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Volumn 42, Issue 3, 2011, Pages 381-390

Repetitive nerve stimulation transiently opens the mitochondrial permeability transition pore in motor nerve terminals of symptomatic mutant SOD1 mice

Author keywords

Mitochondria; Mitochondrial calcium uptake; Mitochondrial membrane potential; Mitochondrial permeability transition pore; Motor nerve terminal; Motor neuron; Mouse models of familial amyotrophic lateral sclerosis; Oxidative stress; Superoxide dismutase 1 G85R; Superoxide dismutase 1 G93A

Indexed keywords

CALCIUM ION; COPPER ZINC SUPEROXIDE DISMUTASE; MITOCHONDRIAL PERMEABILITY TRANSITION PORE;

EID: 79954631234     PISSN: 09699961     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.nbd.2011.01.031     Document Type: Article
Times cited : (14)

References (73)
  • 1
    • 0023580310 scopus 로고
    • The levator auris longus muscle of the mouse: a convenient preparation for studies of short- and long-term presynaptic effects of drugs or toxins
    • Angaut-Petit D., Molgo J., Connold A.L., Faille L. The levator auris longus muscle of the mouse: a convenient preparation for studies of short- and long-term presynaptic effects of drugs or toxins. Neurosci. Lett. 1987, 82:83-88.
    • (1987) Neurosci. Lett. , vol.82 , pp. 83-88
    • Angaut-Petit, D.1    Molgo, J.2    Connold, A.L.3    Faille, L.4
  • 2
    • 75149155060 scopus 로고    scopus 로고
    • Oxidative stress in ALS: key role in motor neuron injury and therapeutic target
    • Barber S.C., Shaw P.J. Oxidative stress in ALS: key role in motor neuron injury and therapeutic target. Free Radic. Biol. Med. 2010, 48:629-641.
    • (2010) Free Radic. Biol. Med. , vol.48 , pp. 629-641
    • Barber, S.C.1    Shaw, P.J.2
  • 3
    • 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
  • 4
    • 77958519939 scopus 로고    scopus 로고
    • Wild-type and mutant SOD1 share an aberrant conformation and a common pathogenic pathway in ALS
    • Bosco D.A., Morfini G., Karabacak N.M., Song Y., Gros-Louis F., Pasinelli P., et al. Wild-type and mutant SOD1 share an aberrant conformation and a common pathogenic pathway in ALS. Nat. Neurosci. 2010, 13:1396-1403.
    • (2010) Nat. Neurosci. , vol.13 , pp. 1396-1403
    • Bosco, D.A.1    Morfini, G.2    Karabacak, N.M.3    Song, Y.4    Gros-Louis, F.5    Pasinelli, P.6
  • 5
    • 33744964144 scopus 로고    scopus 로고
    • Synaptic mitochondria are more susceptible to Ca2+ overload than nonsynaptic mitochondria
    • Brown M.R., Sullivan P.G., Geddes J.W. Synaptic mitochondria are more susceptible to Ca2+ overload than nonsynaptic mitochondria. J. Biol. Chem. 2006, 281:11658-11668.
    • (2006) J. Biol. Chem. , vol.281 , pp. 11658-11668
    • Brown, M.R.1    Sullivan, P.G.2    Geddes, J.W.3
  • 6
    • 0031051485 scopus 로고    scopus 로고
    • ALS-linked SOD1 mutant G85R mediates damage to astrocytes and promotes rapidly progressive disease with SOD1-containing inclusions
    • Bruijn L.I., Becher M.W., Lee M.K., Anderson K.L., Jemkins N.A., Copeland N.G., et al. ALS-linked SOD1 mutant G85R mediates damage to astrocytes and promotes rapidly progressive disease with SOD1-containing inclusions. Neuron 1997, 18:327-338.
    • (1997) Neuron , vol.18 , pp. 327-338
    • Bruijn, L.I.1    Becher, M.W.2    Lee, M.K.3    Anderson, K.L.4    Jemkins, N.A.5    Copeland, N.G.6
  • 7
    • 39449130570 scopus 로고    scopus 로고
    • The mitochondrial membrane potential and Ca2+ oscillations in smooth muscle
    • Chalmers S., McCarron J.G. The mitochondrial membrane potential and Ca2+ oscillations in smooth muscle. J. Cell Sci. 2008, 121:75-85.
