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Volumn 76, Issue , 2014, Pages 59-69

Dysregulation of system xc- expression induced by mutant huntingtin in a striatal neuronal cell line and in R6/2 mice

Author keywords

Glutamate uptake; Glutathione; Huntington's disease; Oxidative stress; STHdh cells; xCT

Indexed keywords

CD98 ANTIGEN; GLUTATHIONE; HUNTINGTIN; MESSENGER RNA; MUTANT PROTEIN; REACTIVE OXYGEN METABOLITE; AMINO ACID TRANSPORTER; HUNTINGTON PROTEIN, MOUSE; NERVE PROTEIN; NUCLEAR PROTEIN; PRIMER DNA; SLC7A11 PROTEIN, MOUSE;

EID: 84905165974     PISSN: 01970186     EISSN: 18729754     Source Type: Journal    
DOI: 10.1016/j.neuint.2014.06.017     Document Type: Article
Times cited : (24)

References (74)
  • 1
    • 29444459269 scopus 로고    scopus 로고
    • Neuronal glutathione deficiency and age-dependent neurodegeneration in the EAAC1 deficient mouse
    • K. Aoyama, S.W. Suh, A.M. Hamby, J. Liu, W.Y. Chan, Y. Chen, and R.A. Swanson Neuronal glutathione deficiency and age-dependent neurodegeneration in the EAAC1 deficient mouse Nat. Neurosci. 9 2006 119 126
    • (2006) Nat. Neurosci. , vol.9 , pp. 119-126
    • Aoyama, K.1    Suh, S.W.2    Hamby, A.M.3    Liu, J.4    Chan, W.Y.5    Chen, Y.6    Swanson, R.A.7
  • 2
    • 0032529347 scopus 로고    scopus 로고
    • Maturation-dependent vulnerability of oligodendrocytes to oxidative stress-induced death caused by glutathione depletion
    • S.A. Back, X. Gan, Y. Li, P.A. Rosenberg, and J.J. Volpe Maturation-dependent vulnerability of oligodendrocytes to oxidative stress-induced death caused by glutathione depletion J. Neurosci. 18 1998 6241 6253
    • (1998) J. Neurosci. , vol.18 , pp. 6241-6253
    • Back, S.A.1    Gan, X.2    Li, Y.3    Rosenberg, P.A.4    Volpe, J.J.5
  • 3
    • 0022969399 scopus 로고
    • Exchange of cystine and glutamate across plasma membrane of human fibroblasts
    • S. Bannai Exchange of cystine and glutamate across plasma membrane of human fibroblasts J. Biol. Chem. 261 1986 2256 2263
    • (1986) J. Biol. Chem. , vol.261 , pp. 2256-2263
    • Bannai, S.1
  • 4
    • 0018963749 scopus 로고
    • Transport interaction of l-cystine and l-glutamate in human diploid fibroblasts in culture
    • S. Bannai, and E. Kitamura Transport interaction of l-cystine and l-glutamate in human diploid fibroblasts in culture J. Biol. Chem. 255 1980 2372 2376
    • (1980) J. Biol. Chem. , vol.255 , pp. 2372-2376
    • Bannai, S.1    Kitamura, E.2
  • 7
    • 81055127888 scopus 로고    scopus 로고
    • - cystine/glutamate antiporter: An update on molecular pharmacology and roles within the CNS
    • - cystine/glutamate antiporter: an update on molecular pharmacology and roles within the CNS Br. J. Pharmacol. 165 2012 20 34
    • (2012) Br. J. Pharmacol. , vol.165 , pp. 20-34
    • Bridges, R.J.1    Natale, N.R.2    Patel, S.A.3
  • 8
    • 57649187103 scopus 로고    scopus 로고
    • Mitochondria and Huntington's disease pathogenesis: Insight from genetic and chemical models
    • S.E. Browne Mitochondria and Huntington's disease pathogenesis: insight from genetic and chemical models Ann. N.Y. Acad. Sci. 1147 2008 358 382
    • (2008) Ann. N.Y. Acad. Sci. , vol.1147 , pp. 358-382
    • Browne, S.E.1
  • 9
    • 33947675275 scopus 로고    scopus 로고
    • Oxidative damage in Huntington's disease pathogenesis
    • S.E. Browne, and M.F. Beal Oxidative damage in Huntington's disease pathogenesis Antioxid. Redox Signal. 8 2006 2061 2073
    • (2006) Antioxid. Redox Signal. , vol.8 , pp. 2061-2073
    • Browne, S.E.1    Beal, M.F.2
  • 12
    • 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
  • 13
