메뉴 건너뛰기




Volumn 62, Issue 4, 2008, Pages 236-249

Glutathione and Parkinson's disease: Is this the elephant in the room?

Author keywords

Glutathione; Parkinson's disease; Therapeutics

Indexed keywords

AMINO ACID; DNA; GLUTAMATE RECEPTOR; GLUTATHIONE; HYDROGEN PEROXIDE; LIPID; PROTEIN;

EID: 43049145863     PISSN: 07533322     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biopha.2008.01.017     Document Type: Article
Times cited : (174)

References (137)
  • 2
    • 34447289622 scopus 로고    scopus 로고
    • Pathogenic mutations in Parkinson disease
    • Tan E.K., and Skipper L.M. Pathogenic mutations in Parkinson disease. Hum Mutat 28 7 (2007) 641
    • (2007) Hum Mutat , vol.28 , Issue.7 , pp. 641
    • Tan, E.K.1    Skipper, L.M.2
  • 3
    • 33750459730 scopus 로고    scopus 로고
    • Parkinsonism genes: culprits and clues
    • Abeliovich A., and Beal M.F. Parkinsonism genes: culprits and clues. J Neurochem 99 4 (2006) 1062
    • (2006) J Neurochem , vol.99 , Issue.4 , pp. 1062
    • Abeliovich, A.1    Beal, M.F.2
  • 4
    • 0027952849 scopus 로고
    • Increased levels of lipid hydroperoxides in the parkinsonian substantia nigra: an HPLC and ESR study
    • Dexter D.T., Holley A.E., Flitter W.D., Slater T.F., Wells F.R., Daniel S.E., et al. Increased levels of lipid hydroperoxides in the parkinsonian substantia nigra: an HPLC and ESR study. Mov Disord 9 (1994) 92
    • (1994) Mov Disord , vol.9 , pp. 92
    • Dexter, D.T.1    Holley, A.E.2    Flitter, W.D.3    Slater, T.F.4    Wells, F.R.5    Daniel, S.E.6
  • 5
    • 0030805622 scopus 로고    scopus 로고
    • A generalized increase in protein carbonyls in the brain in Parkinson's disease but not incidental Lewy body disease
    • Alam Z.I., Daniel S.E., Lees A.J., Marsden C.D., Jenner P., and Halliwell B. A generalized increase in protein carbonyls in the brain in Parkinson's disease but not incidental Lewy body disease. J Neurochem 69 (1997) 1326
    • (1997) J Neurochem , vol.69 , pp. 1326
    • Alam, Z.I.1    Daniel, S.E.2    Lees, A.J.3    Marsden, C.D.4    Jenner, P.5    Halliwell, B.6
  • 6
    • 0036570159 scopus 로고    scopus 로고
    • Oxidatively modified proteins in aging and disease
    • Beal M.F. Oxidatively modified proteins in aging and disease. Free Radic Biol Med 32 9 (2002) 797
    • (2002) Free Radic Biol Med , vol.32 , Issue.9 , pp. 797
    • Beal, M.F.1
  • 7
    • 0030878073 scopus 로고    scopus 로고
    • Oxidative DNA damage in the parkinsonian brain: a selective increase in 8-hydroxy-guanine in substantia nigra?
    • Alam Z.I., Jenner A., Daniel S.E., Lees A.J., Cairns N., Marsden C.D., et al. Oxidative DNA damage in the parkinsonian brain: a selective increase in 8-hydroxy-guanine in substantia nigra?. J Neurochem 69 (1997) 1196
    • (1997) J Neurochem , vol.69 , pp. 1196
    • Alam, Z.I.1    Jenner, A.2    Daniel, S.E.3    Lees, A.J.4    Cairns, N.5    Marsden, C.D.6
  • 8
    • 0000232034 scopus 로고
    • A marker of oxyradical-mediated DNA damage [8-hydroxy-2′-deoxyguanosine] is increased in nigrostriatum of Parkinson's disease brain
    • Sanchez-Ramos J., Overvik E., and Ames B.N. A marker of oxyradical-mediated DNA damage [8-hydroxy-2′-deoxyguanosine] is increased in nigrostriatum of Parkinson's disease brain. Neurodegeneration 3 (1994) 197
    • (1994) Neurodegeneration , vol.3 , pp. 197
    • Sanchez-Ramos, J.1    Overvik, E.2    Ames, B.N.3
  • 9
    • 0024848034 scopus 로고
    • Abnormalities of the electron transport chain in idiopathic Parkinson's disease
    • Parker W.D., Boyson S.J., and Parks J.K. Abnormalities of the electron transport chain in idiopathic Parkinson's disease. Ann Neurol 26 (1989) 719
    • (1989) Ann Neurol , vol.26 , pp. 719
    • Parker, W.D.1    Boyson, S.J.2    Parks, J.K.3
  • 11
    • 0029050583 scopus 로고
    • Low platelet mitochondrial complex I and complex II/III activity in early untreated Parkinson's Disease
    • Haas R.H., Nasirian F., Nakano K., Ward D., Pay R.N., Hill R., et al. Low platelet mitochondrial complex I and complex II/III activity in early untreated Parkinson's Disease. Ann Neurol 37 (1995) 714
    • (1995) Ann Neurol , vol.37 , pp. 714
    • Haas, R.H.1    Nasirian, F.2    Nakano, K.3    Ward, D.4    Pay, R.N.5    Hill, R.6
  • 12
    • 0028176592 scopus 로고
    • An immunohistochemical study on αketoglutarate dehydrogenase complex in Parkinson's disease
    • Mizuno Y., Matsuda S., Yoshino H., Mori H., Hattori N., and Ikebe S.I. An immunohistochemical study on αketoglutarate dehydrogenase complex in Parkinson's disease. Ann Neurol 35 (1994) 204
    • (1994) Ann Neurol , vol.35 , pp. 204
    • Mizuno, Y.1    Matsuda, S.2    Yoshino, H.3    Mori, H.4    Hattori, N.5    Ikebe, S.I.6
  • 13
    • 0027750939 scopus 로고
    • Electron transfer complexes I and IV of platelets are abnormal in Parkinson's disease but normal in Parkinson-plus syndromes
    • Benecke R., Strumper P., and Weiss H. Electron transfer complexes I and IV of platelets are abnormal in Parkinson's disease but normal in Parkinson-plus syndromes. Brain 116 (1993) 1451
    • (1993) Brain , vol.116 , pp. 1451
    • Benecke, R.1    Strumper, P.2    Weiss, H.3
  • 15
    • 0020308323 scopus 로고
    • Parkinson's disease: a disorder due to nigral glutathione deficiency?
