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Volumn 53, Issue 10, 2012, Pages 1857-1867

Glutathione redox cycle dysregulation in Huntington's disease knock-in striatal cells

Author keywords

Huntingtin; Huntington disease; Oxidative stress; Reactive oxygen species; Striatal cells

Indexed keywords

GAMMA GLUTAMYLTRANSFERASE; GLUTAMATE CYSTEINE LIGASE; GLUTATHIONE; GLUTATHIONE DISULFIDE; GLUTATHIONE PEROXIDASE; GLUTATHIONE REDUCTASE; GLUTATHIONE SYNTHASE; GLUTATHIONE TRANSFERASE; MESSENGER RNA; MULTIDRUG RESISTANCE PROTEIN 1;

EID: 84867380632     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2012.09.004     Document Type: Article
Times cited : (59)

References (46)
  • 1
    • 45149107487 scopus 로고    scopus 로고
    • Mechanisms of neurodegeneration in Huntington's disease
    • [Erratum: Eur. J. Neurosci. 28:2156; 2008.]
    • J.M. Gil, and A.C. Rego Mechanisms of neurodegeneration in Huntington's disease Eur. J. Neurosci 27 2008 2803 2820 [Erratum: Eur. J. Neurosci. 28:2156; 2008.]
    • (2008) Eur. J. Neurosci , vol.27 , pp. 2803-2820
    • Gil, J.M.1    Rego, A.C.2
  • 2
    • 0027480960 scopus 로고
    • A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes
    • The Huntington's Disease Collaborative Research Group
    • The Huntington's Disease Collaborative Research Group. A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. Cell 72:971-983; 1993.
    • (1993) Cell , vol.72 , pp. 971-983
  • 7
    • 32644481227 scopus 로고    scopus 로고
    • Oxidative stress promotes mutant huntingtin aggregation and mutant huntingtin-dependent cell death by mimicking proteasomal malfunction
    • A. Goswami, P. Dikshit, A. Mishra, S. Mulherkar, N. Nukina, and N.R. Jana Oxidative stress promotes mutant huntingtin aggregation and mutant huntingtin-dependent cell death by mimicking proteasomal malfunction Biochem. Biophys. Res. Commun. 342 2006 184 190
    • (2006) Biochem. Biophys. Res. Commun. , vol.342 , pp. 184-190
    • Goswami, A.1    Dikshit, P.2    Mishra, A.3    Mulherkar, S.4    Nukina, N.5    Jana, N.R.6
  • 10
    • 0033520166 scopus 로고    scopus 로고
    • Oxidative damage to mitochondrial DNA in Huntington's disease parietal cortex
    • M.C. Polidori, P. Mecocci, S.E. Browne, U. Senin, and M.F. Beal Oxidative damage to mitochondrial DNA in Huntington's disease parietal cortex Neurosci. Lett. 272 1999 53 56
    • (1999) Neurosci. Lett. , vol.272 , pp. 53-56
    • Polidori, M.C.1    Mecocci, P.2    Browne, S.E.3    Senin, U.4    Beal, M.F.5
  • 12
    • 0035668684 scopus 로고    scopus 로고
    • Increased oxidative damage to DNA in a transgenic mouse model of Huntington's disease
    • M.B. Bogdanov, O.A. Andreassen, A. Dedeoglu, R.J. Ferrante, and M.F. Beal Increased oxidative damage to DNA in a transgenic mouse model of Huntington's disease J. Neurochem. 79 2001 1246 1249
    • (2001) J. Neurochem. , vol.79 , pp. 1246-1249
    • Bogdanov, M.B.1    Andreassen, O.A.2    Dedeoglu, A.3    Ferrante, R.J.4    Beal, M.F.5
  • 14
    • 41949126549 scopus 로고    scopus 로고
    • Calcium homeostasis and mitochondrial dysfunction in striatal neurons of Huntington disease
    • D. Lim, L. Fedrizzi, M. Tartari, C. Zuccato, E. Cattaneo, M. Brini, and E. Carafoli Calcium homeostasis and mitochondrial dysfunction in striatal neurons of Huntington disease J. Biol. Chem. 283 2008 5780 5789