    • 35348877164 scopus 로고    scopus 로고
    • Transcriptional signatures in Huntington's disease
    • J.-H.J. Cha Transcriptional signatures in Huntington's disease Prog. Neurobiol. 83 2007 228 248
    • (2007) Prog. Neurobiol. , vol.83 , pp. 228-248
    • Cha, J.-H.J.1
  • 14
    • 79955930293 scopus 로고    scopus 로고
    • Mitochondrial dysfunction, metabolic deficits, and increased oxidative stress in Huntington's disease
    • C.-M. Chen Mitochondrial dysfunction, metabolic deficits, and increased oxidative stress in Huntington's disease Chang Gung Med. J. 34 2011 135 152
    • (2011) Chang Gung Med. J. , vol.34 , pp. 135-152
    • Chen, C.-M.1
  • 15
    • 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.W. 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.W.3    Lesort, M.4
  • 17
    • 0027686249 scopus 로고
    • Oxidative stress, glutamate, and neurodegenerative disorders
    • J.T. Coyle, and P. Puttfarcken Oxidative stress, glutamate, and neurodegenerative disorders Science 262 1993 689 695
    • (1993) Science , vol.262 , pp. 689-695
    • Coyle, J.T.1    Puttfarcken, P.2
  • 18
    • 33646572879 scopus 로고    scopus 로고
    • DNA microarray analysis of striatal gene expression in symptomatic transgenic Huntington's mice (R6/2) reveals neuroinflammation and insulin associations
    • S.F. Crocker, W.J. Costain, and H.A. Robertson DNA microarray analysis of striatal gene expression in symptomatic transgenic Huntington's mice (R6/2) reveals neuroinflammation and insulin associations Brain Res. 1088 2006 176 186
    • (2006) Brain Res. , vol.1088 , pp. 176-186
    • Crocker, S.F.1    Costain, W.J.2    Robertson, H.A.3
  • 19
    • 33749042331 scopus 로고    scopus 로고
    • Transcriptional repression of PGC-1α 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-1α 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
  • 21
    • 0025363346 scopus 로고
    • Excitotoxic injury of the neostriatum: A model for Huntington's disease
    • M. DiFiglia Excitotoxic injury of the neostriatum: a model for Huntington's disease Trends Neurosci. 13 1990 286 289
    • (1990) Trends Neurosci. , vol.13 , pp. 286-289
    • Difiglia, M.1
  • 22
    • 0033876436 scopus 로고    scopus 로고
    • Glutathione metabolism and oxidative stress in neurodegeneration
    • R. Dringen Glutathione metabolism and oxidative stress in neurodegeneration Eur. J. Biochem. 267 2000 4903
    • (2000) Eur. J. Biochem. , vol.267 , pp. 4903
    • Dringen, R.1
  • 23
    • 0038636003 scopus 로고    scopus 로고
    • Glutathione pathways in the brain
    • R. Dringen, and J. Hirrlinger Glutathione pathways in the brain Biol. Chem. 384 2003 505 516
    • (2003) Biol. Chem. , vol.384 , pp. 505-516
    • Dringen, R.1    Hirrlinger, J.2
  • 26
    • 34047100940 scopus 로고    scopus 로고
    • N-methyl-d-aspartate (NMDA) receptor function and excitotoxicity in Huntington's disease
    • M.M.Y. Fan, and L.A. Raymond N-methyl-d-aspartate (NMDA) receptor function and excitotoxicity in Huntington's disease Prog. Neurobiol. 81 2007 272 293
    • (2007) Prog. Neurobiol. , vol.81 , pp. 272-293
    • Fan, M.M.Y.1    Raymond, L.A.2
  • 28
  • 31
    • 33645350633 scopus 로고    scopus 로고
    • Brain-specific factors in combination with mutant huntingtin induce gene-specific transcriptional dysregulation
    • G.T. Gomez, H. Hu, E.A. McCaw, and E.M. Denovan-Wright Brain-specific factors in combination with mutant huntingtin induce gene-specific transcriptional dysregulation Mol. Cell. Neurosci. 31 2006 661 675
    • (2006) Mol. Cell. Neurosci. , vol.31 , pp. 661-675
    • Gomez, G.T.1    Hu, H.2    McCaw, E.A.3    Denovan-Wright, E.M.4