    • Perry T., Godin D.V., and Hansen S. Parkinson's disease: a disorder due to nigral glutathione deficiency?. Neurosci Lett 33 (1982) 305
    • (1982) Neurosci Lett , vol.33 , pp. 305
    • Perry, T.1    Godin, D.V.2    Hansen, S.3
  • 16
    • 0026635461 scopus 로고
    • Oxidative stress as a cause of nigral cell death in Parkinson's disease and incidental Lewy body disease
    • Jenner P., Dexter D.T., Sian J., Schapira A.H.V., and Marsden C.D. Oxidative stress as a cause of nigral cell death in Parkinson's disease and incidental Lewy body disease. Ann Neurol 32 (1992) S82
    • (1992) Ann Neurol , vol.32
    • Jenner, P.1    Dexter, D.T.2    Sian, J.3    Schapira, A.H.V.4    Marsden, C.D.5
  • 18
    • 0030724621 scopus 로고    scopus 로고
    • Alterations in the distribution of glutathione in the substantia nigra in Parkinson's disease
    • Pearce R.K.B., Owen A., Daniel S., Jenner P., and Marsden C.D. Alterations in the distribution of glutathione in the substantia nigra in Parkinson's disease. J Neural Transm 104 (1997) 661
    • (1997) J Neural Transm , vol.104 , pp. 661
    • Pearce, R.K.B.1    Owen, A.2    Daniel, S.3    Jenner, P.4    Marsden, C.D.5
  • 19
    • 0030792637 scopus 로고    scopus 로고
    • Multiple roles of glutathione in the central nervous system
    • Cooper A.J.L., and Kristal B.S. Multiple roles of glutathione in the central nervous system. Biol Chem 378 (2007) 793
    • (2007) Biol Chem , vol.378 , pp. 793
    • Cooper, A.J.L.1    Kristal, B.S.2
  • 20
    • 0343131929 scopus 로고    scopus 로고
    • Differential compartmentalization of brain ascorbate and glutathione between neurons and glia
    • Rice M.E., and Russo-Menna I. Differential compartmentalization of brain ascorbate and glutathione between neurons and glia. Neuroscience 82 4 (1998) 1213
    • (1998) Neuroscience , vol.82 , Issue.4 , pp. 1213
    • Rice, M.E.1    Russo-Menna, I.2
  • 21
    • 0026030924 scopus 로고
    • Cellular and regional distribution of reduced glutathione in the nervous system of the rat: histochemical localization by mercury orange and o-pthaldialdehyde-induced histofluorescence
    • Philbert M.A., Beiswanger C.M., Waters D.K., Reuhl K.R., and Lowndes H.E. Cellular and regional distribution of reduced glutathione in the nervous system of the rat: histochemical localization by mercury orange and o-pthaldialdehyde-induced histofluorescence. Toxicol Appl Pharmacol 107 (1991) 215
    • (1991) Toxicol Appl Pharmacol , vol.107 , pp. 215
    • Philbert, M.A.1    Beiswanger, C.M.2    Waters, D.K.3    Reuhl, K.R.4    Lowndes, H.E.5
  • 22
    • 33746423234 scopus 로고
    • Free radicals and thiol compounds - the role of glutathione against free radical toxicity
    • Vina J. (Ed), CRC Press, Boca Raton, FL, USA
    • Saez G.T., Bannister W.H., and Bannister J.V. Free radicals and thiol compounds - the role of glutathione against free radical toxicity. In: Vina J. (Ed). Glutathione: metabolism and physiological functions (1990), CRC Press, Boca Raton, FL, USA 237
    • (1990) Glutathione: metabolism and physiological functions , pp. 237
    • Saez, G.T.1    Bannister, W.H.2    Bannister, J.V.3
  • 23
    • 0028287096 scopus 로고
    • Nitric oxide reacts with intracellular glutathione and activates the hexose monophosphate shunt in human neutrophils: evidence for S-nitrosoglutathione as a bioactive intermediate
    • Clancy R.M., Lavartovsky D., Leszcynska-Piziak J., Yegudin J., and Abramson S.B. Nitric oxide reacts with intracellular glutathione and activates the hexose monophosphate shunt in human neutrophils: evidence for S-nitrosoglutathione as a bioactive intermediate. Proc Natl Acad Sci U S A 91 (1994) 3680
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 3680
    • Clancy, R.M.1    Lavartovsky, D.2    Leszcynska-Piziak, J.3    Yegudin, J.4    Abramson, S.B.5
  • 24
    • 0028114890 scopus 로고
    • The reactions of superoxide with reduced glutathione
    • Winterbourn C.C., and Metodiewa D. The reactions of superoxide with reduced glutathione. Arch Biochem Biophys 314 (1994) 284
    • (1994) Arch Biochem Biophys , vol.314 , pp. 284
    • Winterbourn, C.C.1    Metodiewa, D.2
  • 25
    • 0031418498 scopus 로고    scopus 로고
    • Neurodegenerative disorders in humans: the role of glutathione in oxidative stress-mediated neuronal death
    • Bains J.S., and Shaw C.A. Neurodegenerative disorders in humans: the role of glutathione in oxidative stress-mediated neuronal death. Brain Res Rev 25 (1997) 335
    • (1997) Brain Res Rev , vol.25 , pp. 335
    • Bains, J.S.1    Shaw, C.A.2
  • 26
    • 0029949789 scopus 로고    scopus 로고
    • Glutathione depletion potentiates MPTP and MPP+ toxicity in nigral dopaminergic neurones
    • Wullner U., Loschmann P.A., Schulz J.B., Schmid A., Dringen R., Eblen F., et al. Glutathione depletion potentiates MPTP and MPP+ toxicity in nigral dopaminergic neurones. NeuroReport 7 (1996) 921
    • (1996) NeuroReport , vol.7 , pp. 921
    • Wullner, U.1    Loschmann, P.A.2    Schulz, J.B.3    Schmid, A.4    Dringen, R.5    Eblen, F.6
  • 27
    • 0031025395 scopus 로고    scopus 로고
    • Energy stress-induced dopamine loss in glutathione peroxidase-overexpressing transgenic mice and in glutathione-depleted mesencephalic cultures
    • Zeevalk G.D., Bernard L.P., Albers D.S., Mirochnitchenko O., Nicklas W.J., and Sonsalla P.K. Energy stress-induced dopamine loss in glutathione peroxidase-overexpressing transgenic mice and in glutathione-depleted mesencephalic cultures. J Neurochem 68 (1997) 426
    • (1997) J Neurochem , vol.68 , pp. 426
    • Zeevalk, G.D.1    Bernard, L.P.2    Albers, D.S.3    Mirochnitchenko, O.4    Nicklas, W.J.5    Sonsalla, P.K.6
  • 28
    • 0031929586 scopus 로고    scopus 로고
    • Role of oxidative stress and the glutathione system in loss of dopamine neurons due to impairment of energy metabolism
    • Zeevalk G.D., Bernard L.P., and Nicklas W.J. Role of oxidative stress and the glutathione system in loss of dopamine neurons due to impairment of energy metabolism. J Neurochem 70 (1998) 1421
    • (1998) J Neurochem , vol.70 , pp. 1421
    • Zeevalk, G.D.1    Bernard, L.P.2    Nicklas, W.J.3
  • 29
    • 0033993641 scopus 로고    scopus 로고
    • Mice deficient in cellular glutathione peroxidase show increased vulnerability to malonate, 3-nitopropionic acid, and 1-methyl-4-phenyl-1,2,5,6-tetrahydropyridine
    • Klivenyi P., Andreassen O.A., Ferrante R.J., Dedeoglu A., Mueller G., Lancelot E., et al. Mice deficient in cellular glutathione peroxidase show increased vulnerability to malonate, 3-nitopropionic acid, and 1-methyl-4-phenyl-1,2,5,6-tetrahydropyridine. J Neurosci 20 (2000) 1
    • (2000) J Neurosci , vol.20 , pp. 1
    • Klivenyi, P.1    Andreassen, O.A.2    Ferrante, R.J.3    Dedeoglu, A.4    Mueller, G.5    Lancelot, E.6
  • 30
    • 0032564134 scopus 로고    scopus 로고
    • Parkinson's disease, pesticides, and glutathione transferase polymorphisms
    • Menegon A., Board P.G., Blackburn A.C., Mellick G.D., and LeCouteur D.G. Parkinson's disease, pesticides, and glutathione transferase polymorphisms. Lancet 352 9137 (1998) 1344
    • (1998) Lancet , vol.352 , Issue.9137 , pp. 1344