    • (2008) J. Biol. Chem. , vol.283 , pp. 5780-5789
    • Lim, D.1    Fedrizzi, L.2    Tartari, M.3    Zuccato, C.4    Cattaneo, E.5    Brini, M.6    Carafoli, E.7
  • 15
    • 33846970909 scopus 로고    scopus 로고
    • Neurochemical changes in Huntington R6/2 mouse striatum detected by in vivo 1H NMR spectroscopy
    • I. Tkac, J.M. Dubinsky, C.D. Keene, R. Gruetter, and W.C. Low Neurochemical changes in Huntington R6/2 mouse striatum detected by in vivo 1H NMR spectroscopy J. Neurochem. 100 2007 1397 1406
    • (2007) J. Neurochem. , vol.100 , pp. 1397-1406
    • Tkac, I.1    Dubinsky, J.M.2    Keene, C.D.3    Gruetter, R.4    Low, W.C.5
  • 16
    • 22544469454 scopus 로고    scopus 로고
    • Increased glutathione levels in cortical and striatal mitochondria of the R6/2 Huntington's disease mouse model
    • Y.S. Choo, Z. Mao, G.V. Johnson, and M. Lesort Increased glutathione levels in cortical and striatal mitochondria of the R6/2 Huntington's disease mouse model Neurosci. Lett. 386 2005 63 68
    • (2005) Neurosci. Lett. , vol.386 , pp. 63-68
    • Choo, Y.S.1    Mao, Z.2    Johnson, G.V.3    Lesort, M.4
  • 18
    • 0026554428 scopus 로고
    • Evaluation of the probe 2′,7′-dichlorofluorescin as an indicator of reactive oxygen species formation and oxidative stress
    • C.P. LeBel, H. Ischiropoulos, and S.C. Bondy Evaluation of the probe 2′,7′-dichlorofluorescin as an indicator of reactive oxygen species formation and oxidative stress Chem. Res. Toxicol. 5 1992 227 231
    • (1992) Chem. Res. Toxicol. , vol.5 , pp. 227-231
    • Lebel, C.P.1    Ischiropoulos, H.2    Bondy, S.C.3
  • 19
    • 0017064979 scopus 로고
    • A fluorometric method for determination of oxidized and reduced glutathione in tissues
    • P.J. Hissin, and R. Hilf A fluorometric method for determination of oxidized and reduced glutathione in tissues Anal. Biochem. 74 1976 214 226
    • (1976) Anal. Biochem. , vol.74 , pp. 214-226
    • Hissin, P.J.1    Hilf, R.2
  • 20
    • 0014108436 scopus 로고
    • Studies on the quantitative and qualitative characterization of erythrocyte glutathione peroxidase
    • D.E. Paglia, and W.N. Valentine Studies on the quantitative and qualitative characterization of erythrocyte glutathione peroxidase J. Lab. Clin. Med. 70 1967 158 169
    • (1967) J. Lab. Clin. Med. , vol.70 , pp. 158-169
    • Paglia, D.E.1    Valentine, W.N.2
  • 21
    • 0038242969 scopus 로고    scopus 로고
    • Fluorescence-based microtiter plate assay for glutamate-cysteine ligase activity
    • C.C. White, H. Viernes, C.M. Krejsa, D. Botta, and T.J. Kavanagh Fluorescence-based microtiter plate assay for glutamate-cysteine ligase activity Anal. Biochem. 318 2003 175 180
    • (2003) Anal. Biochem. , vol.318 , pp. 175-180
    • White, C.C.1    Viernes, H.2    Krejsa, C.M.3    Botta, D.4    Kavanagh, T.J.5
  • 22
    • 33744525840 scopus 로고    scopus 로고
    • Age-related changes in glutathione and glutathione-related enzymes in rat brain
    • Y. Zhu, P.M. Carvey, and Z. Ling Age-related changes in glutathione and glutathione-related enzymes in rat brain Brain Res. 1090 2006 35 44
    • (2006) Brain Res. , vol.1090 , pp. 35-44