  • 32
    • 67651083577 scopus 로고    scopus 로고
    • The glutamate homeostasis hypothesis of addiction
    • P.W. Kalivas The glutamate homeostasis hypothesis of addiction Nat. Publishing Group 10 2009 561 572
    • (2009) Nat. Publishing Group , vol.10 , pp. 561-572
    • Kalivas, P.W.1
  • 33
    • 72049124015 scopus 로고    scopus 로고
    • ATF4-dependent transcription mediates signaling of amino acid limitation
    • M.S. Kilberg, J. Shan, and N. Su ATF4-dependent transcription mediates signaling of amino acid limitation Trends Endocrinol. Metab. 20 2009 436 443
    • (2009) Trends Endocrinol. Metab. , vol.20 , pp. 436-443
    • Kilberg, M.S.1    Shan, J.2    Su, N.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. Hećimović, T. Babić, 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    Hećimović, S.4    Babić, T.5    Trkulja, V.6
  • 35
    • 0842304134 scopus 로고    scopus 로고
    • Nuclear factor E2-related factor 2-dependent antioxidant response element activation by tert-butylhydroquinone and sulforaphane occurring preferentially in astrocytes conditions neurons against oxidative insult
    • A.D. Kraft, D.A. Johnson, and J.A. Johnson Nuclear factor E2-related factor 2-dependent antioxidant response element activation by tert-butylhydroquinone and sulforaphane occurring preferentially in astrocytes conditions neurons against oxidative insult J. Neurosci. 24 2004 1101 1112
    • (2004) J. Neurosci. , vol.24 , pp. 1101-1112
    • Kraft, A.D.1    Johnson, D.A.2    Johnson, J.A.3
  • 37
    • 34548399406 scopus 로고    scopus 로고
    • Unbiased gene expression analysis implicates the huntingtin polyglutamine tract in extra-mitochondrial energy metabolism
    • J.-M. Lee, E.V. Ivanova, I.S. Seong, T. Cashorali, I. Kohane, J.F. Gusella, and M.E. MacDonald Unbiased gene expression analysis implicates the huntingtin polyglutamine tract in extra-mitochondrial energy metabolism PLoS Genet. 3 2007 e135
    • (2007) PLoS Genet. , vol.3 , pp. 135
    • Lee, J.-M.1    Ivanova, E.V.2    Seong, I.S.3    Cashorali, T.4    Kohane, I.5    Gusella, J.F.6    Macdonald, M.E.7
  • 38
    • 84887792874 scopus 로고    scopus 로고
    • Soluble forms of polyQ-expanded huntingtin rather than large aggregates cause endoplasmic reticulum stress
    • J. Leitman, F. Ulrich Hartl, and G.Z. Lederkremer Soluble forms of polyQ-expanded huntingtin rather than large aggregates cause endoplasmic reticulum stress Nat. Commun. 4 2013 2753
    • (2013) Nat. Commun. , vol.4 , pp. 2753
    • Leitman, J.1    Ulrich Hartl, F.2    Lederkremer, G.Z.3
  • 39
    • 59449086812 scopus 로고    scopus 로고
    • Basal levels of eIF2α phosphorylation determine cellular antioxidant status by regulating ATF4 and xCT expression
    • J. Lewerenz, and P. Maher Basal levels of eIF2α phosphorylation determine cellular antioxidant status by regulating ATF4 and xCT expression J. Biol. Chem. 284 2009 1106 1115
    • (2009) J. Biol. Chem. , vol.284 , pp. 1106-1115
    • Lewerenz, J.1    Maher, P.2
  • 42
    • 0030867994 scopus 로고    scopus 로고
    • A role for 12-lipoxygenase in nerve cell death caused by glutathione depletion
    • Y. Li, P. Maher, and D. Schubert A role for 12-lipoxygenase in nerve cell death caused by glutathione depletion Neuron 19 1997 453 463
    • (1997) Neuron , vol.19 , pp. 453-463
    • Li, Y.1    Maher, P.2    Schubert, D.3
  • 43
    • 77950682093 scopus 로고    scopus 로고
    • Aberrant Rab11-dependent trafficking of the neuronal glutamate transporter EAAC1 causes oxidative stress and cell death in Huntington's disease