    • Menegon, A.1    Board, P.G.2    Blackburn, A.C.3    Mellick, G.D.4    LeCouteur, D.G.5
  • 31
  • 34
    • 18844400905 scopus 로고    scopus 로고
    • Peroxiredoxin 6, a 1-cysperoxidredoxin, functions in antioxidant defense and lung phospholipid metabolism
    • Manevich Y., and Fisher A.B. Peroxiredoxin 6, a 1-cysperoxidredoxin, functions in antioxidant defense and lung phospholipid metabolism. Free Radic Biol Med 38 (2005) 1422
    • (2005) Free Radic Biol Med , vol.38 , pp. 1422
    • Manevich, Y.1    Fisher, A.B.2
  • 36
    • 0000326249 scopus 로고
    • Glutathionyl specificity of thioltransferases: mechanistic and physiological implication
    • Packer L.C.E. (Ed), Marcel Decker, New York
    • Mieyal J.J., Srinivasan U., Starke D.W., Gravina S.A., and Mieyal P. Glutathionyl specificity of thioltransferases: mechanistic and physiological implication. In: Packer L.C.E. (Ed). Biothiols in health and disease (1995), Marcel Decker, New York 305
    • (1995) Biothiols in health and disease , pp. 305
    • Mieyal, J.J.1    Srinivasan, U.2    Starke, D.W.3    Gravina, S.A.4    Mieyal, P.5
  • 37
    • 0030296409 scopus 로고    scopus 로고
    • S-glutathiolated hepatocyte proteins and insulin disulfides as substrates for reduction by glutaredoxin, thioredoxin, protein disulfide isomerase and glutathione
    • Jung C.-H., and Thomas J.A. S-glutathiolated hepatocyte proteins and insulin disulfides as substrates for reduction by glutaredoxin, thioredoxin, protein disulfide isomerase and glutathione. Arch Biochem Biophys 335 1 (1996) 61
    • (1996) Arch Biochem Biophys , vol.335 , Issue.1 , pp. 61
    • Jung, C.-H.1    Thomas, J.A.2
  • 38
    • 0032972685 scopus 로고    scopus 로고
    • Rat brain thioltransferase: regional distribution, immunological characterization, and localization by fluorescent in situ hybridization
    • Balijepalli S., Tirumalai P.S., Swamy K.V., Boyd M.R., Mieyal J.J., and Ravindranath V. Rat brain thioltransferase: regional distribution, immunological characterization, and localization by fluorescent in situ hybridization. J Neurochem 72 (1999) 1170
    • (1999) J Neurochem , vol.72 , pp. 1170
    • Balijepalli, S.1    Tirumalai, P.S.2    Swamy, K.V.3    Boyd, M.R.4    Mieyal, J.J.5    Ravindranath, V.6
  • 39
    • 0036768195 scopus 로고    scopus 로고
    • Functional glutaredoxin [thioltransferase] activity in rat brain and liver mitochondria
    • Ehrhart J., Gluck M., Mieyal J., and Zeevalk G.D. Functional glutaredoxin [thioltransferase] activity in rat brain and liver mitochondria. Parkinsonism Relat Disord 8 6 (2002) 395
    • (2002) Parkinsonism Relat Disord , vol.8 , Issue.6 , pp. 395
    • Ehrhart, J.1    Gluck, M.2    Mieyal, J.3    Zeevalk, G.D.4
  • 40
    • 0034727890 scopus 로고    scopus 로고
    • Human brain thioltransferase: constitutive expression and localization by fluorescence in situ hybridization
    • Balijepalli S., Boyd M.R., and Ravindranath V. Human brain thioltransferase: constitutive expression and localization by fluorescence in situ hybridization. Brain Res 85 1-2 (2000) 123
    • (2000) Brain Res , vol.85 , Issue.1-2 , pp. 123
    • Balijepalli, S.1    Boyd, M.R.2    Ravindranath, V.3
  • 41
    • 0025082330 scopus 로고
    • Mammalian thioltransferase [glutaredoxin] and protein disulfide isomerase have dehydroascorbate reductase activity
    • Wells W.W., Xu D.P., Yang Y., and Rocque P.A. Mammalian thioltransferase [glutaredoxin] and protein disulfide isomerase have dehydroascorbate reductase activity. J Biol Chem 265 26 (1990) 15361
    • (1990) J Biol Chem , vol.265 , Issue.26 , pp. 15361
    • Wells, W.W.1    Xu, D.P.2    Yang, Y.3    Rocque, P.A.4
  • 42
    • 0347358043 scopus 로고    scopus 로고
    • Thioltransferase mediated ascorbate recycling in human lens epithelial cells
    • Fernando M.R., Satake M., Monnier V.M., and Lou M.F. Thioltransferase mediated ascorbate recycling in human lens epithelial cells. Invest Ophthalmol Vis Sci 45 1 (2004) 230
    • (2004) Invest Ophthalmol Vis Sci , vol.45 , Issue.1 , pp. 230
    • Fernando, M.R.1    Satake, M.2    Monnier, V.M.3    Lou, M.F.4
  • 43
    • 0034975804 scopus 로고    scopus 로고
    • Hydrogen peroxide removal and glutathione mixed disulfide formation during metabolic inhibition in mesencephalic cultures
    • Ehrhart J., and Zeevalk G.D. Hydrogen peroxide removal and glutathione mixed disulfide formation during metabolic inhibition in mesencephalic cultures. J Neurochem 77 (2001) 1496
    • (2001) J Neurochem , vol.77 , pp. 1496
    • Ehrhart, J.1    Zeevalk, G.D.2
  • 44
    • 0141767061 scopus 로고    scopus 로고
    • Cooperative interaction between ascorbate and glutathione during mitochondrial impairment in mesencephalic cultures
    • Ehrhart J., and Zeevalk G.D. Cooperative interaction between ascorbate and glutathione during mitochondrial impairment in mesencephalic cultures. J Neurochem 86 (2003) 1487
    • (2003) J Neurochem , vol.86 , pp. 1487
    • Ehrhart, J.1    Zeevalk, G.D.2
  • 45
    • 0037713388 scopus 로고    scopus 로고
    • Glutathione and ascorbate: role in protein-glutathione-mixed disulfide formation during oxidative stress and potential relevance to Parkinson's disease
    • Zeevalk G.D., Bernard L.P., and Ehrhart J. Glutathione and ascorbate: role in protein-glutathione-mixed disulfide formation during oxidative stress and potential relevance to Parkinson's disease. Ann N Y Acad Sci 991 (2003) 342
    • (2003) Ann N Y Acad Sci , vol.991 , pp. 342
    • Zeevalk, G.D.1    Bernard, L.P.2    Ehrhart, J.3
  • 46
    • 0035930608 scopus 로고    scopus 로고
    • Reversible glutathionylation regulates actin polymerization in A431 cells
    • Wang J., Boja E.S., Tan W.H., Tekle E., Fales H.M., English S., et al. Reversible glutathionylation regulates actin polymerization in A431 cells. J Biol Chem 276 (2001) 47763
    • (2001) J Biol Chem , vol.276 , pp. 47763
    • Wang, J.1    Boja, E.S.2    Tan, W.H.3    Tekle, E.4    Fales, H.M.5    English, S.6
  • 47
    • 0038015010 scopus 로고    scopus 로고
    • Glutathione-thiyl radical scavenging and transferase properties of human glutaredoxin [thioltransferase] - potential role in redox signal transduction
    • Starke D.W., Chock P.B., and Mieyal J.J. Glutathione-thiyl radical scavenging and transferase properties of human glutaredoxin [thioltransferase] - potential role in redox signal transduction. J Biol Chem 278 17 (2003) 14607
    • (2003) J Biol Chem , vol.278 , Issue.17 , pp. 14607
    • Starke, D.W.1    Chock, P.B.2    Mieyal, J.J.3
  • 49
    • 0034672943 scopus 로고    scopus 로고
    • Metabolism and functions of glutathione in brain
    • Dringen R. Metabolism and functions of glutathione in brain. Prog Neurobiol 62 (2000) 649
    • (2000) Prog Neurobiol , vol.62 , pp. 649
    • Dringen, R.1
  • 50
    • 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 T.K., Nedergaard M., Preuss A., Gelbard A.S., Perumal A.S., and Cooper A.J.L. 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 (1994) 45
    • (1994) J Neurochem , vol.62 , pp. 45
    • Makar, T.K.1    Nedergaard, M.2    Preuss, A.3    Gelbard, A.S.4    Perumal, A.S.5    Cooper, A.J.L.6
  • 51