    • (2008) J. Cell Sci. , vol.121 , pp. 75-85
    • Chalmers, S.1    McCarron, J.G.2
  • 8
    • 0029096114 scopus 로고
    • Age-dependent penetrance of disease in a transgenic mouse model of familial amyotrophic lateral sclerosis
    • Chiu A.Y., Zhai P., Dal Canto M.C., Peters T.M., Kwon Y.W., Prattis S.M., et al. Age-dependent penetrance of disease in a transgenic mouse model of familial amyotrophic lateral sclerosis. Mol. Cell. Neurosci. 1995, 6:349-362.
    • (1995) Mol. Cell. Neurosci. , vol.6 , pp. 349-362
    • Chiu, A.Y.1    Zhai, P.2    Dal Canto, M.C.3    Peters, T.M.4    Kwon, Y.W.5    Prattis, S.M.6
  • 9
    • 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.A., Larochette N., de Pablo M.A., Zamzami N., et al. Oxidation of a critical thiol residue of the adenine nucleotide translocator enforces Bcl-2-independent permeability transition pore opening and apoptosis. Oncogene 2000, 19:307-314.
    • (2000) Oncogene , vol.19 , pp. 307-314
    • Costantini, P.1    Belzacq, A.S.2    Vieira, H.L.A.3    Larochette, N.4    de Pablo, M.A.5    Zamzami, N.6
  • 10
    • 33645102302 scopus 로고    scopus 로고
    • Neural mitochondrial Ca2+ capacity impairment precedes the onset of motor symptoms in G93A Cu/Zn-superoxide dismutase mutant mice
    • Damiano M., Starkov A.A., Petri S., Kipiani K., Kiaei M., Mattiazzi M., et al. Neural mitochondrial Ca2+ capacity impairment precedes the onset of motor symptoms in G93A Cu/Zn-superoxide dismutase mutant mice. J. Neurochem. 2006, 96:1349-1361.
    • (2006) J. Neurochem. , vol.96 , pp. 1349-1361
    • Damiano, M.1    Starkov, A.A.2    Petri, S.3    Kipiani, K.4    Kiaei, M.5    Mattiazzi, M.6
  • 11
    • 0033198196 scopus 로고    scopus 로고
    • Mitochondrial clearance of cytosolic Ca2+ in stimulated lizard motor nerve terminals proceeds without progressive elevation of mitochondrial matrix [Ca2+]
    • David G. Mitochondrial clearance of cytosolic Ca2+ in stimulated lizard motor nerve terminals proceeds without progressive elevation of mitochondrial matrix [Ca2+]. J. Neurosci. 1999, 19:7495-7506.
    • (1999) J. Neurosci. , vol.19 , pp. 7495-7506
    • David, G.1
  • 12
    • 0038414654 scopus 로고    scopus 로고
    • Mitochondrial Ca2+ uptake prevents desynchronization of quantal release and minimizes depletion during repetitive stimulation of mouse motor nerve terminals
    • David G., Barrett E.F. Mitochondrial Ca2+ uptake prevents desynchronization of quantal release and minimizes depletion during repetitive stimulation of mouse motor nerve terminals. J. Physiol. Lond. 2003, 548:425-438.
    • (2003) J. Physiol. Lond. , vol.548 , pp. 425-438
    • David, G.1    Barrett, E.F.2
  • 13
    • 0028819829 scopus 로고
    • Electrical and morphological factors influencing the depolarizing after-potential in rat and lizard myelinated axons
    • David G., Modney B., Scappaticci K.A., Barrett J.N., Barrett E.F. Electrical and morphological factors influencing the depolarizing after-potential in rat and lizard myelinated axons. J. Physiol. 1995, 489:141-157.
    • (1995) J. Physiol. , vol.489 , pp. 141-157
    • David, G.1    Modney, B.2    Scappaticci, K.A.3    Barrett, J.N.4    Barrett, E.F.5
  • 14
    • 0032523758 scopus 로고    scopus 로고
    • Evidence that mitochondria buffer physiological Ca2+ loads in lizard motor nerve terminals
    • David G., Barrett J.N., Barrett E.F. Evidence that mitochondria buffer physiological Ca2+ loads in lizard motor nerve terminals. J. Physiol. Lond. 1998, 509:59-65.
    • (1998) J. Physiol. Lond. , vol.509 , pp. 59-65
    • David, G.1    Barrett, J.N.2    Barrett, E.F.3
  • 15
    • 0343819890 scopus 로고    scopus 로고
    • Fiber types in the mouse levator auris longus muscle: a convenient preparation to study muscle and nerve plasticity
    • Erzen I., Cvetko E., Obreza S., Angaut-Petit D. Fiber types in the mouse levator auris longus muscle: a convenient preparation to study muscle and nerve plasticity. J. Neurosci. Res. 2000, 59:692-697.