    • X. Li, A. Valencia, E. Sapp, N. Masso, J. Alexander, P. Reeves, K.B. Kegel, N. Aronin, and M. DiFiglia Aberrant Rab11-dependent trafficking of the neuronal glutamate transporter EAAC1 causes oxidative stress and cell death in Huntington's disease J. Neurosci. 30 2010 4552 4561
    • (2010) J. Neurosci. , vol.30 , pp. 4552-4561
    • Li, X.1    Valencia, A.2    Sapp, E.3    Masso, N.4    Alexander, J.5    Reeves, P.6    Kegel, K.B.7    Aronin, N.8    Difiglia, M.9
  • 45
    • 0036640537 scopus 로고    scopus 로고
    • Cerebral cystine uptake: A tale of two transporters
    • G.J. McBean Cerebral cystine uptake: a tale of two transporters Trends Pharmacol. Sci. 23 2002 299 302
    • (2002) Trends Pharmacol. Sci. , vol.23 , pp. 299-302
    • McBean, G.J.1
  • 46
    • 41949104569 scopus 로고    scopus 로고
    • Up-regulation of GLT1 expression increases glutamate uptake and attenuates the Huntington's disease phenotype in the R6/2 mouse
    • B.R. Miller, J.L. Dorner, M. Shou, Y. Sari, S.J. Barton, D.R. Sengelaub, R.T. Kennedy, and G.V. Rebec Up-regulation of GLT1 expression increases glutamate uptake and attenuates the Huntington's disease phenotype in the R6/2 mouse Neuroscience 153 2008 329 337
    • (2008) Neuroscience , vol.153 , pp. 329-337
    • Miller, B.R.1    Dorner, J.L.2    Shou, M.3    Sari, Y.4    Barton, S.J.5    Sengelaub, D.R.6    Kennedy, R.T.7    Rebec, G.V.8
  • 47
    • 0025355933 scopus 로고
    • Immature cortical neurons are uniquely sensitive to glutamate toxicity by inhibition of cystine uptake
    • T.H. Murphy, R.L. Schnaar, and J.T. Coyle Immature cortical neurons are uniquely sensitive to glutamate toxicity by inhibition of cystine uptake FASEB J. 4 1990 1624 1633
    • (1990) FASEB J. , vol.4 , pp. 1624-1633
    • Murphy, T.H.1    Schnaar, R.L.2    Coyle, J.T.3
  • 50
    • 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
  • 51
    • 78049277912 scopus 로고    scopus 로고
    • Huntington's disease out of the closet?
    • M. Rawlins Huntington's disease out of the closet? Lancet 376 2010 1372 1373
    • (2010) Lancet , vol.376 , pp. 1372-1373
    • Rawlins, M.1
  • 52
    • 81255149512 scopus 로고    scopus 로고
    • Pathophysiology of Huntington's disease: Time-dependent alterations in synaptic and receptor function
    • L.A. Raymond, V.M. André, C. Cepeda, C.M. Gladding, A.J. Milnerwood, and M.S. Levine Pathophysiology of Huntington's disease: time-dependent alterations in synaptic and receptor function Neuroscience 198 2011 252 273
    • (2011) Neuroscience , vol.198 , pp. 252-273
    • Raymond, L.A.1    André, V.M.2    Cepeda, C.3    Gladding, C.M.4    Milnerwood, A.J.5    Levine, M.S.6
  • 54
    • 0024406708 scopus 로고
    • Hundred-fold increase in neuronal vulnerability to glutamate toxicity in astrocyte-poor cultures of rat cerebral cortex
    • P.A. Rosenberg, and E. Aizenman Hundred-fold increase in neuronal vulnerability to glutamate toxicity in astrocyte-poor cultures of rat cerebral cortex Neurosci. Lett. 103 1989 162 168
    • (1989) Neurosci. Lett. , vol.103 , pp. 162-168
    • Rosenberg, P.A.1    Aizenman, E.2
  • 55
    • 0026596688 scopus 로고
    • Glutamate uptake disguises neurotoxic potency of glutamate agonists in cerebral cortex in dissociated cell culture
    • P.A. Rosenberg, S. Amin, and M. Leitner Glutamate uptake disguises neurotoxic potency of glutamate agonists in cerebral cortex in dissociated cell culture J. Neurosci. 12 1992 56 61
    • (1992) J. Neurosci. , vol.12 , pp. 56-61
    • Rosenberg, P.A.1    Amin, S.2    Leitner, M.3
  • 57
    • 0033597349 scopus 로고    scopus 로고
    • Cloning and expression of a plasma membrane cystine/glutamate exchange transporter composed of two distinct proteins
