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Volumn 23, Issue 8, 2003, Pages 3394-3406

Coordinate regulation of glutathione biosynthesis and release by Nrf2-expressing glia potently protects neurons from oxidative stress

Author keywords

Antioxidant response element; Astrocyte; Cystine deprivation; Glutathione; Neuroprotection; Nrf2; Oxidative glutamate toxicity; Oxidative stress; Phase II detoxification enzymes; Quinone reductase; System xc ; Tert butylhydroquinone; XCT

Indexed keywords

ANTIPORTER; CELL PROTEIN; GLUTAMATE CYSTEINE LIGASE; GLUTAMIC ACID; GLUTATHIONE; GLUTATHIONE REDUCTASE; GLUTATHIONE SYNTHASE; GLUTATHIONE TRANSFERASE; MULTIDRUG RESISTANCE PROTEIN 1; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR NRF2; UNCLASSIFIED DRUG; XCT CYSTINE ANTIPORTER;

EID: 0037996661     PISSN: 02706474     EISSN: None     Source Type: Journal    
DOI: 10.1523/jneurosci.23-08-03394.2003     Document Type: Article
Times cited : (662)

References (85)
  • 1
    • 0033556326 scopus 로고    scopus 로고
    • Coordinate regulation of NAD(P)H:quinone oxidoreductase and glutathione S-transferases in primary cultures of rat neurons and glia: Role of the antioxidant/electrophile responsive element
    • Ahlgren-Beckendorf JA, Reising AM, Schander MA, Herdler JW, Johnson JA (1999) Coordinate regulation of NAD(P)H:quinone oxidoreductase and glutathione S-transferases in primary cultures of rat neurons and glia: role of the antioxidant/electrophile responsive element. Glia 25:131-142.
    • (1999) Glia , vol.25 , pp. 131-142
    • Ahlgren-Beckendorf, J.A.1    Reising, A.M.2    Schander, M.A.3    Herdler, J.W.4    Johnson, J.A.5
  • 2
    • 0033543566 scopus 로고    scopus 로고
    • Nrf2, a Cap'n'Collar transcription factor, regulates induction of the heme oxygenase-1 gene
    • Alam J, Stewart D, Touchard C, Boinapally S, Choi AM, Cook JL (1999) Nrf2, a Cap'n'Collar transcription factor, regulates induction of the heme oxygenase-1 gene. J Biol Chem 274:26071-26078.
    • (1999) J Biol Chem , vol.274 , pp. 26071-26078
    • Alam, J.1    Stewart, D.2    Touchard, C.3    Boinapally, S.4    Choi, A.M.5    Cook, J.L.6
  • 3
    • 0024261104 scopus 로고
    • Alteration of amino acid content of cerebrospinal fluid from patients with epilepsy
    • Araki K, Harada M, Ueda Y, Takino T, Kuriyama K (1988) Alteration of amino acid content of cerebrospinal fluid from patients with epilepsy. Acta Neurol Scand 78:473-479.
    • (1988) Acta Neurol Scand , vol.78 , pp. 473-479
    • Araki, K.1    Harada, M.2    Ueda, Y.3    Takino, T.4    Kuriyama, K.5
  • 4
    • 0022969399 scopus 로고
    • Exchange of cystine and glutamate across plasma membrane of human fibroblasts
    • Bannai S (1986) Exchange of cystine and glutamate across plasma membrane of human fibroblasts. J Biol Chem 261:2256-2263.
    • (1986) J Biol Chem , vol.261 , pp. 2256-2263
    • Bannai, S.1
  • 5
    • 0037192626 scopus 로고    scopus 로고
    • Site-directed mutagenesis of cysteine to serine in the DNA binding region of Nrf2 decreases its capacity to upregulate antioxidant response element-mediated expression and antioxidant induction of NAD(P)H:quinone oxidoreductasel gene
    • Bloom D, Dhakshinamoorthy S, Jaiswal AK (2002) Site-directed mutagenesis of cysteine to serine in the DNA binding region of Nrf2 decreases its capacity to upregulate antioxidant response element-mediated expression and antioxidant induction of NAD(P)H:quinone oxidoreductasel gene. Oncogene 21:2191-2200.
    • (2002) Oncogene , vol.21 , pp. 2191-2200
    • Bloom, D.1    Dhakshinamoorthy, S.2    Jaiswal, A.K.3
  • 6
    • 13044304201 scopus 로고    scopus 로고
    • Nrf2 is essential for protection against acute pulmonary injury in mice
    • Chan K, Kan YW (1999) Nrf2 is essential for protection against acute pulmonary injury in mice. Proc Natl Acad Sci USA 96:12731-12736.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 12731-12736
    • Chan, K.1    Kan, Y.W.2
  • 7
    • 0023392945 scopus 로고
    • High-efficiency transformation of mammalian cells by plasmid DNA
    • Chen C, Okayama H (1987) High-efficiency transformation of mammalian cells by plasmid DNA. Mol Cell Biol 7:2745-2752.
