856526180 scopus 로고    scopus 로고
    • The roles of phosphate and the phosphate carrier in the mitochondrial permeability transition pore
    • P. Varanyuwatana, and A.P. Halestrap The roles of phosphate and the phosphate carrier in the mitochondrial permeability transition pore Mitochondrion 12 2012 120 125
    • (2012) Mitochondrion , vol.12 , pp. 120-125
    • Varanyuwatana, P.1    Halestrap, A.P.2
  • 113
  • 115
    • 77957752614 scopus 로고    scopus 로고
    • Debio-025 is more effective than prednisone in reducing muscular pathology in mdx mice
    • E.R. Wissing, D.P. Millay, G. Vuagniaux, and J.D. Molkentin Debio-025 is more effective than prednisone in reducing muscular pathology in mdx mice Neuromuscul. Disord. 20 2010 753 760
    • (2010) Neuromuscul. Disord. , vol.20 , pp. 753-760
    • Wissing, E.R.1    Millay, D.P.2    Vuagniaux, G.3    Molkentin, J.D.4
  • 116
    • 0032387842 scopus 로고    scopus 로고
    • Direct demonstration of a specific interaction between cyclophilin-D and the adenine nucleotide translocase confirms their role in the mitochondrial permeability transition
    • K. Woodfield, A. Rück, D. Brdiczka, and A.P. Halestrap Direct demonstration of a specific interaction between cyclophilin-D and the adenine nucleotide translocase confirms their role in the mitochondrial permeability transition Biochem. J. 336 1998 287 290
    • (1998) Biochem. J. , vol.336 , pp. 287-290
    • Woodfield, K.1    Rück, A.2    Brdiczka, D.3    Halestrap, A.P.4
  • 117
    • 0034596947 scopus 로고    scopus 로고
    • Reactive oxygen species (ROS)-induced ROS release: A new phenomenon accompanying induction of the mitochondrial permeability transition in cardiac myocytes
    • D.B. Zorov, C.R. Filburn, L.O. Klotz, J.L. Zweier, and S.J. Sollott Reactive oxygen species (ROS)-induced ROS release: a new phenomenon accompanying induction of the mitochondrial permeability transition in cardiac myocytes J. Exp. Med. 192 2000 1001 1014
    • (2000) J. Exp. Med. , vol.192 , pp. 1001-1014
    • Zorov, D.B.1    Filburn, C.R.2    Klotz, L.O.3    Zweier, J.L.4    Sollott, S.J.5


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