    • 0032126145 scopus 로고    scopus 로고
    • Expression and purification of human gamma-glutamylcysteine synthetase
    • Misra I., and Griffith O.W. Expression and purification of human gamma-glutamylcysteine synthetase. Protein Expr Purif 13 (1998) 268
    • (1998) Protein Expr Purif , vol.13 , pp. 268
    • Misra, I.1    Griffith, O.W.2
  • 52
    • 0019506537 scopus 로고
    • Immunocytochemical localization of gamma-glutamyl transpeptidase in the rat CNS
    • Shine H.D., and Haber B. Immunocytochemical localization of gamma-glutamyl transpeptidase in the rat CNS. Brain Res 217 (1981) 339
    • (1981) Brain Res , vol.217 , pp. 339
    • Shine, H.D.1    Haber, B.2
  • 53
    • 0028982312 scopus 로고
    • Glutathione-S-transferases and gamma-glutamyl transpeptidase in the rat nervous system: a basis for differential susceptibility to neurotoxicants
    • Philbert M.A., Beiswanger C.M., Manson M.M., Green J.A., Novak R.F., Primiano T., et al. Glutathione-S-transferases and gamma-glutamyl transpeptidase in the rat nervous system: a basis for differential susceptibility to neurotoxicants. Neurotoxicology 16 (1995) 349
    • (1995) Neurotoxicology , vol.16 , pp. 349
    • Philbert, M.A.1    Beiswanger, C.M.2    Manson, M.M.3    Green, J.A.4    Novak, R.F.5    Primiano, T.6
  • 55
    • 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., and Hamprecht B. Synthesis of the antioxidant glutathione in neurons: supply by astrocytes of CysGly as precursor for neuronal glutathione. J Neurosci 19 (1999) 562
    • (1999) J Neurosci , vol.19 , pp. 562
    • Dringen, R.1    Pfeiffer, B.2    Hamprecht, B.3
  • 56
    • 0027421350 scopus 로고
    • Maintenance of neuronal glutathione by glial cells
    • Sagara J., Miura K., and Bannai S. Maintenance of neuronal glutathione by glial cells. J Neurochem 61 (1993) 1677
    • (1993) J Neurochem , vol.61 , pp. 1677
    • Sagara, J.1    Miura, K.2    Bannai, S.3
  • 57
    • 0027489346 scopus 로고
    • Cystine uptake and glutathione level in fetal brain cells in primary culture and in suspension
    • Sagara J., Miura K., and Bannai S. Cystine uptake and glutathione level in fetal brain cells in primary culture and in suspension. J Neurochem 61 (1993) 1667
    • (1993) J Neurochem , vol.61 , pp. 1667
    • Sagara, J.1    Miura, K.2    Bannai, S.3
  • 58
    • 0029988384 scopus 로고    scopus 로고
    • Glutathione efflux from cultured astrocytes
    • Sagara J., Makino N., and Bannai S. Glutathione efflux from cultured astrocytes. J Neurochem 66 (1996) 1876
    • (1996) J Neurochem , vol.66 , pp. 1876
    • Sagara, J.1    Makino, N.2    Bannai, S.3
  • 60
    • 0031004608 scopus 로고    scopus 로고
    • The gamma-glutamyl transpeptidase inhibitor acivicin preserves glutathione released by astroglial cells in culture
    • Dringen R., Kranich O., and Hamprecht B. The gamma-glutamyl transpeptidase inhibitor acivicin preserves glutathione released by astroglial cells in culture. Neurochem Res 22 6 (1997) 727
    • (1997) Neurochem Res , vol.22 , Issue.6 , pp. 727
    • Dringen, R.1    Kranich, O.2    Hamprecht, B.3
  • 61
    • 0030749694 scopus 로고    scopus 로고
    • Use of dipeptides for the synthesis of glutathione by astroglia-rich primary cultures
    • Dringen R., Kranich O., Loschmann P.A., and Hamprecht B. Use of dipeptides for the synthesis of glutathione by astroglia-rich primary cultures. J Neurochem 69 (1997) 868
    • (1997) J Neurochem , vol.69 , pp. 868
    • Dringen, R.1    Kranich, O.2    Loschmann, P.A.3    Hamprecht, B.4
  • 62
    • 0022553605 scopus 로고
    • Idiopathic Parkinson's disease, progressive supranuclear palsy and glutathione metabolism in the substantia nigra of patients
    • Perry T.L., and Yong V.W. Idiopathic Parkinson's disease, progressive supranuclear palsy and glutathione metabolism in the substantia nigra of patients. Neurosci Lett 67 (1986) 269
    • (1986) Neurosci Lett , vol.67 , pp. 269
    • Perry, T.L.1    Yong, V.W.2
  • 63
    • 0028075410 scopus 로고
    • Alterations in glutathione levels in Parkinson's disease and other neurodegenerative disorders affecting the basal ganglia
    • Sian J., Dexter D.T., Lees A.J., Daniel S., Agid Y., Javoy-Agid F., et al. Alterations in glutathione levels in Parkinson's disease and other neurodegenerative disorders affecting the basal ganglia. Ann Neurol 36 (1994) 348
    • (1994) Ann Neurol , vol.36 , pp. 348
    • Sian, J.1    Dexter, D.T.2    Lees, A.J.3    Daniel, S.4    Agid, Y.5    Javoy-Agid, F.6
  • 64
    • 0026644192 scopus 로고
    • Reduced and oxidized glutathione in the substantia nigra of patients with Parkinson's disease
    • Sofic E., Lange K.W., Jellinger K., and Riederer P. Reduced and oxidized glutathione in the substantia nigra of patients with Parkinson's disease. Neurosci Lett 142 (1992) 128
    • (1992) Neurosci Lett , vol.142 , pp. 128
    • Sofic, E.1    Lange, K.W.2    Jellinger, K.3    Riederer, P.4
  • 66
    • 0023898945 scopus 로고
    • The relevance of the Lewy body to the pathogenesis of idiopathic Parkinson's disease
    • Gibb W.R.G., and Lees A.J. The relevance of the Lewy body to the pathogenesis of idiopathic Parkinson's disease. J Neurol Neurosurg Psychiatr 51 6 (1988) 745
    • (1988) J Neurol Neurosurg Psychiatr , vol.51 , Issue.6 , pp. 745
    • Gibb, W.R.G.1    Lees, A.J.2
  • 67
    • 0037378026 scopus 로고    scopus 로고
    • Oxidative stress in Parkinson's disease
    • Jenner P. Oxidative stress in Parkinson's disease. Ann Neurol 53 (2003) S26
    • (2003) Ann Neurol , vol.53
    • Jenner, P.1
  • 68
    • 30044440010 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3beta modulates synphilin-1 ubiquitylation and cellular inclusion formation by SIAH: implications for proteasomal function and Lewy body formation
    • Avraham E., Szargel R., Eyal A., Rott R., and Engelender S. Glycogen synthase kinase 3beta modulates synphilin-1 ubiquitylation and cellular inclusion formation by SIAH: implications for proteasomal function and Lewy body formation. J Biol Chem 280 52 (2005) 42877
    • (2005) J Biol Chem , vol.280 , Issue.52 , pp. 42877
    • Avraham, E.1    Szargel, R.2    Eyal, A.3    Rott, R.4    Engelender, S.5
  • 69
    • 0034946830 scopus 로고    scopus 로고
    • Effect of proteasome inhibition on cellular oxidative damage, antioxidant defences and nitric oxide production
    • Lee M.H., Hyun D.H., Jenner P., and Halliwell B. Effect of proteasome inhibition on cellular oxidative damage, antioxidant defences and nitric oxide production. J Neurochem 78 (2001) 32
    • (2001) J Neurochem , vol.78 , pp. 32
    • Lee, M.H.1    Hyun, D.H.2    Jenner, P.3    Halliwell, B.4
  • 70
    • 33750350994 scopus 로고    scopus 로고
    • The role of protein aggregates in neuronal pathology: guilty, innocent, or just trying to help?
    • Gispert-Sanchez S., and Auburger G. The role of protein aggregates in neuronal pathology: guilty, innocent, or just trying to help?. J Neural Transm Suppl 70 (2006) 111
    • (2006) J Neural Transm Suppl , vol.70 , pp. 111
    • Gispert-Sanchez, S.1    Auburger, G.2
  • 71
    • 23644461006 scopus 로고    scopus 로고
    • Lewy bodies in Parkinson's disease: protectors or perpetrators?