    • (1987) Mol Cell Biol , vol.7 , pp. 2745-2752
    • Chen, C.1    Okayama, H.2
  • 8
    • 0034977186 scopus 로고    scopus 로고
    • Astrocytes protect neurons from nitric oxide toxicity by a glutathionedependent mechanism
    • Chen Y, Vartiainen NE, Ying W, Chan PH, Koistinaho J, Swanson RA (2001) Astrocytes protect neurons from nitric oxide toxicity by a glutathionedependent mechanism, J Neurochem 77:1601-1610,
    • (2001) J Neurochem , vol.77 , pp. 1601-1610
    • Chen, Y.1    Vartiainen, N.E.2    Ying, W.3    Chan, P.H.4    Koistinaho, J.5    Swanson, R.A.6
  • 10
    • 0027686249 scopus 로고
    • Oxidative stress, glutamate, and neurodegenerative disorders
    • Coyle JT, Puttfarcken P (1993) Oxidative stress, glutamate, and neurodegenerative disorders. Science 262:689-695.
    • (1993) Science , vol.262 , pp. 689-695
    • Coyle, J.T.1    Puttfarcken, P.2
  • 12
    • 0029990439 scopus 로고    scopus 로고
    • Astrocytes protect neurons from hydrogen peroxide toxicity
    • Desagher S, Glowinski J, Premont J (1996) Astrocytes protect neurons from hydrogen peroxide toxicity. J Neurosci 16:2553-2562.
    • (1996) J Neurosci , vol.16 , pp. 2553-2562
    • Desagher, S.1    Glowinski, J.2    Premont, J.3
  • 13
    • 0033555806 scopus 로고    scopus 로고
    • Synthesis of the antioxidant glutathione in neurons: Supply by astrocytes of CysGly as precursor for neuronal glutathione
    • Dringen R, Pfeiffer B, Hamprecht B (1999) Synthesis of the antioxidant glutathione in neurons: supply by astrocytes of CysGly as precursor for neuronal glutathione. J Neurosci 19:562-569.
    • (1999) J Neurosci , vol.19 , pp. 562-569
    • Dringen, R.1    Pfeiffer, B.2    Hamprecht, B.3
  • 14
    • 0033899176 scopus 로고    scopus 로고
    • Glutathione metabolism in brain metabolic interaction between astrocytes and neurons in the defense against reactive oxygen species
    • Dringen R, Gutterer JM, Hirrlinger J (2000) Glutathione metabolism in brain metabolic interaction between astrocytes and neurons in the defense against reactive oxygen species. Eur J Biochem 267:4912-4916.
    • (2000) Eur J Biochem , vol.267 , pp. 4912-4916
    • Dringen, R.1    Gutterer, J.M.2    Hirrlinger, J.3
  • 15
    • 0035577287 scopus 로고    scopus 로고
    • Aminopeptidase N mediates the utilization of the GSH precursor CysGly by cultured neurons
    • Dringen R, Gutterer JM, Gros C, Hirrlinger J (2001) Aminopeptidase N mediates the utilization of the GSH precursor CysGly by cultured neurons. J Neurosci Res 66:1003-1008.
    • (2001) J Neurosci Res , vol.66 , pp. 1003-1008
    • Dringen, R.1    Gutterer, J.M.2    Gros, C.3    Hirrlinger, J.4
  • 16
    • 0030772178 scopus 로고    scopus 로고
    • Astrocyte-mediated enhancement of neuronal survival is abolished by glutathione deficiency
    • Drukarch B, Schepens E, Jongenelen CA, Stoof JC, Langeveld CH (1997) Astrocyte-mediated enhancement of neuronal survival is abolished by glutathione deficiency. Brain Res 770:123-130.
    • (1997) Brain Res , vol.770 , pp. 123-130
    • Drukarch, B.1    Schepens, E.2    Jongenelen, C.A.3    Stoof, J.C.4    Langeveld, C.H.5
  • 17
    • 0031866279 scopus 로고    scopus 로고
    • Activation of endogenous antioxidant defenses in neuronal cells prevents free radical-mediated damage
    • Duffy S, So A, Murphy TH (1998) Activation of endogenous antioxidant defenses in neuronal cells prevents free radical-mediated damage. J Neurochem 71:69-77.
    • (1998) J Neurochem , vol.71 , pp. 69-77
    • Duffy, S.1    So, A.2    Murphy, T.H.3
  • 18
    • 0028929896 scopus 로고
    • Differential expression of heme oxygenase-1 in cultured cortical neurons and astrocytes determined by the aid of a new heme oxygenase antibody. Response to oxidative stress
    • Dwyer BE, Nishimura RN, Lu SY (1995) Differential expression of heme oxygenase-1 in cultured cortical neurons and astrocytes determined by the aid of a new heme oxygenase antibody. Response to oxidative stress. Brain Res Mol Brain Res 30:37-47.
    • (1995) Brain Res Mol Brain Res , vol.30 , pp. 37-47
    • Dwyer, B.E.1    Nishimura, R.N.2    Lu, S.Y.3
  • 19
    • 0033828495 scopus 로고    scopus 로고
    • Thioredoxin reductase and glutathione synthesis is [sic] upregulated by t-butylhydroquinone in cortical astrocytes but not in cortical neurons
    • Eftekharpour E, Holmgren A, Juurlink BH (2000) Thioredoxin reductase and glutathione synthesis is [sic] upregulated by t-butylhydroquinone in cortical astrocytes but not in cortical neurons. Glia 31:241-248.