    • (2000) J. Neurosci. Res. , vol.59 , pp. 692-697
    • Erzen, I.1    Cvetko, E.2    Obreza, S.3    Angaut-Petit, D.4
  • 16
    • 34250177650 scopus 로고    scopus 로고
    • Wild-type superoxide dismutase acquires binding and toxic properties of ALS-linked mutant forms through oxidation
    • Ezzi S.A., Urushitani M., Julien J.P. Wild-type superoxide dismutase acquires binding and toxic properties of ALS-linked mutant forms through oxidation. J. Neurochem. 2007, 102:170-178.
    • (2007) J. Neurochem. , vol.102 , pp. 170-178
    • Ezzi, S.A.1    Urushitani, M.2    Julien, J.P.3
  • 19
    • 0032055923 scopus 로고    scopus 로고
    • Inactivation of presynaptic calcium current contributes to synaptic depression at a fast central synapse
    • Forsythe I.D., Tsujimoto T., Barnes-Davies M., Cuttle M.F., Takahashi T. Inactivation of presynaptic calcium current contributes to synaptic depression at a fast central synapse. Neuron 1998, 20:797-807.
    • (1998) Neuron , vol.20 , pp. 797-807
    • Forsythe, I.D.1    Tsujimoto, T.2    Barnes-Davies, M.3    Cuttle, M.F.4    Takahashi, T.5
  • 20
    • 0034175513 scopus 로고    scopus 로고
    • Early and selective loss of neuromuscular synapse subtypes with low sprouting competence in motoneuron diseases
    • Frey D., Schneider C., Xu L., Borg J., Spooren W., Caroni P. Early and selective loss of neuromuscular synapse subtypes with low sprouting competence in motoneuron diseases. J. Neurosci. 2000, 20:2534-2542.
    • (2000) J. Neurosci. , vol.20 , pp. 2534-2542
    • Frey, D.1    Schneider, C.2    Xu, L.3    Borg, J.4    Spooren, W.5    Caroni, P.6
  • 21
    • 69049098806 scopus 로고    scopus 로고
    • Structural and functional link between the mitochondrial network and the endoplasmic reticulum
    • Giorgi C., De Stefani D., Bononi A., Rizzuto R., Pinton P. Structural and functional link between the mitochondrial network and the endoplasmic reticulum. Int. J. Biochem. Cell Biol. 2009, 41:1817-1827.
    • (2009) Int. J. Biochem. Cell Biol. , vol.41 , pp. 1817-1827
    • Giorgi, C.1    De Stefani, D.2    Bononi, A.3    Rizzuto, R.4    Pinton, P.5
  • 22
    • 0025292743 scopus 로고
    • Mechanisms by which mitochondria transport calcium
    • Gunter T.E., Pfeiffer D.R. 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
  • 23
    • 0028284779 scopus 로고
    • Motor neuron degeneration in mice that express a human Cu/Zn superoxide dismutase mutation
    • Gurney M.E., Pu H., Chiu A.Y., Dal Canto M.C., Polchow C.Y., Alexander D.D., et al. Motor neuron degeneration in mice that express a human Cu/Zn superoxide dismutase mutation. Science 1994, 264:1772-1775.
    • (1994) Science , vol.264 , pp. 1772-1775
    • Gurney, M.E.1    Pu, H.2    Chiu, A.Y.3    Dal Canto, M.C.4    Polchow, C.Y.5    Alexander, D.D.6
  • 24
    • 38849182472 scopus 로고    scopus 로고
    • SOD1 mutations disrupt redox-sensitive Rac regulation of NADPH oxidase in a familial ALS model
    • Harraz M.M., Marden J.J., Zhou W., Zhang Y., Williams A., Sharov V.S. SOD1 mutations disrupt redox-sensitive Rac regulation of NADPH oxidase in a familial ALS model. J. Clin. Invest. 2008, 118:659-670.
    • (2008) J. Clin. Invest. , vol.118 , pp. 659-670
    • Harraz, M.M.1    Marden, J.J.2    Zhou, W.3    Zhang, Y.4    Williams, A.5    Sharov, V.S.6
  • 25
    • 48949120504 scopus 로고    scopus 로고
    • Preferential motor unit loss in the SOD1G93A transgenic mouse model of amyotrophic lateral sclerosis
    • Hegedus J., Putman C.T., Tyreman N., Gordon T. Preferential motor unit loss in the SOD1G93A transgenic mouse model of amyotrophic lateral sclerosis. J. Physiol. Lond. 2008, 586:3337-3351.