    • Harrower T.P., Michell A.W., and Barker R.A. Lewy bodies in Parkinson's disease: protectors or perpetrators?. Exp Neurol 195 1 (2005) 1
    • (2005) Exp Neurol , vol.195 , Issue.1 , pp. 1
    • Harrower, T.P.1    Michell, A.W.2    Barker, R.A.3
  • 72
    • 0026740057 scopus 로고
    • New insights into the cause of Parkinson's disease
    • Jenner P., Schapira A.H.V., and Marsden C.D. New insights into the cause of Parkinson's disease. Neurology 42 (1992) 2241
    • (1992) Neurology , vol.42 , pp. 2241
    • Jenner, P.1    Schapira, A.H.V.2    Marsden, C.D.3
  • 74
    • 0026718086 scopus 로고
    • Brain, skeletal muscle and platelet homogenate mitochondrial function in Parkinson's disease
    • Mann V.M., Cooper J.M., Krige D., Daniel S.E., Schapira A.H.V., and Marsden C.D. Brain, skeletal muscle and platelet homogenate mitochondrial function in Parkinson's disease. Brain 115 (1992) 333
    • (1992) Brain , vol.115 , pp. 333
    • Mann, V.M.1    Cooper, J.M.2    Krige, D.3    Daniel, S.E.4    Schapira, A.H.V.5    Marsden, C.D.6
  • 76
    • 0025640845 scopus 로고
    • Anatomic and disease specificity of NADH CoQ reductase (complexI) deficiency in Parkinson's disease
    • Schapira A.H.V., Mann V.M., Cooper J.M., Dexter D., Daniel S.E., Jenner P., et al. Anatomic and disease specificity of NADH CoQ reductase (complexI) deficiency in Parkinson's disease. J Neurochem 55 (1990) 2142
    • (1990) J Neurochem , vol.55 , pp. 2142
    • Schapira, A.H.V.1    Mann, V.M.2    Cooper, J.M.3    Dexter, D.4    Daniel, S.E.5    Jenner, P.6
  • 77
    • 33749047253 scopus 로고    scopus 로고
    • Reversible inhibition of mitochondrial complex I activity following chronic dopaminergic glutathione depletion in vitro: implications for Parkinson's disease
    • Chinta S.J., and Andersen J.K. Reversible inhibition of mitochondrial complex I activity following chronic dopaminergic glutathione depletion in vitro: implications for Parkinson's disease. Free Radic Biol Med 41 9 (2006) 1442
    • (2006) Free Radic Biol Med , vol.41 , Issue.9 , pp. 1442
    • Chinta, S.J.1    Andersen, J.K.2
  • 78
    • 33644688266 scopus 로고    scopus 로고
    • Acute glutathione depletion restricts mitochondrial ATP export in cerebellar granule neurons
    • Vesce S., Jekabsons M.B., Johnson-Cadwell L.I., and Nicholls D.G. Acute glutathione depletion restricts mitochondrial ATP export in cerebellar granule neurons. J Biol Chem 280 46 (2005) 38720
    • (2005) J Biol Chem , vol.280 , Issue.46 , pp. 38720
    • Vesce, S.1    Jekabsons, M.B.2    Johnson-Cadwell, L.I.3    Nicholls, D.G.4
  • 79
    • 0033952292 scopus 로고    scopus 로고
    • Enhancement of dopaminergic neurotoxicity by the mercapturate of dopamine: relevance to Parkinson's disease
    • Zhang J., Kravtsov V., Amarnath V., Picklo M.J., Graham D.G., and Montine T.J. Enhancement of dopaminergic neurotoxicity by the mercapturate of dopamine: relevance to Parkinson's disease. J Neurochem 74 (2000) 970
    • (2000) J Neurochem , vol.74 , pp. 970
    • Zhang, J.1    Kravtsov, V.2    Amarnath, V.3    Picklo, M.J.4    Graham, D.G.5    Montine, T.J.6
  • 80
    • 0022503139 scopus 로고
    • Studies on the neurotoxicity of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine: inhibition of NAD-linked substrate oxidation by its metabolite, 1-methyl-4-phenylpyridinium
    • Vyas I., Heikkila R.E., and Nicklas W.J. Studies on the neurotoxicity of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine: inhibition of NAD-linked substrate oxidation by its metabolite, 1-methyl-4-phenylpyridinium. J Neurochem 46 (1986) 1501
    • (1986) J Neurochem , vol.46 , pp. 1501
    • Vyas, I.1    Heikkila, R.E.2    Nicklas, W.J.3
  • 81
    • 0345438935 scopus 로고
    • Do glutathione and ascorbic acid play a role in the neurotoxicity of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine?
    • Riederer P., Strolin B.M., Dostert P., Sofic E., Heusch-neider G., and Guffroy D. Do glutathione and ascorbic acid play a role in the neurotoxicity of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine?. Pharmacol Toxicol 60 S1 (1987) 39
    • (1987) Pharmacol Toxicol , vol.60 , Issue.SUPPL.1 , pp. 39
    • Riederer, P.1    Strolin, B.M.2    Dostert, P.3    Sofic, E.4    Heusch-neider, G.5    Guffroy, D.6
  • 82
    • 0031008555 scopus 로고    scopus 로고
    • The effects of oxidative stress on in vivo brain GSH turnover in young and mature mice
    • Chang M.L., Klaidman L.K., and Adams Jr. J.D. The effects of oxidative stress on in vivo brain GSH turnover in young and mature mice. Mol Chem Neuropathol 30 3 (1997) 187
    • (1997) Mol Chem Neuropathol , vol.30 , Issue.3 , pp. 187
    • Chang, M.L.1    Klaidman, L.K.2    Adams Jr., J.D.3
  • 83
    • 0024446756 scopus 로고
    • Striatal dopaminergic toxicity following intranigral injection in rats of 2-methyl-norharman, a B-carbolinium analog of n-methyl-4-phenylpyridinium ion
    • [MPP+]
    • Neafsey E.J., Drucker G., Raikoff K., and Collins M.A. Striatal dopaminergic toxicity following intranigral injection in rats of 2-methyl-norharman, a B-carbolinium analog of n-methyl-4-phenylpyridinium ion. [MPP+]. Neurosci Lett 105 (1989) 344
    • (1989) Neurosci Lett , vol.105 , pp. 344
    • Neafsey, E.J.1    Drucker, G.2    Raikoff, K.3    Collins, M.A.4
  • 84
    • 0021992979 scopus 로고
    • B-carboline analogues of n-methyl-4-phenyl-1,2,5,6-tetrahydropyridine [MPTP]: endogenous factors underlying idiopathic parkinsonism?
    • Collins M.A., and Neafsey E.J. B-carboline analogues of n-methyl-4-phenyl-1,2,5,6-tetrahydropyridine [MPTP]: endogenous factors underlying idiopathic parkinsonism?. Neurosci Lett 55 (1985) 179
    • (1985) Neurosci Lett , vol.55 , pp. 179
    • Collins, M.A.1    Neafsey, E.J.2
  • 85
    • 0023148530 scopus 로고
    • 4-Phenylpyridine and three other analogues of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine: lack of dopaminergic nigrostriatal neurotoxicity in mice and marmosets
    • Perry T.L., Jone K., Hansen S., and Wall R.A. 4-Phenylpyridine and three other analogues of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine: lack of dopaminergic nigrostriatal neurotoxicity in mice and marmosets. Neurosci Lett 75 (1987) 65
    • (1987) Neurosci Lett , vol.75 , pp. 65
    • Perry, T.L.1    Jone, K.2    Hansen, S.3    Wall, R.A.4
  • 86
    • 0029759598 scopus 로고    scopus 로고
    • Reactive dopamine metabolites and neurotoxicity: implications for Parkinson's disease
    • Hastings T.G., Lewis D.A., and Zigmond M.J. Reactive dopamine metabolites and neurotoxicity: implications for Parkinson's disease. Adv Exp Med Biol 387 (1996) 97
    • (1996) Adv Exp Med Biol , vol.387 , pp. 97
    • Hastings, T.G.1    Lewis, D.A.2    Zigmond, M.J.3
  • 87
    • 0034026634 scopus 로고    scopus 로고
    • Role for dopamine in malonate-induced damage in vivo in striatum and in vitro in mesencephalic cultures
    • Moy L.Y., Zeevalk G.D., and Sonsalla P.K. Role for dopamine in malonate-induced damage in vivo in striatum and in vitro in mesencephalic cultures. J Neurochem 74 (2000) 1656
    • (2000) J Neurochem , vol.74 , pp. 1656
    • Moy, L.Y.1    Zeevalk, G.D.2    Sonsalla, P.K.3
  • 88