    • (2000) Glia , vol.31 , pp. 241-248
    • Eftekharpour, E.1    Holmgren, A.2    Juurlink, B.H.3
  • 20
    • 0030931522 scopus 로고    scopus 로고
    • Broccoli sprouts: An exceptionally rich source of inducers of enzymes that protect against chemical carcinogens
    • Fahey JW, Zhang Y, Talalay P (1997) Broccoli sprouts: an exceptionally rich source of inducers of enzymes that protect against chemical carcinogens. Proc Natl Acad Sci USA 94:10367-10372.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 10367-10372
    • Fahey, J.W.1    Zhang, Y.2    Talalay, P.3
  • 21
    • 0025145723 scopus 로고
    • Xenobiotic-inducible expression of murine glutathione S-transferase Ya subunit gene is controlled by an electrophile-responsive element
    • Friling RS, Bensimon A, Tichauer Y, Daniel V (1990) Xenobiotic-inducible expression of murine glutathione S-transferase Ya subunit gene is controlled by an electrophile-responsive element. Proc Natl Acad Sci USA 87:6258-6262.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 6258-6262
    • Friling, R.S.1    Bensimon, A.2    Tichauer, Y.3    Daniel, V.4
  • 22
    • 0035909947 scopus 로고    scopus 로고
    • Powerful and prolonged protection of human retinal pigment epithelial cells, keratinocytes, and mouse leukemia cells against oxidative damage: The indirect antioxidant effects of sulforaphane
    • Gao X, Dinkova-Kostova AT, Talalay P (2001) Powerful and prolonged protection of human retinal pigment epithelial cells, keratinocytes, and mouse leukemia cells against oxidative damage: the indirect antioxidant effects of sulforaphane. Proc Natl Acad Sci USA 98:15221-15226.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 15221-15226
    • Gao, X.1    Dinkova-Kostova, A.T.2    Talalay, P.3
  • 24
    • 0018666729 scopus 로고
    • Potent and specific inhibition of glutathione synthesis by buthionine sulfoximine (S-n-butyl homocysteine sulfoximine)
    • Griffith OW, Meister A (1979) Potent and specific inhibition of glutathione synthesis by buthionine sulfoximine (S-n-butyl homocysteine sulfoximine). J Biol Chem 254:7558-7560.
    • (1979) J Biol Chem , vol.254 , pp. 7558-7560
    • Griffith, O.W.1    Meister, A.2
  • 25
    • 0031055468 scopus 로고    scopus 로고
    • Construction of adenovirus vectors through Cre-lox recombination
    • Hardy S, Kitamura M, Harris-Stansil T, Dai Y, Phipps ML (1997) Construction of adenovirus vectors through Cre-lox recombination. J Virol 71:1842-1849.
    • (1997) J Virol , vol.71 , pp. 1842-1849
    • Hardy, S.1    Kitamura, M.2    Harris-Stansil, T.3    Dai, Y.4    Phipps, M.L.5
  • 26
    • 0029561598 scopus 로고
    • The glutathione S-transferase supergene family: Regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance
    • Hayes JD, Pulford DJ (1995) The glutathione S-transferase supergene family: regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance. Crit Rev Biochem Mol Biol 30:445-600.
    • (1995) Crit Rev Biochem Mol Biol , vol.30 , pp. 445-600
    • Hayes, J.D.1    Pulford, D.J.2
  • 27
    • 0033956744 scopus 로고    scopus 로고
    • The Nrf2 transcription factor contributes both to the basal expression of glutathione S-transferases in mouse liver and to their induction by the chemopreventive synthetic antioxidants, butylated hydroxyanisole and ethoxyquin
    • Hayes JD, Chanas SA, Henderson CJ, McMahon M, Sun C, Moffat GJ, Wolf CR, Yamamoto M (2000) The Nrf2 transcription factor contributes both to the basal expression of glutathione S-transferases in mouse liver and to their induction by the chemopreventive synthetic antioxidants, butylated hydroxyanisole and ethoxyquin. Biochem Soc Trans 28:33-41.
    • (2000) Biochem Soc Trans , vol.28 , pp. 33-41
    • Hayes, J.D.1    Chanas, S.A.2    Henderson, C.J.3    McMahon, M.4    Sun, C.5    Moffat, G.J.6    Wolf, C.R.7    Yamamoto, M.8
  • 28
    • 0035145779 scopus 로고    scopus 로고
    • The multidrug resistance protein MRP1 mediates the release of glutathione disulfide from rat astrocytes during oxidative stress
    • Hirrlinger J, Konig J, Keppler D, Lindenau J, Schulz JB, Dringen R (2001) The multidrug resistance protein MRP1 mediates the release of glutathione disulfide from rat astrocytes during oxidative stress. J Neurochem 76:627-636.
    • (2001) J Neurochem , vol.76 , pp. 627-636
    • Hirrlinger, J.1    Konig, J.2    Keppler, D.3    Lindenau, J.4    Schulz, J.B.5    Dringen, R.6
  • 29
    • 0036682171 scopus 로고    scopus 로고
    • Glutathione release from cultured brain cells: Multidrug resistance protein 1 mediates the release of GSH from rat astroglial cells
    • Hirrlinger J, Schulz JB, Dringen R (2002) Glutathione release from cultured brain cells: multidrug resistance protein 1 mediates the release of GSH from rat astroglial cells. J Neurosci Res 69:318-326.
