메뉴 건너뛰기




Volumn 33, Issue 7, 2008, Pages 1410-1418

Astrocytes protect against copper-catalysed loss of extracellular glutathione

Author keywords

Astrocytes; Copper; Extracellular; Glutathione; Oxidative stress

Indexed keywords

ASCORBIC ACID; COPPER; GLUTATHIONE; PENTETIC ACID;

EID: 44549085157     PISSN: 03643190     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11064-008-9602-3     Document Type: Article
Times cited : (34)

References (51)
  • 1
    • 0028114890 scopus 로고
    • The reaction of superoxide with reduced glutathione
    • Winterbourn CC, Metodiewa D (1994) The reaction of superoxide with reduced glutathione. Arch Biochem Biophys 314:284-290
    • (1994) Arch Biochem Biophys , vol.314 , pp. 284-290
    • Winterbourn, C.C.1    Metodiewa, D.2
  • 2
    • 0020027542 scopus 로고
    • The reaction of the hydroxyl radical with glutathione in neutral and alkaline aqueous solution
    • Sjoberg L, Eriksen TE, Revesz L (1982) The reaction of the hydroxyl radical with glutathione in neutral and alkaline aqueous solution. Radiat Res 89:255-263
    • (1982) Radiat Res , vol.89 , pp. 255-263
    • Sjoberg, L.1    Eriksen, T.E.2    Revesz, L.3
  • 3
    • 0031418498 scopus 로고    scopus 로고
    • Neurodegenerative disorders in humans: The role of glutathione in oxidative stress-mediated neuronal death
    • Bains JS, Shaw CA (1997) Neurodegenerative disorders in humans: the role of glutathione in oxidative stress-mediated neuronal death. Brain Res Rev 25:335-358
    • (1997) Brain Res Rev , vol.25 , pp. 335-358
    • Bains, J.S.1    Shaw, C.A.2
  • 4
    • 0028075410 scopus 로고
    • Alterations in glutathione levels in Parkinson's disease and other neurodegenerative disorders affecting basal ganglia
    • Sian J, Dexter DT, Lees AJ et al (1994) Alterations in glutathione levels in Parkinson's disease and other neurodegenerative disorders affecting basal ganglia. Ann Neurol 36:348-355
    • (1994) Ann Neurol , vol.36 , pp. 348-355
    • Sian, J.1    Dexter, D.T.2    Lees, A.J.3
  • 5
    • 0026644192 scopus 로고
    • Reduced and oxidized glutathione in the substantia nigra of patients with Parkinson's disease
    • Sofic E, Lange KW, Jellinger K et al (1992) Reduced and oxidized glutathione in the substantia nigra of patients with Parkinson's disease. Neurosci Lett 142:128-130
    • (1992) Neurosci Lett , vol.142 , pp. 128-130
    • Sofic, E.1    Lange, K.W.2    Jellinger, K.3
  • 6
    • 0028799706 scopus 로고
    • Depletion of brain glutathione is accompanied by impaired mitochondrial function and decreased N-acetyl aspartate concentration
    • Heales SJ, Davies SE, Bates TE et al (1995) Depletion of brain glutathione is accompanied by impaired mitochondrial function and decreased N-acetyl aspartate concentration. Neurochem Res 20:31-38
    • (1995) Neurochem Res , vol.20 , pp. 31-38
    • Heales, S.J.1    Davies, S.E.2    Bates, T.E.3
  • 7
    • 0025971259 scopus 로고
    • Glutathione deficiency leads to mitochondrial damage in brain
    • Jain A, Martensson J, Stole E et al (1991) Glutathione deficiency leads to mitochondrial damage in brain. Proc Natl Acad Sci USA 88:1913-1917
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 1913-1917
    • Jain, A.1    Martensson, J.2    Stole, E.3
  • 8
    • 0029910556 scopus 로고    scopus 로고
    • Nitric oxide-mediated mitochondrial damage: A potential neuroprotective role for glutathione
    • Bolanos JP, Heales SJ, Peuchen S et al (1996) Nitric oxide-mediated mitochondrial damage: a potential neuroprotective role for glutathione. Free Radic Biol Med 21:995-1001
    • (1996) Free Radic Biol Med , vol.21 , pp. 995-1001
    • Bolanos, J.P.1    Heales, S.J.2    Peuchen, S.3
  • 9
    • 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
  • 10
    • 13844256359 scopus 로고    scopus 로고
    • Co-culture of neurones with glutathione deficient astrocytes leads to increased neuronal susceptibility to nitric oxide and increased glutamate-cysteine ligase activity