    • Zhu, Y.1    Carvey, P.M.2    Ling, Z.3
  • 23
    • 2142648906 scopus 로고    scopus 로고
    • Evaluation and comparison of MRP1 activity with three fluorescent dyes and three modulators in leukemic cell lines
    • A.L. Dogan, O. Legrand, AM. Faussat, JY. Perrot, and JP. Marie Evaluation and comparison of MRP1 activity with three fluorescent dyes and three modulators in leukemic cell lines Leuk. Res. 28 2004 619 622
    • (2004) Leuk. Res. , vol.28 , pp. 619-622
    • Dogan, A.L.1    Legrand, O.2    Faussat, A.M.3    Perrot, J.Y.4    Marie, J.P.5
  • 24
    • 19444362449 scopus 로고    scopus 로고
    • Hypochlorous acid-mediated mitochondrial dysfunction and apoptosis in human hepatoma HepG2 and human fetal liver cells: Role of mitochondrial permeability transition
    • M. Whiteman, P. Rose, J.L. Siau, N.S. Cheung, G.S. Tan, B. Halliwell, and J.S. Armstrong Hypochlorous acid-mediated mitochondrial dysfunction and apoptosis in human hepatoma HepG2 and human fetal liver cells: role of mitochondrial permeability transition Free Radic. Biol. Med. 38 2005 1571 1584
    • (2005) Free Radic. Biol. Med. , vol.38 , pp. 1571-1584
    • Whiteman, M.1    Rose, P.2    Siau, J.L.3    Cheung, N.S.4    Tan, G.S.5    Halliwell, B.6    Armstrong, J.S.7
  • 25
    • 0028578004 scopus 로고
    • Overexpression of the gene encoding the multidrug resistance-associated protein results in increased ATP-dependent glutathione S-conjugate transport
    • M. Müller, C. Meijer, G.J. Zaman, P. Borst, R.J. Scheper, N.H. Mulder, E.G. de Vries, and P.L. Jansen Overexpression of the gene encoding the multidrug resistance-associated protein results in increased ATP-dependent glutathione S-conjugate transport Proc. Natl. Acad. Sci. USA 91 1994 13033 13037
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 13033-13037
    • Müller, M.1    Meijer, C.2    Zaman, G.J.3    Borst, P.4    Scheper, R.J.5    Mulder, N.H.6    De Vries, E.G.7    Jansen, P.L.8
  • 26
    • 12144288637 scopus 로고    scopus 로고
    • Segovia, J. Increased formation of reactive oxygen species, but no changes in glutathione peroxidase activity, in striata of mice transgenic for the Huntington's disease mutation
    • F. Perez-Severiano, A. Santamaria, J. Pedraza-Chaverri, O.N. Medina-Campos, and C. Rios Segovia, J. Increased formation of reactive oxygen species, but no changes in glutathione peroxidase activity, in striata of mice transgenic for the Huntington's disease mutation Neurochem. Res. 29 2004 729 733
    • (2004) Neurochem. Res. , vol.29 , pp. 729-733
    • Perez-Severiano, F.1    Santamaria, A.2    Pedraza-Chaverri, J.3    Medina-Campos, O.N.4    Rios, C.5
  • 27
    • 24744444740 scopus 로고    scopus 로고
    • Mitochondrial respiration and ATP production are significantly impaired in striatal cells expressing mutant huntingtin
    • T. Milakovic, and G.V. Johnson Mitochondrial respiration and ATP production are significantly impaired in striatal cells expressing mutant huntingtin J. Biol. Chem. 280 2005 30773 30782
    • (2005) J. Biol. Chem. , vol.280 , pp. 30773-30782
    • Milakovic, T.1    Johnson, G.V.2
  • 29
    • 54449092109 scopus 로고    scopus 로고