    • (2002) J Neurosci Res , vol.69 , pp. 318-326
    • Hirrlinger, J.1    Schulz, J.B.2    Dringen, R.3
  • 30
    • 0032981550 scopus 로고    scopus 로고
    • Evidence of glutathione transporter in rat brain synaptosomal membrane vesicles
    • Iantomasi T, Favilli F, Vincenzini MT (1999) Evidence of glutathione transporter in rat brain synaptosomal membrane vesicles. Neurochem Int 34:509-516.
    • (1999) Neurochem Int , vol.34 , pp. 509-516
    • Iantomasi, T.1    Favilli, F.2    Vincenzini, M.T.3
  • 31
    • 0034717329 scopus 로고    scopus 로고
    • Transcription factor Nrf2 coordinately regulates a group of oxidative stress-inducible genes in macrophages
    • Ishii T, Itoh K, Takahashi S, Sato H, Yanagawa T, Katoh Y, Bannai S, Yamamoto M (2000) Transcription factor Nrf2 coordinately regulates a group of oxidative stress-inducible genes in macrophages. J Biol Chem 275:16023-16029.
    • (2000) J Biol Chem , vol.275 , pp. 16023-16029
    • Ishii, T.1    Itoh, K.2    Takahashi, S.3    Sato, H.4    Yanagawa, T.5    Katoh, Y.6    Bannai, S.7    Yamamoto, M.8
  • 33
    • 0032827002 scopus 로고    scopus 로고
    • Regulatory mechanisms of cellular response to oxidative stress
    • Itoh K, Ishii T, Wakabayashi N, Yamamoto M (1999) Regulatory mechanisms of cellular response to oxidative stress. Free Radic Res 31:319-324.
    • (1999) Free Radic Res , vol.31 , pp. 319-324
    • Itoh, K.1    Ishii, T.2    Wakabayashi, N.3    Yamamoto, M.4
  • 34
    • 0036319473 scopus 로고    scopus 로고
    • Activation of the antioxidant response element in primary cortical neuronal cultures derived from transgenic reporter mice
    • Johnson DA, Andrews GK, Xu W, Johnson JA (2002) Activation of the antioxidant response element in primary cortical neuronal cultures derived from transgenic reporter mice. J Neurochem 81:1233-1241.
    • (2002) J Neurochem , vol.81 , pp. 1233-1241
    • Johnson, D.A.1    Andrews, G.K.2    Xu, W.3    Johnson, J.A.4
  • 35
    • 0029942499 scopus 로고    scopus 로고
    • Evidence for the existence of a sodium-dependent glutathione (GSH) transporter. Expression of bovine brain capillary mRNA and size fractions in Xenopus laevis oocytes and dissociation from γ-glutamyltranspeptidase and facilitative GSH transporters
    • Kannan R, Yi JR, Tang D, Li Y, Zlokovic BV, Kaplowitz N (1996) Evidence for the existence of a sodium-dependent glutathione (GSH) transporter. Expression of bovine brain capillary mRNA and size fractions in Xenopus laevis oocytes and dissociation from γ-glutamyltranspeptidase and facilitative GSH transporters. J Biol Chem 271:9754-9758.
    • (1996) J Biol Chem , vol.271 , pp. 9754-9758
    • Kannan, R.1    Yi, J.R.2    Tang, D.3    Li, Y.4    Zlokovic, B.V.5    Kaplowitz, N.6
  • 36
    • 0033036416 scopus 로고    scopus 로고
    • GSH transport in immortalized mouse brain endothelial cells: Evidence for apical localization of a sodium-dependent GSH transporter
    • Kannan R, Mittur A, Bao Y, Tsuruo T, Kaplowitz N (1999) GSH transport in immortalized mouse brain endothelial cells: evidence for apical localization of a sodium-dependent GSH transporter. J Neurochem 73:390-399.
    • (1999) J Neurochem , vol.73 , pp. 390-399
    • Kannan, R.1    Mittur, A.2    Bao, Y.3    Tsuruo, T.4    Kaplowitz, N.5
  • 38
    • 0030868098 scopus 로고    scopus 로고
    • Chemoprevention by inducers of carcinogen detoxication enzymes
    • Kensler TW (1997) Chemoprevention by inducers of carcinogen detoxication enzymes. Environ Health Perspect 105[Suppl 4]:965-970.
    • (1997) Environ Health Perspect , vol.105 , Issue.SUPPL. 4 , pp. 965-970
    • Kensler, T.W.1
  • 39
    • 0034788643 scopus 로고    scopus 로고
    • Pathways of neuron-astrocyte interactions and their possible role in neuroprotection
    • Kirchhoff F, Dringen R, Giaume C (2001) Pathways of neuron-astrocyte interactions and their possible role in neuroprotection. Eur Arch Psychiatry Clin Neurosci 251:159-169.
    • (2001) Eur Arch Psychiatry Clin Neurosci , vol.251 , pp. 159-169
    • Kirchhoff, F.1    Dringen, R.2    Giaume, C.3
  • 40
    • 0030606289 scopus 로고    scopus 로고
    • Different preferences in the utilization of amino acids for glutathione synthesis in cultured neurons and astroglial cells derived from rat brain
    • Kranich O, Hamprecht B, Dringen R (1996) Different preferences in the utilization of amino acids for glutathione synthesis in cultured neurons and astroglial cells derived from rat brain. Neurosci Lett 219:211-214.