    • (2008) J. Physiol. Lond. , vol.586 , pp. 3337-3351
    • Hegedus, J.1    Putman, C.T.2    Tyreman, N.3    Gordon, T.4
  • 26
    • 73249150574 scopus 로고    scopus 로고
    • Regulation of vascular smooth muscle cell bioenergetic function by protein glutathiolation
    • Hill B.G., Higdon A.N., Dranka B.P., Darley-Usmar V.M. Regulation of vascular smooth muscle cell bioenergetic function by protein glutathiolation. Biochim. Biophys. Acta 2010, 1797:285-295.
    • (2010) Biochim. Biophys. Acta , vol.1797 , pp. 285-295
    • Hill, B.G.1    Higdon, A.N.2    Dranka, B.P.3    Darley-Usmar, V.M.4
  • 27
    • 0037745119 scopus 로고    scopus 로고
    • Fluctuations in mitochondrial membrane potential caused by repetitive gating of the permeability transition pore
    • Hϋser J., Blatter L.A. Fluctuations in mitochondrial membrane potential caused by repetitive gating of the permeability transition pore. Biochem. J. 1999, 343:311-317.
    • (1999) Biochem. J. , vol.343 , pp. 311-317
    • Hϋser, J.1    Blatter, L.A.2
  • 28
    • 0038421272 scopus 로고    scopus 로고
    • Imaging the permeability pore transition in single mitochondria
    • Hϋser J., Rechenmacher C.E., Blatter L.A. Imaging the permeability pore transition in single mitochondria. Biophys. J. 1998, 74:2129-2137.
    • (1998) Biophys. J. , vol.74 , pp. 2129-2137
    • Hϋser, J.1    Rechenmacher, C.E.2    Blatter, L.A.3
  • 29
    • 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
    • Ichas F., Mazat J.P. From calcium signaling to cell death: two conformations for the mitochondrial permeability transition pore. Switching from low- to high-conductance state. Biochim. Biophys. Acta 1998, 1366:33-50.
    • (1998) Biochim. Biophys. Acta , vol.1366 , pp. 33-50
    • Ichas, F.1    Mazat, J.P.2
  • 31
    • 0034714346 scopus 로고    scopus 로고
    • Glutathione depletion in PC12 results in selective inhibition of mitochondrial complex I activity. Implications for Parkinson's disease
    • Jha N., Jurma O., Lalli G., Liu Y., Pettus E.H., Greenamyre J.T., et al. Glutathione depletion in PC12 results in selective inhibition of mitochondrial complex I activity. Implications for Parkinson's disease. J. Biol. Chem. 2000, 275:26096-26101.
    • (2000) J. Biol. Chem. , vol.275 , pp. 26096-26101
    • Jha, N.1    Jurma, O.2    Lalli, G.3    Liu, Y.4    Pettus, E.H.5    Greenamyre, J.T.6
  • 32
    • 70349669093 scopus 로고    scopus 로고
    • Genome-wide RNAi screen identifies Letm1 as a mitochondrial Ca2+/H+ antiporter
    • Jiang D., Zhao L., Clapham D.E. Genome-wide RNAi screen identifies Letm1 as a mitochondrial Ca2+/H+ antiporter. Science 2009, 326:144-147.
    • (2009) Science , vol.326 , pp. 144-147
    • Jiang, D.1    Zhao, L.2    Clapham, D.E.3
  • 33
    • 34249781383 scopus 로고    scopus 로고
    • 'Mild uncoupling' does not decrease mitochondrial superoxide levels in cultured cerebellar granule neurons but decreases spare respiratory capacity and increases toxicity to glutamate and oxidative stress
    • Johnson-Cadwell L.I., Jekabsons M.B., Wang A., Polster B.M., Nicholls D.G. 'Mild uncoupling' does not decrease mitochondrial superoxide levels in cultured cerebellar granule neurons but decreases spare respiratory capacity and increases toxicity to glutamate and oxidative stress. J. Neurochem. 2007, 101:1619-1631.
    • (2007) J. Neurochem. , vol.101 , pp. 1619-1631
    • Johnson-Cadwell, L.I.1    Jekabsons, M.B.2    Wang, A.3    Polster, B.M.4    Nicholls, D.G.5
  • 34
    • 37849007550 scopus 로고    scopus 로고
    • Oxidized/misfolded superoxide dismutase-1: the cause of all amyotrophic lateral sclerosis?
    • Kabashi E., Valdmanis P.N., Dion P., Rouleau G.A. Oxidized/misfolded superoxide dismutase-1: the cause of all amyotrophic lateral sclerosis?. Ann. Neurol. 2007, 62:553-559.