    • 0018095085 scopus 로고
    • Oxidative pathways for catecholamines in the genesis of neuromelanin and cytotoxic quinones
    • Graham D.G. Oxidative pathways for catecholamines in the genesis of neuromelanin and cytotoxic quinones. Mol Pharmacol 14 (1978) 633
    • (1978) Mol Pharmacol , vol.14 , pp. 633
    • Graham, D.G.1
  • 89
    • 0028215392 scopus 로고
    • Effects of l-cysteine on the oxidation chemistry of dopamine: new reaction pathways of potential relevance to idiopathic Parkinson's disease
    • Zhang F., and Dryhurst G. Effects of l-cysteine on the oxidation chemistry of dopamine: new reaction pathways of potential relevance to idiopathic Parkinson's disease. J Med Chem 37 8 (1994) 1084
    • (1994) J Med Chem , vol.37 , Issue.8 , pp. 1084
    • Zhang, F.1    Dryhurst, G.2
  • 90
    • 0031722906 scopus 로고    scopus 로고
    • Conjugates of catecholamines with cysteine and GSH in Parkinson's disease: possible mechanisms of formation involving reactive oxygen species
    • Spencer P.E., Jenner P., Daniel S.E., Lees A.J., Marsden C.D., and Halliwell B. Conjugates of catecholamines with cysteine and GSH in Parkinson's disease: possible mechanisms of formation involving reactive oxygen species. J Neurochem 71 (1998) 2112
    • (1998) J Neurochem , vol.71 , pp. 2112
    • Spencer, P.E.1    Jenner, P.2    Daniel, S.E.3    Lees, A.J.4    Marsden, C.D.5    Halliwell, B.6
  • 91
    • 0026164647 scopus 로고
    • Catechol metabolites in the cerebrospinal fluid as possible markers in the early diagnosis of Parkinson's disease
    • Carlsson A., and Fornstedt B. Catechol metabolites in the cerebrospinal fluid as possible markers in the early diagnosis of Parkinson's disease. Neurology 41 5 (1991) 50
    • (1991) Neurology , vol.41 , Issue.5 , pp. 50
    • Carlsson, A.1    Fornstedt, B.2
  • 92
    • 0029878379 scopus 로고    scopus 로고
    • Elevated 5-S-cysteinyldopamine/homovanillic acid ratio and reduced homovanillic acid in cerebrospinal fluid: possible markers for and potential insights into the pathoetiology of Parkinson's disease
    • Cheng F.C., Kuo J.S., Chia L.G., and Dryhurst G. Elevated 5-S-cysteinyldopamine/homovanillic acid ratio and reduced homovanillic acid in cerebrospinal fluid: possible markers for and potential insights into the pathoetiology of Parkinson's disease. J Neural Transm 103 4 (1996) 433
    • (1996) J Neural Transm , vol.103 , Issue.4 , pp. 433
    • Cheng, F.C.1    Kuo, J.S.2    Chia, L.G.3    Dryhurst, G.4
  • 93
    • 0031038440 scopus 로고    scopus 로고
    • Quercetin protects cutaneous tissue-associated cell types including sensory neurons from oxidative stress induced by glutathione depletion: cooperative effects of ascorbic acid
    • Skaper S.D., Fabris M., Ferrari V., Dalle Carbonare M., and Leon A. Quercetin protects cutaneous tissue-associated cell types including sensory neurons from oxidative stress induced by glutathione depletion: cooperative effects of ascorbic acid. Free Radic Biol Med 22 4 (1997) 669
    • (1997) Free Radic Biol Med , vol.22 , Issue.4 , pp. 669
    • Skaper, S.D.1    Fabris, M.2    Ferrari, V.3    Dalle Carbonare, M.4    Leon, A.5
  • 95
    • 34250804439 scopus 로고    scopus 로고
    • Reactive oxygen species induced by proteasome inhibition in neuronal cells mediate mitochondrial dysfunction and a caspase-independent cell death
    • Papa L., Gomes E., and Rockwell P. Reactive oxygen species induced by proteasome inhibition in neuronal cells mediate mitochondrial dysfunction and a caspase-independent cell death. Apoptosis 12 8 (2007) 1389
    • (2007) Apoptosis , vol.12 , Issue.8 , pp. 1389
    • Papa, L.1    Gomes, E.2    Rockwell, P.3
  • 96
    • 33947517977 scopus 로고    scopus 로고
    • Proteasome inhibition induces glutathione synthesis and protects cells from oxidative stress: relevance to Parkinson disease
    • Yamamoto N., Sawada H., Izumi Y., Kumd T., Katsuki H., Shimohama S., et al. Proteasome inhibition induces glutathione synthesis and protects cells from oxidative stress: relevance to Parkinson disease. J Biol Chem 282 (2007) 4364
    • (2007) J Biol Chem , vol.282 , pp. 4364
    • Yamamoto, N.1    Sawada, H.2    Izumi, Y.3    Kumd, T.4    Katsuki, H.5    Shimohama, S.6
  • 97
    • 22044436635 scopus 로고    scopus 로고
    • Glutathione depletion in a midbrain-derived immortalized dopaminergic cell line results in limited tyrosine nitration of mitochondrial complex I subunits: implications for Parkinson's disease
    • Bharath S., and Andersen J.K. Glutathione depletion in a midbrain-derived immortalized dopaminergic cell line results in limited tyrosine nitration of mitochondrial complex I subunits: implications for Parkinson's disease. Antioxid Redox Signal 7 7-8 (2005) 900
    • (2005) Antioxid Redox Signal , vol.7 , Issue.7-8 , pp. 900
    • Bharath, S.1    Andersen, J.K.2
  • 98
    • 0033948161 scopus 로고    scopus 로고
    • Cerebral antioxidant status and free radical generation following glutathione depletion and subsequent recovery
    • Gupta A., Gupta A., Datta M., and Shukla G.S. Cerebral antioxidant status and free radical generation following glutathione depletion and subsequent recovery. Mol Cell Biochem 209 1-2 (2000) 55
    • (2000) Mol Cell Biochem , vol.209 , Issue.1-2 , pp. 55
    • Gupta, A.1    Gupta, A.2    Datta, M.3    Shukla, G.S.4
  • 99
    • 17444419341 scopus 로고    scopus 로고
    • Role of glutathione transport processes in kidney function
    • Lash L.H. Role of glutathione transport processes in kidney function. Toxicol Appl Pharmacol 204 3 (2005) 329
    • (2005) Toxicol Appl Pharmacol , vol.204 , Issue.3 , pp. 329
    • Lash, L.H.1
  • 100
    • 0009538631 scopus 로고
    • Dolphin D., Poulson R., and Avramovic O. (Eds), Wiley, New York
    • In: Dolphin D., Poulson R., and Avramovic O. (Eds). Glutathione: chemical, biochemical and medical aspects (1989), Wiley, New York 22
    • (1989) Glutathione: chemical, biochemical and medical aspects , pp. 22
  • 101
    • 33846418007 scopus 로고    scopus 로고
    • Characterization of intracellular elevation of glutathione [GSH] with glutathione monoethyl ester and GSH in brain and neuronal cultures: relevance to Parkinson's disease
    • Zeevalk G.D., Manzino L., Sonsalla P.K., and Bernard L.P. Characterization of intracellular elevation of glutathione [GSH] with glutathione monoethyl ester and GSH in brain and neuronal cultures: relevance to Parkinson's disease. Exp Neurol 203 2 (2007) 512
    • (2007) Exp Neurol , vol.203 , Issue.2 , pp. 512
    • Zeevalk, G.D.1    Manzino, L.2    Sonsalla, P.K.3    Bernard, L.P.4
  • 102
  • 103
    • 0018175411 scopus 로고
    • Blood-brain barrier restriction of peptides and the low uptake of enkephalins
    • Cornford E.M., Braun L.D., Crane P.D., and Oldendorf W.H. Blood-brain barrier restriction of peptides and the low uptake of enkephalins. Endocrinology 103 4 (1978) 1297
    • (1978) Endocrinology , vol.103 , Issue.4 , pp. 1297
    • Cornford, E.M.1    Braun, L.D.2    Crane, P.D.3    Oldendorf, W.H.4
  • 104
    • 0026665103 scopus 로고
    • Increase in rat-brain glutathione following intracerebroventricular administration of gamma-glutamylcysteine