    • (1996) Neurosci Lett , vol.219 , pp. 211-214
    • Kranich, O.1    Hamprecht, B.2    Dringen, R.3
  • 41
    • 0017182854 scopus 로고
    • Amino acid abnormalities in cerebrospinal fluid of patients with parkinsonism and extrapyramidal disorders
    • Lakke JP, Teelken AW (1976) Amino acid abnormalities in cerebrospinal fluid of patients with parkinsonism and extrapyramidal disorders. Neurology 26:489-493.
    • (1976) Neurology , vol.26 , pp. 489-493
    • Lakke, J.P.1    Teelken, A.W.2
  • 42
    • 0034805627 scopus 로고    scopus 로고
    • Nrf2-dependent activation of the antioxidant response element by tert-butylhydroquinone is independent of oxidative stress in IMR-32 human neuroblastoma cells
    • Lee JM, Moehlenkamp JD, Hanson JM, Johnson JA (2001) Nrf2-dependent activation of the antioxidant response element by tert-butylhydroquinone is independent of oxidative stress in IMR-32 human neuroblastoma cells. Biochem Biophys Res Commun 280:286-292.
    • (2001) Biochem Biophys Res Commun , vol.280 , pp. 286-292
    • Lee, J.M.1    Moehlenkamp, J.D.2    Hanson, J.M.3    Johnson, J.A.4
  • 43
    • 0346739951 scopus 로고    scopus 로고
    • Time-dependent changes in ARE-driven gene expression by use of a noise-filtering process for microarray data
    • Li J, Johnson JA (2002) Time-dependent changes in ARE-driven gene expression by use of a noise-filtering process for microarray data. Physiol Genomics 9:137-144.
    • (2002) Physiol Genomics , vol.9 , pp. 137-144
    • Li, J.1    Johnson, J.A.2
  • 44
    • 0037016759 scopus 로고    scopus 로고
    • Microarray analysis reveals an antioxidant responsive element-driven gene set involved in conferring protection from an oxidative stress-induced apoptosis in IMR-32 cells
    • Li J, Lee JM, Johnson JA (2002) Microarray analysis reveals an antioxidant responsive element-driven gene set involved in conferring protection from an oxidative stress-induced apoptosis in IMR-32 cells. J Biol Chem 277:388-394.
    • (2002) J Biol Chem , vol.277 , pp. 388-394
    • Li, J.1    Lee, J.M.2    Johnson, J.A.3
  • 45
    • 0030447364 scopus 로고    scopus 로고
    • Postnatal retinal ganglion cells in vitro: Protection against reactive oxygen species (ROS)-induced axonal degeneration by cocultured astrocytes
    • Lucius R, Sievers J (1996) Postnatal retinal ganglion cells in vitro: protection against reactive oxygen species (ROS)-induced axonal degeneration by cocultured astrocytes. Brain Res 743:56-62.
    • (1996) Brain Res , vol.743 , pp. 56-62
    • Lucius, R.1    Sievers, J.2
  • 46
    • 0027976087 scopus 로고
    • Vitamin E, ascorbate, glutathione, glutathione disulfide, and enzymes of glutathione metabolism in cultures of chick astrocytes and neurons: Evidence that astrocytes play an important role in antioxidative processes in the brain
    • Makar TK, Nedergaard M, Preuss A, Gelbard AS, Perumal AS, Cooper AJ (1994) Vitamin E, ascorbate, glutathione, glutathione disulfide, and enzymes of glutathione metabolism in cultures of chick astrocytes and neurons: evidence that astrocytes play an important role in antioxidative processes in the brain. J Neurochem 62:45-53.
    • (1994) J Neurochem , vol.62 , pp. 45-53
    • Makar, T.K.1    Nedergaard, M.2    Preuss, A.3    Gelbard, A.S.4    Perumal, A.S.5    Cooper, A.J.6
  • 47
    • 0032848944 scopus 로고    scopus 로고
    • Changes in amino acid concentrations over time and space around an impact injury and their diffusion through the rat spinal cord
    • McAdoo DJ, Xu GY, Robak G, Hughes MG (1999) Changes in amino acid concentrations over time and space around an impact injury and their diffusion through the rat spinal cord. Exp Neurol 159:538-544.
    • (1999) Exp Neurol , vol.159 , pp. 538-544
    • McAdoo, D.J.1    Xu, G.Y.2    Robak, G.3    Hughes, M.G.4
  • 48
    • 0029915162 scopus 로고    scopus 로고
    • Glia-conditioned medium protects fetal rat midbrain neurones in culture from L-DOPA toxicity
    • Mena MA, Casarejos MJ, Carazo A, Paino CL, Garcia de Yebenes J (1996) Glia-conditioned medium protects fetal rat midbrain neurones in culture from L-DOPA toxicity. NeuroReport 7:441-445.
    • (1996) NeuroReport , vol.7 , pp. 441-445
    • Mena, M.A.1    Casarejos, M.J.2    Carazo, A.3    Paino, C.L.4    Garcia de Yebenes, J.5
  • 49
    • 0037119577 scopus 로고    scopus 로고
    • Drug targeting: Breaking down barriers
    • Miller G (2002) Drug targeting: breaking down barriers. Science 297:1116-1118.