    • Rosiglitazone treatment prevents mitochondrial dysfunction in mutant huntingtin-expressing cells: Possible role of peroxisome proliferator-activated receptor-gamma (PPARgamma) in the pathogenesis of Huntington disease
    • R.A. Quintanilla, Y.N. Jin, K. Fuenzalida, M. Bronfman, and G.V. Johnson Rosiglitazone treatment prevents mitochondrial dysfunction in mutant huntingtin-expressing cells: possible role of peroxisome proliferator-activated receptor-gamma (PPARgamma) in the pathogenesis of Huntington disease J. Biol. Chem. 283 2008 25628 25637
    • (2008) J. Biol. Chem. , vol.283 , pp. 25628-25637
    • Quintanilla, R.A.1    Jin, Y.N.2    Fuenzalida, K.3    Bronfman, M.4    Johnson, G.V.5
  • 30
    • 33645841052 scopus 로고    scopus 로고
    • Transcranial magnetic stimulation attenuates cell loss and oxidative damage in the striatum induced in the 3-nitropropionic model of Huntington's disease
    • I. Tunez, R. Drucker-Colin, I. Jimena, F.J. Medina, C. Munoz Mdel, J. Pena, and P. Montilla Transcranial magnetic stimulation attenuates cell loss and oxidative damage in the striatum induced in the 3-nitropropionic model of Huntington's disease J. Neurochem. 97 2006 619 630
    • (2006) J. Neurochem. , vol.97 , pp. 619-630
    • Tunez, I.1    Drucker-Colin, R.2    Jimena, I.3    Medina, F.J.4    Munoz Mdel, C.5    Pena, J.6    Montilla, P.7
  • 32
    • 33645450264 scopus 로고    scopus 로고
    • Cystamine and cysteamine prevent 3-NP-induced mitochondrial depolarization of Huntington's disease knock-in striatal cells
    • Z. Mao, Y.S. Choo, and M. Lesort Cystamine and cysteamine prevent 3-NP-induced mitochondrial depolarization of Huntington's disease knock-in striatal cells Eur. J. Neurosci 23 2006 1701 1710
    • (2006) Eur. J. Neurosci , vol.23 , pp. 1701-1710
    • Mao, Z.1    Choo, Y.S.2    Lesort, M.3
  • 34
    • 37749000434 scopus 로고    scopus 로고
    • Oxidative stress parameters in plasma of Huntington's disease patients, asymptomatic Huntington's disease gene carriers and healthy subjects: A cross-sectional study
    • N. Klepac, M. Relja, R. Klepac, S. Hecimovic, T. Babic, and V. Trkulja Oxidative stress parameters in plasma of Huntington's disease patients, asymptomatic Huntington's disease gene carriers and healthy subjects: a cross-sectional study J. Neurol. 254 2007 1676 1683
    • (2007) J. Neurol. , vol.254 , pp. 1676-1683
    • Klepac, N.1    Relja, M.2    Klepac, R.3    Hecimovic, S.4    Babic, T.5    Trkulja, V.6
  • 35
    • 0028075410 scopus 로고
    • Alterations in glutathione levels in Parkinson's disease and other neurodegenerative disorders affecting basal ganglia
    • J. Sian, D.T. Dexter, A.J. Lees, S. Daniel, Y. Agid, F. Javoy-Agid, P. Jenner, and C.D. Marsden Alterations in glutathione levels in Parkinson's disease and other neurodegenerative disorders affecting basal ganglia Ann. Neurol. 36 1994 348 355
    • (1994) Ann. Neurol. , vol.36 , pp. 348-355
    • Sian, J.1    Dexter, D.T.2    Lees, A.J.3    Daniel, S.4    Agid, Y.5    Javoy-Agid, F.6    Jenner, P.7    Marsden, C.D.8
  • 38
    • 51749107237 scopus 로고    scopus 로고
    • Increased glucose metabolism and ATP level in brain tissue of Huntington's disease transgenic mice