    • (2007) Ann. Neurol. , vol.62 , pp. 553-559
    • Kabashi, E.1    Valdmanis, P.N.2    Dion, P.3    Rouleau, G.A.4
  • 35
    • 3042511616 scopus 로고    scopus 로고
    • Life span extension and reduced neuronal death after weekly intraventricular cyclosporin injections in the G93A transgenic mouse model of amyotrophic lateral sclerosis
    • Karlsson J., Fong K.S., Hansson M.J., Elmer E., Csiszar K., Keep M.F. Life span extension and reduced neuronal death after weekly intraventricular cyclosporin injections in the G93A transgenic mouse model of amyotrophic lateral sclerosis. J. Neurosurg. 2004, 101:128-137.
    • (2004) J. Neurosurg. , vol.101 , pp. 128-137
    • Karlsson, J.1    Fong, K.S.2    Hansson, M.J.3    Elmer, E.4    Csiszar, K.5    Keep, M.F.6
  • 36
    • 77956183828 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and intracellular calcium dysregulation in ALS
    • Kawamata, H., Manfredi, G., 2010. Mitochondrial dysfunction and intracellular calcium dysregulation in ALS. Mech. Ageing Dev. 131, 517-526.
    • (2010) Mech. Ageing Dev. , vol.131 , pp. 517-526
    • Kawamata, H.1    Manfredi, G.2
  • 37
    • 1642540210 scopus 로고    scopus 로고
    • The mitochondrial calcium uniporter is a highly selective ion channel
    • Kirichok Y., Krapivinsky G., Clapham D.E. The mitochondrial calcium uniporter is a highly selective ion channel. Nature 2004, 427:360-364.
    • (2004) Nature , vol.427 , pp. 360-364
    • Kirichok, Y.1    Krapivinsky, G.2    Clapham, D.E.3
  • 38
    • 1042289650 scopus 로고    scopus 로고
    • An ALS mouse model with a permeable blood-brain barrier benefits from systemic cyclosporine A treatment
    • Kirkinezos I.G., Hernandez D., Bradley W.G., Moraes C.T. An ALS mouse model with a permeable blood-brain barrier benefits from systemic cyclosporine A treatment. J. Neurochem. 2004, 88:821-826.
    • (2004) J. Neurochem. , vol.88 , pp. 821-826
    • Kirkinezos, I.G.1    Hernandez, D.2    Bradley, W.G.3    Moraes, C.T.4
  • 39
    • 12144257165 scopus 로고    scopus 로고
    • Cytochrome c association with the inner mitochondrial membrane is impaired in the CNS of G93A-SOD1 mice
    • Kirkinezos I.G., Bacman S.R., Hernandez D., Oca-Cossio J., Arias L.J., Perez-Pinzon M.A., et al. Cytochrome c association with the inner mitochondrial membrane is impaired in the CNS of G93A-SOD1 mice. J. Neurosci. 2005, 25:164-172.
    • (2005) J. Neurosci. , vol.25 , pp. 164-172
    • Kirkinezos, I.G.1    Bacman, S.R.2    Hernandez, D.3    Oca-Cossio, J.4    Arias, L.J.5    Perez-Pinzon, M.A.6
  • 40
    • 0032079517 scopus 로고    scopus 로고
    • Massive mitochondrial degeneration in motor neurons triggers the onset of amyotrophic lateral sclerosis in mice expressing a mutant SOD1
    • Kong J., Xu Z. Massive mitochondrial degeneration in motor neurons triggers the onset of amyotrophic lateral sclerosis in mice expressing a mutant SOD1. J. Neurosci. 1998, 18:3241-3250.
    • (1998) J. Neurosci. , vol.18 , pp. 3241-3250
    • Kong, J.1    Xu, Z.2
  • 41
    • 0034655601 scopus 로고    scopus 로고
    • Prooxidants open both the mitochondrial permeability transition pore and a low-conductance channel in the inner mitochondrial membrane
    • Kushnareva Y.E., Sokolove P.M. Prooxidants open both the mitochondrial permeability transition pore and a low-conductance channel in the inner mitochondrial membrane. Arch. Biochem. Biophys. 2000, 376:377-388.
    • (2000) Arch. Biochem. Biophys. , vol.376 , pp. 377-388
    • Kushnareva, Y.E.1    Sokolove, P.M.2
  • 43
    • 0025893168 scopus 로고
    • Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes
    • Liu J., Farmer J.D., Lane W.S., Friedman J., Weissman I., Schreiber S.L. Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes. Cell 1991, 66:807-815.