    • Gegg ME, Clark JB, Heales SJ (2005) Co-culture of neurones with glutathione deficient astrocytes leads to increased neuronal susceptibility to nitric oxide and increased glutamate-cysteine ligase activity. Brain Res 1036:1-6
    • (2005) Brain Res , vol.1036 , pp. 1-6
    • Gegg, M.E.1    Clark, J.B.2    Heales, S.J.3
  • 11
    • 0027421350 scopus 로고
    • Maintenance of neuronal glutathione by glial cells
    • Sagara JI, Miura K, Bannai S (1993) Maintenance of neuronal glutathione by glial cells. J Neurochem 61:1672-1676
    • (1993) J Neurochem , vol.61 , pp. 1672-1676
    • Sagara, J.I.1    Miura, K.2    Bannai, S.3
  • 12
    • 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
  • 13
    • 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
  • 14
    • 0036826902 scopus 로고    scopus 로고
    • Preservation of extracellular glutathione by an astrocyte derived factor with properties comparable to extracellular superoxide dismutase
    • Stewart VC, Stone R, Gegg ME et al (2002) Preservation of extracellular glutathione by an astrocyte derived factor with properties comparable to extracellular superoxide dismutase. J Neurochem 83:984-991
    • (2002) J Neurochem , vol.83 , pp. 984-991
    • Stewart, V.C.1    Stone, R.2    Gegg, M.E.3
  • 15
    • 0031004608 scopus 로고    scopus 로고
    • The gamma-glutamyl transpeptidase inhibitor acivicin preserves glutathione released by astroglial cells in culture
    • Dringen R, Kranich O, Hamprecht B (1997) The gamma-glutamyl transpeptidase inhibitor acivicin preserves glutathione released by astroglial cells in culture. Neurochem Res 22:727-733
    • (1997) Neurochem Res , vol.22 , pp. 727-733
    • Dringen, R.1    Kranich, O.2    Hamprecht, B.3
  • 16
    • 0035577287 scopus 로고    scopus 로고
    • Aminopeptidase N mediates the utilization of the GSH precursor CysGly by cultured neurons
    • Dringen R, Gutterer JM, Gros C et al (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
  • 17
    • 0016389670 scopus 로고
    • Interaction of gamma-glutamyl transpeptidase with amino acids, dipeptides, and derivatives and analogs of glutathione
    • Tate SS, Meister A (1974) Interaction of gamma-glutamyl transpeptidase with amino acids, dipeptides, and derivatives and analogs of glutathione. J Biol Chem 249:7593-7602
    • (1974) J Biol Chem , vol.249 , pp. 7593-7602
    • Tate, S.S.1    Meister, A.2
  • 18
    • 0018801102 scopus 로고
    • Comparison of the hydrolytic and transfer activities of rat renal gamma-glutamyltranspeptidase
    • McIntyre TM, Curthoys NP (1979) Comparison of the hydrolytic and transfer activities of rat renal gamma-glutamyltranspeptidase. J Biol Chem 254:6499-6504
    • (1979) J Biol Chem , vol.254 , pp. 6499-6504
    • McIntyre, T.M.1    Curthoys, N.P.2
  • 19
    • 0029957584 scopus 로고    scopus 로고
    • Catalytic metal ions and the loss of reduced glutathione from University of Wisconsin preservation solution
    • Evans PJ, Tredger JM, Dunne JB et al (1996) Catalytic metal ions and the loss of reduced glutathione from University of Wisconsin preservation solution. Transplantation 62:1046-1049
    • (1996) Transplantation , vol.62 , pp. 1046-1049
    • Evans, P.J.1    Tredger, J.M.2    Dunne, J.B.3
  • 20
    • 0034810075 scopus 로고    scopus 로고
    • Oxidation and generation of hydrogen peroxide by thiol compounds in commonly used cell culture media
    • Hua LL, Halliwell B (2001) Oxidation and generation of hydrogen peroxide by thiol compounds in commonly used cell culture media. Biochem Biophys Res Commun 286:991-994
    • (2001) Biochem Biophys Res Commun , vol.286 , pp. 991-994
    • Hua, L.L.1    Halliwell, B.2
  • 21
    • 0031842534 scopus 로고    scopus 로고
    • Mechanism of copper-catalyzed oxidation of glutathione