    • Pileblad E., and Magnusson T. Increase in rat-brain glutathione following intracerebroventricular administration of gamma-glutamylcysteine. Biochem Pharmacol 44 5 (1992) 895
    • (1992) Biochem Pharmacol , vol.44 , Issue.5 , pp. 895
    • Pileblad, E.1    Magnusson, T.2
  • 105
    • 0031957160 scopus 로고    scopus 로고
    • Effects of reduced glutathione and N-acetylcysteine on likocaine metabolism in cimetidine treated rats
    • Testa R., Ghia M., Mattioli F., Borzone S., Caglieris S., Mereto E., et al. Effects of reduced glutathione and N-acetylcysteine on likocaine metabolism in cimetidine treated rats. Fund & Clin Pharmacol 12 (1998) 220
    • (1998) Fund & Clin Pharmacol , vol.12 , pp. 220
    • Testa, R.1    Ghia, M.2    Mattioli, F.3    Borzone, S.4    Caglieris, S.5    Mereto, E.6
  • 106
    • 0030902329 scopus 로고    scopus 로고
    • Nacystelyn, a novel lysine salt of N-acetylcysteine, to augment cellular antioxidant defence in vitro
    • Gillissen A., Joworska M., Orth M., Coffiner M., Maes P., App E.M., et al. Nacystelyn, a novel lysine salt of N-acetylcysteine, to augment cellular antioxidant defence in vitro. Respiratory Medicine 91 (2006) 159
    • (2006) Respiratory Medicine , vol.91 , pp. 159
    • Gillissen, A.1    Joworska, M.2    Orth, M.3    Coffiner, M.4    Maes, P.5    App, E.M.6
  • 107
    • 0034988283 scopus 로고    scopus 로고
    • Glutathione elevation and its protective role in acrolein-induced protein damage in synaptosomal membranes: relevance to brain lipid peroxidation in neurodegenerative disease
    • Pocernich C.B., Cardin A.L., Racine C.L., Lauderback C.M., and Butterfield D.A. Glutathione elevation and its protective role in acrolein-induced protein damage in synaptosomal membranes: relevance to brain lipid peroxidation in neurodegenerative disease. Neurochem Int 39 (2001) 141
    • (2001) Neurochem Int , vol.39 , pp. 141
    • Pocernich, C.B.1    Cardin, A.L.2    Racine, C.L.3    Lauderback, C.M.4    Butterfield, D.A.5
  • 108
    • 0033967664 scopus 로고    scopus 로고
    • In vivo glutathione elevation protects against hydroxyl free radical-induced protein oxidation in rat brain
    • Pocernich C.B., LaFontaine M., and Butterfield D.A. In vivo glutathione elevation protects against hydroxyl free radical-induced protein oxidation in rat brain. Neurochem Int 36 (2000) 185
    • (2000) Neurochem Int , vol.36 , pp. 185
    • Pocernich, C.B.1    LaFontaine, M.2    Butterfield, D.A.3
  • 109
    • 0029154990 scopus 로고
    • Uptake and distribution of N-acetylcysteine in mice: tissue specific effects on glutathione concentrations
    • McLellan L., Lewis A.D., Hall D.J., Ansell J.D., and Wolf C.R. Uptake and distribution of N-acetylcysteine in mice: tissue specific effects on glutathione concentrations. Carcinogenesis 16 (1995) 2099
    • (1995) Carcinogenesis , vol.16 , pp. 2099
    • McLellan, L.1    Lewis, A.D.2    Hall, D.J.3    Ansell, J.D.4    Wolf, C.R.5
  • 110
    • 0019454465 scopus 로고
    • Cysteine and cystine transport at the blood-brain barrier
    • Wade L.A., and Brady H.M. Cysteine and cystine transport at the blood-brain barrier. J Neurochem 37 (1981) 730
    • (1981) J Neurochem , vol.37 , pp. 730
    • Wade, L.A.1    Brady, H.M.2
  • 111
    • 0025299455 scopus 로고
    • l-cysteine, a bicarbonate-sensitive endogenous excitotoxin
    • Olney J.W., Zorumski C., Price M.T., and Labruyere J. l-cysteine, a bicarbonate-sensitive endogenous excitotoxin. Science 248 4955 (1990) 596
    • (1990) Science , vol.248 , Issue.4955 , pp. 596
    • Olney, J.W.1    Zorumski, C.2    Price, M.T.3    Labruyere, J.4
  • 113
    • 2342522756 scopus 로고    scopus 로고
    • Systemic administration of N-acetylcysteine protects dopaminergic neurons against 6-hydroxydopamine-induced degeneration
    • Munoz A.M., Rey P., Soto-Otero R., Guerra M.J., and Labandeira-Garcia J.L. Systemic administration of N-acetylcysteine protects dopaminergic neurons against 6-hydroxydopamine-induced degeneration. J Neurosci Res 76 4 (2004) 551
    • (2004) J Neurosci Res , vol.76 , Issue.4 , pp. 551
    • Munoz, A.M.1    Rey, P.2    Soto-Otero, R.3    Guerra, M.J.4    Labandeira-Garcia, J.L.5
  • 114
    • 0010478667 scopus 로고
    • Mitochondrial damage in muscle occurs after marked depletion of glutathione and is prevented by giving glutathione monoester
    • Martensson J., and Meister A. Mitochondrial damage in muscle occurs after marked depletion of glutathione and is prevented by giving glutathione monoester. Proc Natl Acad Sci U S A 86 (1989) 471
    • (1989) Proc Natl Acad Sci U S A , vol.86 , pp. 471
    • Martensson, J.1    Meister, A.2
  • 115
    • 0141991150 scopus 로고    scopus 로고
    • Glutathione monoethylester prevents mitochondrial glutathione depletion during focal cerebral ischemia
    • Anderson M.F., Nilsson M., and Sims N.R. Glutathione monoethylester prevents mitochondrial glutathione depletion during focal cerebral ischemia. Neurochem Int 44 3 (2004) 153
    • (2004) Neurochem Int , vol.44 , Issue.3 , pp. 153
    • Anderson, M.F.1    Nilsson, M.2    Sims, N.R.3
  • 116
    • 0036313070 scopus 로고    scopus 로고
    • The effects of focal ischemia and reperfusion on the glutathione content of mitochondria from rat brain subregions
    • Anderson M.F., and Sims N.R. The effects of focal ischemia and reperfusion on the glutathione content of mitochondria from rat brain subregions. J Neurochem 81 (2002) 541
    • (2002) J Neurochem , vol.81 , pp. 541
    • Anderson, M.F.1    Sims, N.R.2
  • 117
    • 0026636491 scopus 로고
    • A pilot trial of high-dose alpha-tocopherol and ascorbate in early Parkinson's disease
    • Fahn S. A pilot trial of high-dose alpha-tocopherol and ascorbate in early Parkinson's disease. Ann Neurol 32 Suppl (1992) S128
    • (1992) Ann Neurol , vol.32 , Issue.SUPPL
    • Fahn, S.1
  • 118
    • 0031711714 scopus 로고    scopus 로고
    • DATATOP: a decade of neuroprotective inquiry. Parkinson study group. Deprenyl and tocopherol antioxidative therapy of Parkinsonism
    • Shoulson I. DATATOP: a decade of neuroprotective inquiry. Parkinson study group. Deprenyl and tocopherol antioxidative therapy of Parkinsonism. Ann Neurol 44 3 Suppl 1 (1998) S160
    • (1998) Ann Neurol , vol.44 , Issue.3 SUPPL. 1
    • Shoulson, I.1
  • 119
    • 0030612117 scopus 로고    scopus 로고
    • Coenzyme Q10 levels correlate with the activities of complexes I and II/III in mitochondria from parkinsonian and nonparkinsonian subjects
    • Shults C.W., Haas R.H., Passov D., and Beal M.F. Coenzyme Q10 levels correlate with the activities of complexes I and II/III in mitochondria from parkinsonian and nonparkinsonian subjects. Ann Neurol 42 (1997) 261
    • (1997) Ann Neurol , vol.42 , pp. 261
    • Shults, C.W.1    Haas, R.H.2    Passov, D.3    Beal, M.F.4
  • 120
    • 34447252358 scopus 로고    scopus 로고
    • Randomized double-blind, placebo-controlled trial on symptomatic effects of coenzyme Q(10) in Parkinson disease
    • Storch A., Jost W.H., Vieregge P., Spiegel J., Greulich W., Durner J., et al. Randomized double-blind, placebo-controlled trial on symptomatic effects of coenzyme Q(10) in Parkinson disease. Arch Neurol 64 (2007) 938