    • (1991) Cell , vol.66 , pp. 807-815
    • Liu, J.1    Farmer, J.D.2    Lane, W.S.3    Friedman, J.4    Weissman, I.5    Schreiber, S.L.6
  • 45
    • 71849092300 scopus 로고    scopus 로고
    • The mitochondrial permeability transition pore: a molecular target for amyotrophic lateral sclerosis therapy
    • Martin L.J. The mitochondrial permeability transition pore: a molecular target for amyotrophic lateral sclerosis therapy. Biochim. Biophys. Acta 2010, 1802:186-197.
    • (2010) Biochim. Biophys. Acta , vol.1802 , pp. 186-197
    • Martin, L.J.1
  • 46
    • 67649811029 scopus 로고    scopus 로고
    • The mitochondrial permeability transition pore in motor neurons: involvement in the pathobiology of ALS mice
    • Martin L.J., Gertz B., Pan Y., Price A.C., Molkentin J.D., Chang Q. The mitochondrial permeability transition pore in motor neurons: involvement in the pathobiology of ALS mice. Exp. Neurol. 2009, 218:333-346.
    • (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
  • 47
    • 0037119407 scopus 로고    scopus 로고
    • Mutated human SOD1 causes dysfunction of oxidative phosphorylation in mitochondria of transgenic mice
    • Mattiazzi M., D'Aurelio M., Gajewski C.D., Martushova K., Kiaei M., Beal M.F., et al. Mutated human SOD1 causes dysfunction of oxidative phosphorylation in mitochondria of transgenic mice. J. Biol. Chem. 2002, 277:29626-29633.
    • (2002) J. Biol. Chem. , vol.277 , pp. 29626-29633
    • Mattiazzi, M.1    D'Aurelio, M.2    Gajewski, C.D.3    Martushova, K.4    Kiaei, M.5    Beal, M.F.6
  • 48
    • 0037109064 scopus 로고    scopus 로고
    • Role of critical thiol groups on the matrix surface of the adenine nucleotide translocase in the mechanism of the mitochondrial permeability transition pore
    • McStay G.P., Clarke S.J., Halestrap A.P. Role of critical thiol groups on the matrix surface of the adenine nucleotide translocase in the mechanism of the mitochondrial permeability transition pore. Biochem. J. 2002, 367:541-548.
    • (2002) Biochem. J. , vol.367 , pp. 541-548
    • McStay, G.P.1    Clarke, S.J.2    Halestrap, A.P.3
  • 49
    • 0025469547 scopus 로고
    • Evidence for two calcium-dependent potassium conductances in lizard motor nerve terminals
    • Morita K., Barrett E.F. Evidence for two calcium-dependent potassium conductances in lizard motor nerve terminals. J. Neurosci. 1990, 10:2614-2625.
    • (1990) J. Neurosci. , vol.10 , pp. 2614-2625
    • Morita, K.1    Barrett, E.F.2
  • 50
    • 77949909934 scopus 로고    scopus 로고
    • Review: neuromuscular synaptic vulnerability in motor neurone disease: amyotrophic lateral sclerosis and spinal muscular atrophy
    • Murray L.M., Talbot K., Gillingwater T.H. Review: neuromuscular synaptic vulnerability in motor neurone disease: amyotrophic lateral sclerosis and spinal muscular atrophy. Neuropathol. Appl. Neurobiol. 2010, 36:133-156.
    • (2010) Neuropathol. Appl. Neurobiol. , vol.36 , pp. 133-156
    • Murray, L.M.1    Talbot, K.2    Gillingwater, T.H.3
  • 51
    • 34447498864 scopus 로고    scopus 로고
    • High cyclophilin D content of synaptic mitochondria results in increased vulnerability to permeability transition
    • Naga K.K., Sullivan P.G., Geddes J.W. High cyclophilin D content of synaptic mitochondria results in increased vulnerability to permeability transition. J. Neurosci. 2007, 27:7469-7475.
    • (2007) J. Neurosci. , vol.27 , pp. 7469-7475
    • Naga, K.K.1    Sullivan, P.G.2    Geddes, J.W.3
  • 52
    • 60549090787 scopus 로고    scopus 로고
    • The Ψm depolarization that accompanies mitochondrial Ca2+ uptake is greater in mutant SOD1 than in wild-type mouse motor terminals
    • Nguyen K.T., García-Chacón L.E., Barrett J.N., Barrett E.F., David G. The Ψm depolarization that accompanies mitochondrial Ca2+ uptake is greater in mutant SOD1 than in wild-type mouse motor terminals. Proc. Natl Acad. Sci. USA 2009, 106:2007-2011.