    • Kachur AV, Koch CJ, Biaglow JE (1998) Mechanism of copper-catalyzed oxidation of glutathione. Free Radic Res 28:259-269
    • (1998) Free Radic Res , vol.28 , pp. 259-269
    • Kachur, A.V.1    Koch, C.J.2    Biaglow, J.E.3
  • 22
    • 0035873398 scopus 로고    scopus 로고
    • Pyruvate released by astrocytes protects neurons from copper-catalyzed cysteine neurotoxicity
    • Wang XF, Cynader MS (2001) Pyruvate released by astrocytes protects neurons from copper-catalyzed cysteine neurotoxicity. J Neurosci 21:3322-3331
    • (2001) J Neurosci , vol.21 , pp. 3322-3331
    • Wang, X.F.1    Cynader, M.S.2
  • 23
    • 0029883795 scopus 로고    scopus 로고
    • Copper biochemistry and molecular biology
    • Linder MC, Hazegh-Azam M (1996) Copper biochemistry and molecular biology. Am J Clin Nutr 63:797S-811S
    • (1996) Am J Clin Nutr , vol.63
    • Linder, M.C.1    Hazegh-Azam, M.2
  • 25
    • 0031050483 scopus 로고    scopus 로고
    • Copper transport and its alterations in Menkes and Wilson diseases
    • DiDonato M, Sarkar B (1997) Copper transport and its alterations in Menkes and Wilson diseases. Biochim Biophys Acta 1360:3-16
    • (1997) Biochim Biophys Acta , vol.1360 , pp. 3-16
    • Didonato, M.1    Sarkar, B.2
  • 26
    • 33748893007 scopus 로고    scopus 로고
    • Relationship between oxidative stress and antioxidant systems in the liver of patients with Wilson disease: Hepatic manifestation in Wilson disease as a consequence of augmented oxidative stress
    • Nagasaka H, Inoue I, Inui A et al (2006) Relationship between oxidative stress and antioxidant systems in the liver of patients with Wilson disease: hepatic manifestation in Wilson disease as a consequence of augmented oxidative stress. Pediatr Res 60:472-477
    • (2006) Pediatr Res , vol.60 , pp. 472-477
    • Nagasaka, H.1    Inoue, I.2    Inui, A.3
  • 27
    • 0041589350 scopus 로고    scopus 로고
    • Proteomic analysis of astrocytic secretion in the mouse. Comparison with the cerebrospinal fluid proteome
    • Lafon-Cazal M, Adjali O, Galeotti N et al (2003) Proteomic analysis of astrocytic secretion in the mouse. Comparison with the cerebrospinal fluid proteome. J Biol Chem 278:24438-24448
    • (2003) J Biol Chem , vol.278 , pp. 24438-24448
    • Lafon-Cazal, M.1    Adjali, O.2    Galeotti, N.3
  • 28
    • 0023259759 scopus 로고
    • Glucose autoxidation and protein modification. the potential role of 'autoxidative glycosylation' in diabetes
    • Wolff SP, Dean RT (1987) Glucose autoxidation and protein modification. The potential role of 'autoxidative glycosylation' in diabetes. Biochem J 245:243-250
    • (1987) Biochem J , vol.245 , pp. 243-250
    • Wolff, S.P.1    Dean, R.T.2
  • 29
    • 0037443602 scopus 로고    scopus 로고
    • Neurotoxicity from glutathione depletion is dependent on extracellular trace copper
    • White AR, Cappai R (2003) Neurotoxicity from glutathione depletion is dependent on extracellular trace copper. J Neurosci Res 71:889-897
    • (2003) J Neurosci Res , vol.71 , pp. 889-897
    • White, A.R.1    Cappai, R.2
  • 30
    • 0031808935 scopus 로고    scopus 로고
    • Detoxification of exogenous hydrogen peroxide and organic hydroperoxides by cultured astroglial cells assessed by microtiter plate assay
    • Dringen R, Kussmaul L, Hamprecht B (1998) Detoxification of exogenous hydrogen peroxide and organic hydroperoxides by cultured astroglial cells assessed by microtiter plate assay. Brain Res Protoc 2:223-228
    • (1998) Brain Res Protoc , vol.2 , pp. 223-228
    • Dringen, R.1    Kussmaul, L.2    Hamprecht, B.3
  • 31
    • 0024557734 scopus 로고
    • Transition metals, ferritin, glutathione, and ascorbic acid in parkinsonian brains
    • Riederer P, Sofic E, Rausch WD et al (1989) Transition metals, ferritin, glutathione, and ascorbic acid in parkinsonian brains. J Neurochem 52:515-520
    • (1989) J Neurochem , vol.52 , pp. 515-520
    • Riederer, P.1    Sofic, E.2    Rausch, W.D.3
  • 32