    • J. Olah, P. Klivenyi, G. Gardian, L. Vecsei, F. Orosz, G.G. Kovacs, H.V. Westerhoff, and J. Ovadi Increased glucose metabolism and ATP level in brain tissue of Huntington's disease transgenic mice FEBS J. 275 2008 4740 4755
    • (2008) FEBS J. , vol.275 , pp. 4740-4755
    • Olah, J.1    Klivenyi, P.2    Gardian, G.3    Vecsei, L.4    Orosz, F.5    Kovacs, G.G.6    Westerhoff, H.V.7    Ovadi, J.8
  • 39
    • 0030678131 scopus 로고    scopus 로고
    • Evidence that the multidrug resistance protein (MRP) functions as a co-transporter of glutathione and natural product toxins
    • G. Rappa, A. Lorico, R.A. Flavell, and A.C. Sartorelli Evidence that the multidrug resistance protein (MRP) functions as a co-transporter of glutathione and natural product toxins Cancer Res 57 1997 5232 5237
    • (1997) Cancer Res , vol.57 , pp. 5232-5237
    • Rappa, G.1    Lorico, A.2    Flavell, R.A.3    Sartorelli, A.C.4
  • 40
    • 33745897902 scopus 로고    scopus 로고
    • Transport of glutathione and glutathione conjugates by MRP1
    • S.P. Cole, and R.G. Deeley Transport of glutathione and glutathione conjugates by MRP1 Trends Pharmacol. Sci. 27 2006 438 446
    • (2006) Trends Pharmacol. Sci. , vol.27 , pp. 438-446
    • Cole, S.P.1    Deeley, R.G.2
  • 41
    • 0034283877 scopus 로고    scopus 로고
    • Transcriptional dysregulation in Huntington's disease
    • J.H. Cha Transcriptional dysregulation in Huntington's disease Trends Neurosci. 23 2000 387 392
    • (2000) Trends Neurosci. , vol.23 , pp. 387-392
    • Cha, J.H.1
  • 42
    • 0035430282 scopus 로고    scopus 로고
    • Transcriptional regulation by the phosphorylation-dependent factor CREB
    • B. Mayr, and M. Montminy Transcriptional regulation by the phosphorylation-dependent factor CREB Nat. Rev. Mol. Cell. Biol. 2 2001 599 609
    • (2001) Nat. Rev. Mol. Cell. Biol. , vol.2 , pp. 599-609
    • Mayr, B.1    Montminy, M.2
  • 44
    • 33749042331 scopus 로고    scopus 로고
    • Transcriptional repression of PGC-1alpha by mutant huntingtin leads to mitochondrial dysfunction and neurodegeneration
    • L. Cui, H. Jeong, F. Borovecki, C.N. Parkhurst, N. Tanese, and D. Krainc Transcriptional repression of PGC-1alpha by mutant huntingtin leads to mitochondrial dysfunction and neurodegeneration Cell 127 2006 59 69
    • (2006) Cell , vol.127 , pp. 59-69
    • Cui, L.1    Jeong, H.2    Borovecki, F.3    Parkhurst, C.N.4    Tanese, N.5    Krainc, D.6
  • 45
    • 33645304045 scopus 로고    scopus 로고
    • The multidrug resistance protein 1 (Mrp1), but not Mrp5, mediates export of glutathione and glutathione disulfide from brain astrocytes
    • T. Minich, J. Riemer, J.B. Schulz, P. Wielinga, J. Wijnholds, and R. Dringen The multidrug resistance protein 1 (Mrp1), but not Mrp5, mediates export of glutathione and glutathione disulfide from brain astrocytes J. Neurochem. 97 2006 373 384
    • (2006) J. Neurochem. , vol.97 , pp. 373-384
    • Minich, T.1    Riemer, J.2    Schulz, J.B.3    Wielinga, P.4    Wijnholds, J.5    Dringen, R.6
  • 46
    • 0033230779 scopus 로고    scopus 로고
    • Export pumps for glutathione S-conjugates
    • D. Keppler Export pumps for glutathione S-conjugates Free Radic. Biol. Med. 27 1999 985 991
    • (1999) Free Radic. Biol. Med. , vol.27 , pp. 985-991
    • Keppler, D.1


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