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 2007-2011
    • Nguyen, K.T.1    García-Chacón, L.E.2    Barrett, J.N.3    Barrett, E.F.4    David, G.5
  • 53
    • 10244257617 scopus 로고    scopus 로고
    • The integration of mitochondrial calcium transport and storage
    • Nicholls D.G., Chalmers S. The integration of mitochondrial calcium transport and storage. J. Bioenerg. Biomembr. 2004, 36:277-281.
    • (2004) J. Bioenerg. Biomembr. , vol.36 , pp. 277-281
    • Nicholls, D.G.1    Chalmers, S.2
  • 55
    • 0034176843 scopus 로고    scopus 로고
    • Mitochondrial membrane potential and neuronal glutamate excitotoxicity: mortality and millivolts
    • Nicholls D.G., Ward M.W. Mitochondrial membrane potential and neuronal glutamate excitotoxicity: mortality and millivolts. Trends Neurosci. 2000, 23:166-174.
    • (2000) Trends Neurosci. , vol.23 , pp. 166-174
    • Nicholls, D.G.1    Ward, M.W.2
  • 57
    • 79954629145 scopus 로고    scopus 로고
    • Increasing mitochondrial calcium buffering capacity systemically in mice expressing ALS-linked mutations does not alter disease course
    • Society for Neuroscience, San Diego, CA, Online
    • Parone P.A., Da Cruz S., Garcia M.L., Forte M.A., Bernardi P., Cleveland D.W. Increasing mitochondrial calcium buffering capacity systemically in mice expressing ALS-linked mutations does not alter disease course. Program No. 656/13/N7. 2010 Neuroscience Meeting Planner 2010, Society for Neuroscience, San Diego, CA, Online.
    • (2010) Program No. 656/13/N7. 2010 Neuroscience Meeting Planner
    • Parone, P.A.1    Da Cruz, S.2    Garcia, M.L.3    Forte, M.A.4    Bernardi, P.5    Cleveland, D.W.6
  • 59
    • 33344462702 scopus 로고    scopus 로고
    • Selective vulnerability and pruning of phasic motoneuron axons in motoneuron disease alleviated by CNTF
    • Pun S., Santos A.F., Saxena S., Xu L., Caroni P. Selective vulnerability and pruning of phasic motoneuron axons in motoneuron disease alleviated by CNTF. Nat. Neurosci. 2006, 9:408-419.
    • (2006) Nat. Neurosci. , vol.9 , pp. 408-419
    • Pun, S.1    Santos, A.F.2    Saxena, S.3    Xu, L.4    Caroni, P.5
  • 60
    • 0027401203 scopus 로고
    • Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis
    • Rosen D.R., Siddique T., Patterson D.A., Figlewicz P., Sapp A., Hentati D., et al. Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature 1993, 362:59-62.
    • (1993) Nature , vol.362 , pp. 59-62
    • Rosen, D.R.1    Siddique, T.2    Patterson, D.A.3    Figlewicz, P.4    Sapp, A.5    Hentati, D.6
  • 61
    • 66249144695 scopus 로고    scopus 로고
    • Transient opening of mitochondrial permeability transition pore by reactive oxygen species protects myocardium from ischemia-reperfusion injury
    • Saotome M., Katoh H., Yaguchi Y., Tanaka T., Urushida T., Satoh H., et al. Transient opening of mitochondrial permeability transition pore by reactive oxygen species protects myocardium from ischemia-reperfusion injury. Am. J. Physiol. Heart Circ. Physiol. 2009, 296:H1125-H1132.
    • (2009) Am. J. Physiol. Heart Circ. Physiol. , vol.296
    • Saotome, M.1    Katoh, H.2    Yaguchi, Y.3    Tanaka, T.4    Urushida, T.5    Satoh, H.6
  • 62
    • 23744445580 scopus 로고    scopus 로고
    • A compensatory subpopulation of motor neurons in a mouse model of amyotrophic lateral sclerosis
    • Schaefer A.M., Sanes J.R., Lichtman J.W. A compensatory subpopulation of motor neurons in a mouse model of amyotrophic lateral sclerosis. J. Comp. Neurol. 2005, 490:209-219.
    • (2005) J. Comp. Neurol. , vol.490 , pp. 209-219
    • Schaefer, A.M.1    Sanes, J.R.2    Lichtman, J.W.3
  • 63
    • 21844446870 scopus 로고    scopus 로고
    • Glutathione redox state regulates mitochondrial reactive oxygen production
    • Shen D., Dalton T.P., Nebert D.W., Shertzer H.G. Glutathione redox state regulates mitochondrial reactive oxygen production. J. Biol. Chem. 2005, 280:25305-25312.