    • (2002) Science , vol.297 , pp. 1116-1118
    • Miller, G.1
  • 50
    • 0033102622 scopus 로고    scopus 로고
    • Activation of antioxidant/electrophile-responsive elements in IMR-32 human neuroblastoma cells
    • Moehlenkamp JD, Johnson JA (1999) Activation of antioxidant/electrophile-responsive elements in IMR-32 human neuroblastoma cells. Arch Biochem Biophys 363:98-106.
    • (1999) Arch Biochem Biophys , vol.363 , pp. 98-106
    • Moehlenkamp, J.D.1    Johnson, J.A.2
  • 51
    • 0024678458 scopus 로고
    • Glutamate toxicity in a neuronal cell line involves inhibition of cystine transport leading to oxidative stress
    • Murphy TH, Miyamoto M, Sastre A, Schnaar RL, Coyle JT (1989) Glutamate toxicity in a neuronal cell line involves inhibition of cystine transport leading to oxidative stress. Neuron 2:1547-1558.
    • (1989) Neuron , vol.2 , pp. 1547-1558
    • Murphy, T.H.1    Miyamoto, M.2    Sastre, A.3    Schnaar, R.L.4    Coyle, J.T.5
  • 52
    • 0025355933 scopus 로고
    • Immature cortical neurons are uniquely sensitive to glutamate toxicity by inhibition of cystine uptake
    • Murphy TH, Schnaar RL, Coyle JT (1990) Immature cortical neurons are uniquely sensitive to glutamate toxicity by inhibition of cystine uptake. FASEB J 4:1624-1633.
    • (1990) FASEB J , vol.4 , pp. 1624-1633
    • Murphy, T.H.1    Schnaar, R.L.2    Coyle, J.T.3
  • 53
    • 0031969963 scopus 로고    scopus 로고
    • Histochernical detection of quinone reductase activity in situ using LY 83583 reduction and oxidation
    • Murphy TH, So AP, Vincent SR (1998) Histochernical detection of quinone reductase activity in situ using LY 83583 reduction and oxidation. J Neurochem 70:2156-2164.
    • (1998) J Neurochem , vol.70 , pp. 2156-2164
    • Murphy, T.H.1    So, A.P.2    Vincent, S.R.3
  • 54
    • 0035107463 scopus 로고    scopus 로고
    • Preferential expression of antioxidant response element mediated gene expression in astrocytes
    • Murphy TH, Yu J, Ng R, Johnson DA, Shen H, Honey CR, Johnson JA (2001) Preferential expression of antioxidant response element mediated gene expression in astrocytes. J Neurochem 76:1670-1678.
    • (2001) J Neurochem , vol.76 , pp. 1670-1678
    • Murphy, T.H.1    Yu, J.2    Ng, R.3    Johnson, D.A.4    Shen, H.5    Honey, C.R.6    Johnson, J.A.7
  • 55
    • 0034685897 scopus 로고    scopus 로고
    • Transcriptional regulation of the antioxidant response element. Activation by Nrf2 and repression by MafK
    • Nguyen T, Huang HC, Pickett CB (2000) Transcriptional regulation of the antioxidant response element. Activation by Nrf2 and repression by MafK. J Biol Chem 275:15466-15473.
    • (2000) J Biol Chem , vol.275 , pp. 15466-15473
    • Nguyen, T.1    Huang, H.C.2    Pickett, C.B.3
  • 56
    • 0013282861 scopus 로고    scopus 로고
    • Increased protein stability as a mechanism that enhances Nrf2-mediated transcriptional activation of the antioxidant response element: Degradation of Nrf2 by the 26S proteasome
    • Nguyen T, Sherratt PJ, Huang HC, Yang CS, Pickett CB (2003) Increased protein stability as a mechanism that enhances Nrf2-mediated transcriptional activation of the antioxidant response element: degradation of Nrf2 by the 26S proteasome. J Biol Chem 278:4536-4541.
    • (2003) J Biol Chem , vol.278 , pp. 4536-4541
    • Nguyen, T.1    Sherratt, P.J.2    Huang, H.C.3    Yang, C.S.4    Pickett, C.B.5
  • 57
    • 0023370658 scopus 로고
    • Calcium-dependent and -independent release of glutamate from synaptosomes monitored by continuous fluorometry
    • Nicholls DG, Sihra TS, Sanchez-Prieto J (1987) Calcium-dependent and -independent release of glutamate from synaptosomes monitored by continuous fluorometry. J Neurochem 49:50-57.
    • (1987) J Neurochem , vol.49 , pp. 50-57
    • Nicholls, D.G.1    Sihra, T.S.2    Sanchez-Prieto, J.3
  • 58
    • 0027487416 scopus 로고
    • The electrophile counterattack response: Protection against neoplasia and toxicity
    • Prestera T, Zhang Y, Spencer SR, Wilczak CA, Talalay P (1993) The electrophile counterattack response: protection against neoplasia and toxicity. Adv Enzyme Regul 33:281-296.