    • 0036667917 scopus 로고    scopus 로고
    • Quenching of bathocuproine disulfonate fluorescence by Cu(I) as a basis for copper quantification
    • Rapisarda VA, Volentini SI, Farias RN et al (2002) Quenching of bathocuproine disulfonate fluorescence by Cu(I) as a basis for copper quantification. Anal Biochem 307:105-109
    • (2002) Anal Biochem , vol.307 , pp. 105-109
    • Rapisarda, V.A.1    Volentini, S.I.2    Farias, R.N.3
  • 33
    • 0142125716 scopus 로고    scopus 로고
    • Factors affecting the ascorbate- and phenolic-dependent generation of hydrogen peroxide in Dulbecco's Modified Eagles Medium
    • Wee LM, Long LH, Whiteman M et al (2003) Factors affecting the ascorbate- and phenolic-dependent generation of hydrogen peroxide in Dulbecco's Modified Eagles Medium. Free Radic Res 37:1123-1130
    • (2003) Free Radic Res , vol.37 , pp. 1123-1130
    • Wee, L.M.1    Long, L.H.2    Whiteman, M.3
  • 34
    • 0033952388 scopus 로고    scopus 로고
    • Glutamate stimulates ascorbate transport by astrocytes
    • Wilson JX, Peters CE, Sitar SM et al (2000) Glutamate stimulates ascorbate transport by astrocytes. Brain Res 858:61-66
    • (2000) Brain Res , vol.858 , pp. 61-66
    • Wilson, J.X.1    Peters, C.E.2    Sitar, S.M.3
  • 35
    • 0029992521 scopus 로고    scopus 로고
    • The effect of ascorbate and ubiquinone supplementation on plasma and CSF total antioxidant capacity
    • Lonnrot K, Metsa-Ketela T, Molnar G et al (1996) The effect of ascorbate and ubiquinone supplementation on plasma and CSF total antioxidant capacity. Free Radic Biol Med 21:211-217
    • (1996) Free Radic Biol Med , vol.21 , pp. 211-217
    • Lonnrot, K.1    Metsa-Ketela, T.2    Molnar, G.3
  • 36
    • 0038636003 scopus 로고    scopus 로고
    • Glutathione pathways in the brain
    • Dringen R, Hirrlinger J (2003) Glutathione pathways in the brain. Biol Chem 384:505-516
    • (2003) Biol Chem , vol.384 , pp. 505-516
    • Dringen, R.1    Hirrlinger, J.2
  • 37
    • 0031569806 scopus 로고    scopus 로고
    • Essential trace element alterations in amyotrophic lateral sclerosis
    • Kapaki E, Zournas C, Kanias G et al (1997) Essential trace element alterations in amyotrophic lateral sclerosis. J Neurol Sci 147:171-175
    • (1997) J Neurol Sci , vol.147 , pp. 171-175
    • Kapaki, E.1    Zournas, C.2    Kanias, G.3
  • 38
    • 14444272313 scopus 로고    scopus 로고
    • Cerebrospinal fluid levels of transition metals in patients with Parkinson's disease
    • Jimenez-Jimenez FJ, Molina JA, Aguilar MV et al (1998) Cerebrospinal fluid levels of transition metals in patients with Parkinson's disease. J Neural Transm 105:497-505
    • (1998) J Neural Transm , vol.105 , pp. 497-505
    • Jimenez-Jimenez, F.J.1    Molina, J.A.2    Aguilar, M.V.3
  • 39
    • 0034105324 scopus 로고    scopus 로고
    • CSF copper concentrations, blood-brain barrier function, and coeruloplasmin synthesis during the treatment of Wilson's disease
    • Stuerenburg HJ (2000) CSF copper concentrations, blood-brain barrier function, and coeruloplasmin synthesis during the treatment of Wilson's disease. J Neural Transm 107:321-329
    • (2000) J Neural Transm , vol.107 , pp. 321-329
    • Stuerenburg, H.J.1
  • 40
    • 0021346169 scopus 로고
    • Copper-phenanthroline-induced site-specific oxygen-radical damage to DNA. Detection of loosely bound trace copper in biological fluids
    • Gutteridge JM (1984) Copper-phenanthroline-induced site-specific oxygen-radical damage to DNA. Detection of loosely bound trace copper in biological fluids. Biochem J 218:983-985
    • (1984) Biochem J , vol.218 , pp. 983-985
    • Gutteridge, J.M.1
  • 41
    • 0023241926 scopus 로고
    • Non-caeruloplasmin-bound copper ('phenanthroline copper') is not detectable in fresh serum or synovial fluid from patients with rheumatoid arthritis