    • H. Sato, M. Tamba, T. Ishii, and S. Bannai Cloning and expression of a plasma membrane cystine/glutamate exchange transporter composed of two distinct proteins J. Biol. Chem. 274 1999 11455 11458
    • (1999) J. Biol. Chem. , vol.274 , pp. 11455-11458
    • Sato, H.1    Tamba, M.2    Ishii, T.3    Bannai, S.4
  • 59
    • 79960741110 scopus 로고    scopus 로고
    • Regulation of the system x(C)- cystine/glutamate exchanger by intracellular glutathione levels in rat astrocyte primary cultures
    • T.M. Seib, S.A. Patel, and R.J. Bridges Regulation of the system x(C)- cystine/glutamate exchanger by intracellular glutathione levels in rat astrocyte primary cultures Glia 59 2011 1387 1401
    • (2011) Glia , vol.59 , pp. 1387-1401
    • Seib, T.M.1    Patel, S.A.2    Bridges, R.J.3
  • 60
    • 33749831751 scopus 로고    scopus 로고
    • Cystine/glutamate exchange modulates glutathione supply for neuroprotection from oxidative stress and cell proliferation
    • A.Y. Shih, H. Erb, X. Sun, S. Toda, P.W. Kalivas, and T.H. Murphy Cystine/glutamate exchange modulates glutathione supply for neuroprotection from oxidative stress and cell proliferation J. Neurosci. 26 2006 10514 10523
    • (2006) J. Neurosci. , vol.26 , pp. 10514-10523
    • Shih, A.Y.1    Erb, H.2    Sun, X.3    Toda, S.4    Kalivas, P.W.5    Murphy, T.H.6
  • 62
    • 0027480960 scopus 로고
    • A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes
    • Huntington'S Disease Collaborative Research Group T.
    • 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 1993 971 983
    • (1993) Cell , vol.72 , pp. 971-983
  • 63
    • 0014481378 scopus 로고
    • Enzymic method for quantitative determination of nanogram amounts of total and oxidized glutathione: Applications to mammalian blood and other tissues
    • F. Tietze Enzymic method for quantitative determination of nanogram amounts of total and oxidized glutathione: applications to mammalian blood and other tissues Anal. Biochem. 27 1969 502 522
    • (1969) Anal. Biochem. , vol.27 , pp. 502-522
    • Tietze, F.1
  • 64
    • 33846970909 scopus 로고    scopus 로고
    • Neurochemical changes in Huntington R6/2 mouse striatum detected by in vivo 1H NMR spectroscopy
    • I. Tkác, 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
    • Tkác, I.1    Dubinsky, J.M.2    Keene, C.D.3    Gruetter, R.4    Low, W.C.5
  • 69
    • 0025313258 scopus 로고
    • Depletion of tissue glutathione with diethyl maleate enhances hyperbaric oxygen toxicity
    • L308-12
    • C.A. Weber, C.A. Duncan, M.J. Lyons, and S.G. Jenkinson Depletion of tissue glutathione with diethyl maleate enhances hyperbaric oxygen toxicity Am. J. Physiol. 258 1990 L308-12
    • (1990) Am. J. Physiol. , vol.258
    • Weber, C.A.1    Duncan, C.A.2    Lyons, M.J.3    Jenkinson, S.G.4
  • 73
    • 0033198997 scopus 로고    scopus 로고
    • Glioma cells release excitotoxic concentrations of glutamate
    • Z.C. Ye, and H. Sontheimer Glioma cells release excitotoxic concentrations of glutamate Cancer Res. 59 1999 4383 4391
    • (1999) Cancer Res. , vol.59 , pp. 4383-4391
    • Ye, Z.C.1    Sontheimer, H.2
  • 74
    • 0029891464 scopus 로고    scopus 로고
    • Interaction of l-cysteine with a human excitatory amino acid transporter
    • N. Zerangue, and M.P. Kavanaugh Interaction of l-cysteine with a human excitatory amino acid transporter J. Physiol. (Lond.) 493 Pt. 2 1996 419 423
    • (1996) J. Physiol. (Lond.) , vol.493 , Issue.PART 2 , pp. 419-423
    • Zerangue, N.1    Kavanaugh, M.P.2


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