    • (1993) Adv Enzyme Regul , vol.33 , pp. 281-296
    • Prestera, T.1    Zhang, Y.2    Spencer, S.R.3    Wilczak, C.A.4    Talalay, P.5
  • 60
    • 0024324666 scopus 로고
    • Glutathione is present in high concentrations in cultured astrocytes but not in cultured neurons
    • Raps SP, Lai JC, Hertz L, Cooper AJ (1989) Glutathione is present in high concentrations in cultured astrocytes but not in cultured neurons. Brain Res 493:398-401.
    • (1989) Brain Res , vol.493 , pp. 398-401
    • Raps, S.P.1    Lai, J.C.2    Hertz, L.3    Cooper, A.J.4
  • 61
    • 0028095981 scopus 로고
    • Oxidative stress induces apoptosis in embryonic cortical neurons
    • Ratan RR, Murphy TH, Baraban JM (1994) Oxidative stress induces apoptosis in embryonic cortical neurons. J Neurochem 62:376-379.
    • (1994) J Neurochem , vol.62 , pp. 376-379
    • Ratan, R.R.1    Murphy, T.H.2    Baraban, J.M.3
  • 62
    • 0025948113 scopus 로고
    • The antioxidant responsive element. Activation by oxidative stress and identification of the DNA consensus sequence required for functional activity
    • Rushmore TH, Morton MR, Pickett CB (1991) The antioxidant responsive element. Activation by oxidative stress and identification of the DNA consensus sequence required for functional activity. J Biol Chem 266:11632-11639.
    • (1991) J Biol Chem , vol.266 , pp. 11632-11639
    • Rushmore, T.H.1    Morton, M.R.2    Pickett, C.B.3
  • 63
    • 0027489346 scopus 로고
    • Cystine uptake and glutathione level in fetal brain cells in primary culture and in suspension
    • Sagara J, Miura K, Bannai S (1993a) Cystine uptake and glutathione level in fetal brain cells in primary culture and in suspension. J Neurochem 61:1667-1671.
    • (1993) J Neurochem , vol.61 , pp. 1667-1671
    • Sagara, J.1    Miura, K.2    Bannai, S.3
  • 64
    • 0027421350 scopus 로고
    • Maintenance of neuronal glutathione by glial cells
    • Sagara J, Miura K, Bannai S (1993b) Maintenance of neuronal glutathione by glial cells. J Neurochem 61:1672-1676.
    • (1993) J Neurochem , vol.61 , pp. 1672-1676
    • Sagara, J.1    Miura, K.2    Bannai, S.3
  • 65
    • 0029988384 scopus 로고    scopus 로고
    • Glutathione efflux from cultured astrocytes
    • Sagara J, Makino N, Bannai S (1996) Glutathione efflux from cultured astrocytes. J Neurochem 66:1876-1881.
    • (1996) J Neurochem , vol.66 , pp. 1876-1881
    • Sagara, J.1    Makino, N.2    Bannai, S.3
  • 67
    • 0033597349 scopus 로고    scopus 로고
    • Cloning and expression of a plasma membrane cystine/glutamate exchange transporter composed of two distinct proteins
    • Sato H, Tamba M, Ishii T, Bannai S (1999) Cloning and expression of a plasma membrane cystine/glutamate exchange transporter composed of two distinct proteins. J Biol Chem 274:11455-11458.
    • (1999) J Biol Chem , vol.274 , pp. 11455-11458
    • Sato, H.1    Tamba, M.2    Ishii, T.3    Bannai, S.4
  • 68
    • 0035478598 scopus 로고    scopus 로고
    • Oxidative glutamate toxicity can be a component of the excitotoxicity cascade
    • Schubert D, Piasecki D (2001) Oxidative glutamate toxicity can be a component of the excitotoxicity cascade. J Neurosci 21:7455-7462.
    • (2001) J Neurosci , vol.21 , pp. 7455-7462
    • Schubert, D.1    Piasecki, D.2
  • 69
    • 0037015682 scopus 로고    scopus 로고
    • Nrf2 degradation by the ubiquitin proteasome pathway is inhibited by KIAA0132, the human homolog to INrf2
    • Sekhar KR, Yan XX, Freeman ML (2002) Nrf2 degradation by the ubiquitin proteasome pathway is inhibited by KIAA0132, the human homolog to INrf2. Oncogene 21:6829-6834.
    • (2002) Oncogene , vol.21 , pp. 6829-6834
    • Sekhar, K.R.1    Yan, X.X.2    Freeman, M.L.3
  • 70
    • 0034812524 scopus 로고    scopus 로고
    • xCt cystine transporter expression in HEK293 cells: Pharmacology and localization
    • Shih AY, Murphy TH (2001) xCt cystine transporter expression in HEK293 cells: pharmacology and localization. Biochem Biophys Res Commun 282:1132-1137.
    • (2001) Biochem Biophys Res Commun , vol.282 , pp. 1132-1137
    • Shih, A.Y.1    Murphy, T.H.2
  • 72
    • 0036759157 scopus 로고
    • Lack of neurodegeneration in transgenic mice overexpressing mutant amyloid precursor protein is associated with increased levels of transthyretin and the activation of cell survival pathways
    • Stein TD, Johnson JA (2002) Lack of neurodegeneration in transgenic mice overexpressing mutant amyloid precursor protein is associated with increased levels of transthyretin and the activation of cell survival pathways. J Neurosci 22:7380-7388.