    • (2005) J. Biol. Chem. , vol.280 , pp. 25305-25312
    • Shen, D.1    Dalton, T.P.2    Nebert, D.W.3    Shertzer, H.G.4
  • 64
  • 65
    • 44749089373 scopus 로고    scopus 로고
    • High and low calcium-dependent mechanisms of mitochondrial calcium signalling
    • Hajnóczky
    • Spät A., Szanda G., Csordás G., Hajnóczky High and low calcium-dependent mechanisms of mitochondrial calcium signalling. Cell Calcium 2008, 44:51-63.
    • (2008) Cell Calcium , vol.44 , pp. 51-63
    • Spät, A.1    Szanda, G.2    Csordás, G.3
  • 66
    • 0024589641 scopus 로고
    • Three potassium currents in mouse motor nerve terminals
    • Tabti N., Bourret C., Mallart A. Three potassium currents in mouse motor nerve terminals. Pflugers Arch. 1989, 413:395-400.
    • (1989) Pflugers Arch. , vol.413 , pp. 395-400
    • Tabti, N.1    Bourret, C.2    Mallart, A.3
  • 67
    • 33947136312 scopus 로고    scopus 로고
    • Stimulation-induced changes in NADH fluorescence and mitochondrial membrane potential in lizard motor nerve terminals
    • Talbot J., Barrett J.N., Barrett E.F., David G. Stimulation-induced changes in NADH fluorescence and mitochondrial membrane potential in lizard motor nerve terminals. J. Physiol. 2007, 579:783-798.
    • (2007) J. Physiol. , vol.579 , pp. 783-798
    • Talbot, J.1    Barrett, J.N.2    Barrett, E.F.3    David, G.4
  • 68
    • 22244479388 scopus 로고    scopus 로고
    • Copper-zinc superoxide dismutase and amyotrophic lateral sclerosis
    • Valentine J.S., Doucette P.A., Zittin Potter S. Copper-zinc superoxide dismutase and amyotrophic lateral sclerosis. Annu. Rev. Biochem. 2005, 74:563-593.
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 563-593
    • Valentine, J.S.1    Doucette, P.A.2    Zittin Potter, S.3
  • 69
    • 0038380657 scopus 로고    scopus 로고
    • Stimulation-induced mitochondrial [Ca2+] elevations in mouse motor terminals: comparison of wild-type with SOD1G93A
    • Vila L., Barrett E.F., Barrett J.N. Stimulation-induced mitochondrial [Ca2+] elevations in mouse motor terminals: comparison of wild-type with SOD1G93A. J. Physiol. Lond. 2003, 549:719-728.
    • (2003) J. Physiol. Lond. , vol.549 , pp. 719-728
    • Vila, L.1    Barrett, E.F.2    Barrett, J.N.3
  • 70
    • 18144427184 scopus 로고    scopus 로고
    • Ca2+-induced permeabilization promotes free radical release from rat brain mitochondria with partially inhibited complex I
    • Votyakova T.V., Reynolds I.J. Ca2+-induced permeabilization promotes free radical release from rat brain mitochondria with partially inhibited complex I. J. Neurochem. 2005, 93:526-537.
    • (2005) J. Neurochem. , vol.93 , pp. 526-537
    • Votyakova, T.V.1    Reynolds, I.J.2
  • 71
    • 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
    • Woodfield K.A., Ruck A.D., Brdiczka D., Halestrap A.P. Direct demonstration of a specific interaction between cyclophilin-D and the adenine nucleotide translocase confirms their role in the mitochondrial permeability transition. Biochem. J. 1998, 336:287-290.
    • (1998) Biochem. J. , vol.336 , pp. 287-290
    • Woodfield, K.A.1    Ruck, A.D.2    Brdiczka, D.3    Halestrap, A.P.4
  • 73
    • 33747047814 scopus 로고    scopus 로고
    • The inflammatory NADPH oxidase enzyme modulates motor neuron degeneration in amyotrophic lateral sclerosis mice
    • Wu D.C., Ré D.B., Nagai M., Ischiropoulos H., Przedborski S. The inflammatory NADPH oxidase enzyme modulates motor neuron degeneration in amyotrophic lateral sclerosis mice. Proc. Natl Acad. Sci. USA 2006, 103:12132-12137.
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 12132-12137
    • Wu, D.C.1    Ré, D.B.2    Nagai, M.3    Ischiropoulos, H.4    Przedborski, S.5


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