    • Winyard PG, Pall H, Lunec J et al (1987) Non-caeruloplasmin-bound copper ('phenanthroline copper') is not detectable in fresh serum or synovial fluid from patients with rheumatoid arthritis. Biochem J 247:245-246
    • (1987) Biochem J , vol.247 , pp. 245-246
    • Winyard, P.G.1    Pall, H.2    Lunec, J.3
  • 42
    • 29044438902 scopus 로고    scopus 로고
    • The crucial role of metal ions in neurodegeneration: The basis for a promising therapeutic strategy
    • Gaeta A, Hider RC (2005) The crucial role of metal ions in neurodegeneration: the basis for a promising therapeutic strategy. Br J Pharmacol 146:1041-1059
    • (2005) Br J Pharmacol , vol.146 , pp. 1041-1059
    • Gaeta, A.1    Hider, R.C.2
  • 43
    • 0023237555 scopus 로고
    • Raised cerebrospinal-fluid copper concentration in Parkinson's disease
    • Pall HS, Williams AC, Blake DR et al (1987) Raised cerebrospinal-fluid copper concentration in Parkinson's disease. Lancet 2:238-241
    • (1987) Lancet , vol.2 , pp. 238-241
    • Pall, H.S.1    Williams, A.C.2    Blake, D.R.3
  • 44
    • 0026041595 scopus 로고
    • Metals and trace elements in plasma and cerebrospinal fluid in normal aging and Alzheimer's disease
    • Basun H, Forssell LG, Wetterberg L et al (1991) Metals and trace elements in plasma and cerebrospinal fluid in normal aging and Alzheimer's disease. J Neural Transm Park Dis Dement Sect 3:231-258
    • (1991) J Neural Transm Park Dis Dement Sect , vol.3 , pp. 231-258
    • Basun, H.1    Forssell, L.G.2    Wetterberg, L.3
  • 45
    • 1842524044 scopus 로고    scopus 로고
    • Role of the prion protein in copper turnover in astrocytes
    • Brown DR (2004) Role of the prion protein in copper turnover in astrocytes. Neurobiol Dis 15:534-543
    • (2004) Neurobiol Dis , vol.15 , pp. 534-543
    • Brown, D.R.1
  • 46
    • 0031444294 scopus 로고    scopus 로고
    • The cellular prion protein binds copper in vivo
    • Brown DR, Qin K, Herms JW et al (1997) The cellular prion protein binds copper in vivo. Nature 390:684-687
    • (1997) Nature , vol.390 , pp. 684-687
    • Brown, D.R.1    Qin, K.2    Herms, J.W.3
  • 47
    • 3142720757 scopus 로고    scopus 로고
    • Biological inorganic and bioinorganic chemistry of neurodegeneration based on prion and Alzheimer diseases
    • Brown DR, Kozlowski H (2004) Biological inorganic and bioinorganic chemistry of neurodegeneration based on prion and Alzheimer diseases. Dalton Trans 1907-1917
    • (2004) Dalton Trans , pp. 1907-1917
    • Brown, D.R.1    Kozlowski, H.2
  • 48
    • 0033430087 scopus 로고    scopus 로고
    • Copper inhibits beta-amyloid production and stimulates the non-amyloidogenic pathway of amyloid-precursor-protein secretion
    • Pt 2
    • Borchardt T, Camakaris J, Cappai R et al (1999) Copper inhibits beta-amyloid production and stimulates the non-amyloidogenic pathway of amyloid-precursor-protein secretion. Biochem J 344(Pt 2):461-467
    • (1999) Biochem J , vol.344 , pp. 461-467
    • Borchardt, T.1    Camakaris, J.2    Cappai, R.3
  • 49
    • 0028801746 scopus 로고
    • Copper incorporation into ceruloplasmin in rat livers
    • Terada K, Kawarada Y, Miura N et al (1995) Copper incorporation into ceruloplasmin in rat livers. Biochim Biophys Acta 1270:58-62
    • (1995) Biochim Biophys Acta , vol.1270 , pp. 58-62
    • Terada, K.1    Kawarada, Y.2    Miura, N.3
  • 50
    • 51149212381 scopus 로고
    • Oxidation of -diketones and -keto-acids by hydrogen peroxide
    • Bunton CA (1949) Oxidation of -diketones and -keto-acids by hydrogen peroxide. Nature 163:444
    • (1949) Nature , vol.163 , pp. 444
    • Bunton, C.A.1
  • 51
    • 0347916885 scopus 로고    scopus 로고
    • Peroxiredoxins in antioxidant defense and redox regulation
    • Flohe L, Budde H, Hofmann B (2003) Peroxiredoxins in antioxidant defense and redox regulation. Biofactors 19:3-10
    • (2003) Biofactors , vol.19 , pp. 3-10
    • Flohe, L.1    Budde, H.2    Hofmann, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.