    • (1981) J Neurosci , vol.22 , pp. 7380-7388
    • Stein, T.D.1    Johnson, J.A.2
  • 73
    • 0037462651 scopus 로고    scopus 로고
    • Degradation of transcription factor Nrf2 via the ubiquitin-proteasome pathway and stabilization by cadmium
    • Stewart D, Killeen E, Naquin R, Alam S, Alam J (2003) Degradation of transcription factor Nrf2 via the ubiquitin-proteasome pathway and stabilization by cadmium. J Biol Chem 278:2396-2402.
    • (2003) J Biol Chem , vol.278 , pp. 2396-2402
    • Stewart, D.1    Killeen, E.2    Naquin, R.3    Alam, S.4    Alam, J.5
  • 75
    • 0032526940 scopus 로고    scopus 로고
    • The regulation of reactive oxygen species production during programmed cell death
    • Tan S, Sagara Y, Liu Y, Maher P, Schubert D (1998) The regulation of reactive oxygen species production during programmed cell death. J Cell Biol 141:1423-1432.
    • (1998) J Cell Biol , vol.141 , pp. 1423-1432
    • Tan, S.1    Sagara, Y.2    Liu, Y.3    Maher, P.4    Schubert, D.5
  • 76
    • 0033230119 scopus 로고    scopus 로고
    • Astrocytes prevent neuronal death induced by reactive oxygen and nitrogen species
    • Tanaka J, Toku K, Zhang B, Ishihara K, Sakanaka M, Maeda N (1999) Astrocytes prevent neuronal death induced by reactive oxygen and nitrogen species. Glia 28:85-96.
    • (1999) Glia , vol.28 , pp. 85-96
    • Tanaka, J.1    Toku, K.2    Zhang, B.3    Ishihara, K.4    Sakanaka, M.5    Maeda, N.6
  • 78
    • 0037106099 scopus 로고    scopus 로고
    • Identification of Nrf2-regulated genes induced by the chemopreventive agent sulforaphane by oligonucleotide microarray
    • Thimmulappa RK, Mai KH, Srisuma S, Kensler TW, Yamamoto M, Biswal S (2002) Identification of Nrf2-regulated genes induced by the chemopreventive agent sulforaphane by oligonucleotide microarray. Cancer Res 62:5196-5203.
    • (2002) Cancer Res , vol.62 , pp. 5196-5203
    • Thimmulappa, R.K.1    Mai, K.H.2    Srisuma, S.3    Kensler, T.W.4    Yamamoto, M.5    Biswal, S.6
  • 79
    • 0014481378 scopus 로고
    • Enzymic method for quantitative determination of nanogram amounts of total and oxidized glutathione: Applications to mammalian blood and other tissues
    • Tietze F (1969) Enzymic method for quantitative determination of nanogram amounts of total and oxidized glutathione: applications to mammalian blood and other tissues. Anal Biochem 27:502-522.
    • (1969) Anal Biochem , vol.27 , pp. 502-522
    • Tietze, F.1
  • 80
    • 0027985428 scopus 로고
    • Glia: The brain's other cells
    • Travis J (1994) Glia: the brain's other cells. Science 266:970-972.
    • (1994) Science , vol.266 , pp. 970-972
    • Travis, J.1
  • 81
    • 0029906134 scopus 로고    scopus 로고
    • Nrf1 and Nrf2 positively and c-Fos and Fra1 negatively regulate the human antioxidant response elementmediated expression of NAD(P)H:quinone oxidoreductase1 gene
    • Venugopal R, Jaiswal AK (1996) Nrf1 and Nrf2 positively and c-Fos and Fra1 negatively regulate the human antioxidant response elementmediated expression of NAD(P)H:quinone oxidoreductase1 gene. Proc Natl Acad Sci USA 93:14960-14965.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 14960-14965
    • Venugopal, R.1    Jaiswal, A.K.2
  • 82
    • 0032542213 scopus 로고    scopus 로고
    • Nrf2 and Nrf1 in association with Jun proteins regulate antioxidant response element-mediated expression and coordinated induction of genes encoding detoxifying enzymes
    • Venugopal R, Jaiswal AK (1998) Nrf2 and Nrf1 in association with Jun proteins regulate antioxidant response element-mediated expression and coordinated induction of genes encoding detoxifying enzymes. Oncogene 17:3145-3156.
    • (1998) Oncogene , vol.17 , pp. 3145-3156
    • Venugopal, R.1    Jaiswal, A.K.2
  • 83
    • 0001412747 scopus 로고    scopus 로고
    • Astrocytes provide cysteine to neurons by releasing glutathione
    • Wang XF, Cynader MS (2000) Astrocytes provide cysteine to neurons by releasing glutathione. J Neurochem 74:1434-1442.
    • (2000) J Neurochem , vol.74 , pp. 1434-1442
    • Wang, X.F.1    Cynader, M.S.2
  • 84
    • 0029067149 scopus 로고
    • A detailed analysis of hydrogen peroxide-induced cell death in primary neuronal culture
    • Whittemore ER, Loo DT, Watt JA, Cotman CW (1995) A detailed analysis of hydrogen peroxide-induced cell death in primary neuronal culture. Neuroscience 67:921-932.
    • (1995) Neuroscience , vol.67 , pp. 921-932
    • Whittemore, E.R.1    Loo, D.T.2    Watt, J.A.3    Cotman, C.W.4


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