    • (2007) Arch Neurol , vol.64 , pp. 938
    • Storch, A.1    Jost, W.H.2    Vieregge, P.3    Spiegel, J.4    Greulich, W.5    Durner, J.6
  • 122
    • 0021705485 scopus 로고
    • Human plasma glutathione oxidation in normal and pathological conditions
    • Magnani M., Novelli G., and Palloni R. Human plasma glutathione oxidation in normal and pathological conditions. Clin Physiol Biochem 2 (1984) 287
    • (1984) Clin Physiol Biochem , vol.2 , pp. 287
    • Magnani, M.1    Novelli, G.2    Palloni, R.3
  • 123
    • 34250683023 scopus 로고    scopus 로고
    • Safety and tolerability of gene therapy with an adeno-associated virus (AVV) borne GAD gene for Parkinson's disease: an open label, phase I trial
    • Kaplitt M.G., Feigin A., Tang C., Fitzsimons H.L., Mattis P., Lawlor P.A., et al. Safety and tolerability of gene therapy with an adeno-associated virus (AVV) borne GAD gene for Parkinson's disease: an open label, phase I trial. Lancet 369 (2007) 2097
    • (2007) Lancet , vol.369 , pp. 2097
    • Kaplitt, M.G.1    Feigin, A.2    Tang, C.3    Fitzsimons, H.L.4    Mattis, P.5    Lawlor, P.A.6
  • 124
    • 0032973861 scopus 로고    scopus 로고
    • Glial cells protect neurons against oxidative stress via transcriptional up-regulation of the glutathione synthesis
    • Iwata-Ichikawa E., Kondo Y., Miyazaki I., Asanuma M., and Ogawa N. Glial cells protect neurons against oxidative stress via transcriptional up-regulation of the glutathione synthesis. J Neurochem 72 6 (1999) 2334
    • (1999) J Neurochem , vol.72 , Issue.6 , pp. 2334
    • Iwata-Ichikawa, E.1    Kondo, Y.2    Miyazaki, I.3    Asanuma, M.4    Ogawa, N.5
  • 125
    • 0037996661 scopus 로고    scopus 로고
    • Coordinate regulation of glutathione biosynthesis and release by Nrf2-expressing glia potently protects neurons from oxidative stress
    • Shih A.Y., Johnson D.A., Wong G., Kraft A.D., Jiang L., Erb H., et al. Coordinate regulation of glutathione biosynthesis and release by Nrf2-expressing glia potently protects neurons from oxidative stress. J Neurosci 23 (2003) 3394
    • (2003) J Neurosci , vol.23 , pp. 3394
    • Shih, A.Y.1    Johnson, D.A.2    Wong, G.3    Kraft, A.D.4    Jiang, L.5    Erb, H.6
  • 126
    • 33750017152 scopus 로고    scopus 로고
    • Enhanced biosynthesis of glutathione in the spiral ganglion of the cochlea after in vivo treatment with dexamethasone in mice
    • Nagashima R., and Ogita K. Enhanced biosynthesis of glutathione in the spiral ganglion of the cochlea after in vivo treatment with dexamethasone in mice. Brain Res 1117 1 (2006) 101
    • (2006) Brain Res , vol.1117 , Issue.1 , pp. 101
    • Nagashima, R.1    Ogita, K.2
  • 127
    • 0032931535 scopus 로고    scopus 로고
    • Potentiation of excitotoxic injury by high concentrations of extracellular reduced glutathione
    • Regan R.F., and Guo Y.P. Potentiation of excitotoxic injury by high concentrations of extracellular reduced glutathione. Neuroscience 91 2 (1999) 463
    • (1999) Neuroscience , vol.91 , Issue.2 , pp. 463
    • Regan, R.F.1    Guo, Y.P.2
  • 128
    • 0033616356 scopus 로고    scopus 로고
    • Extracellular reduced glutathione increases neuronal vulnerability to combined chemical hypoxia and glucose deprivation
    • Regan R., and Guo Y. Extracellular reduced glutathione increases neuronal vulnerability to combined chemical hypoxia and glucose deprivation. Brain Res 817 (1999) 145
    • (1999) Brain Res , vol.817 , pp. 145
    • Regan, R.1    Guo, Y.2
  • 129
    • 0031865773 scopus 로고    scopus 로고
    • The peptide transporter PepT2 mediates the uptake of the glutathione precursor CysGly in astroglia-rich primary cultures
    • Dringen R., Hamprecht B., and Broer S. The peptide transporter PepT2 mediates the uptake of the glutathione precursor CysGly in astroglia-rich primary cultures. J Neurochem 71 (1998) 388
    • (1998) J Neurochem , vol.71 , pp. 388
    • Dringen, R.1    Hamprecht, B.2    Broer, S.3
  • 130
    • 0032889671 scopus 로고    scopus 로고
    • The peptide transporter PepT2 is expressed in rat brain and mediates the accumulation of the fluorescent dipeptide derivative B-Ala-Lys-N-AMCA in astrocytes
    • Tom Dieck S., Heuer H., Ehrchen J., Otto C., and Bauer K. The peptide transporter PepT2 is expressed in rat brain and mediates the accumulation of the fluorescent dipeptide derivative B-Ala-Lys-N-AMCA in astrocytes. Glia 25 (1999) 10
    • (1999) Glia , vol.25 , pp. 10
    • Tom Dieck, S.1    Heuer, H.2    Ehrchen, J.3    Otto, C.4    Bauer, K.5
  • 131
    • 0029965218 scopus 로고    scopus 로고
    • Glutamate and cysteinylglycine effects on NMDA receptors: inhibition by ethanol
    • Morris J., and Leslie S.W. Glutamate and cysteinylglycine effects on NMDA receptors: inhibition by ethanol. Alcohol 13 2 (1996) 157
    • (1996) Alcohol , vol.13 , Issue.2 , pp. 157
    • Morris, J.1    Leslie, S.W.2
  • 132
    • 0037215549 scopus 로고    scopus 로고
    • Transcellular transport of a highly polar 3+ net charge opioid tetrapeptide
    • Zhao K., Luo G., Zhao G.-M., Schiller P.W., and Szeto H.H. Transcellular transport of a highly polar 3+ net charge opioid tetrapeptide. J Pharmacol Exp Ther 304 1 (2003) 425
    • (2003) J Pharmacol Exp Ther , vol.304 , Issue.1 , pp. 425
    • Zhao, K.1    Luo, G.2    Zhao, G.-M.3    Schiller, P.W.4    Szeto, H.H.5
  • 133
    • 0035937595 scopus 로고    scopus 로고
    • Nanoparticulate systems for brain delivery of drugs
    • Kreuter J. Nanoparticulate systems for brain delivery of drugs. Adv Drug Deliv Rev 47 (2001) 65
    • (2001) Adv Drug Deliv Rev , vol.47 , pp. 65
    • Kreuter, J.1
  • 134
    • 0031765572 scopus 로고    scopus 로고
    • Nanoparticle technology for delivery of drugs across the blood-brain barrier
    • Schroeder U., Sommerfeld P., Ulrich S., and Sabel B.A. Nanoparticle technology for delivery of drugs across the blood-brain barrier. J Pharm Sci 87 (1998) 1305
    • (1998) J Pharm Sci , vol.87 , pp. 1305
    • Schroeder, U.1    Sommerfeld, P.2    Ulrich, S.3    Sabel, B.A.4
  • 135
    • 0028911362 scopus 로고
    • Passage of peptides through the blood-brain barrier with colloidal polymer particles
    • [nanoparticles]
    • Kreuter J., Alyautdin R.N., Kharkevich D.A., and Ivanov A.A. Passage of peptides through the blood-brain barrier with colloidal polymer particles. [nanoparticles]. Brain Res 674 (1995) 171
    • (1995) Brain Res , vol.674 , pp. 171
    • Kreuter, J.1    Alyautdin, R.N.2    Kharkevich, D.A.3    Ivanov, A.A.4
  • 136
    • 0029550090 scopus 로고
    • Relative vulnerability of dopamine and GABA neurons in mesencephalic culture to inhibition of succinate dehydrogenase by malonate and 3-nitropropionic acid and protection by NMDA receptor blockade
    • Zeevalk G.D., Derr-Yellin E., and Nicklas W.J. Relative vulnerability of dopamine and GABA neurons in mesencephalic culture to inhibition of succinate dehydrogenase by malonate and 3-nitropropionic acid and protection by NMDA receptor blockade. J Pharmacol Exp Ther 275 (1995) 1124
    • (1995) J Pharmacol Exp Ther , vol.275 , pp. 1124
    • Zeevalk, G.D.1    Derr-Yellin, E.2    Nicklas, W.J.3
  • 137
    • 0033970161 scopus 로고    scopus 로고
    • Oxidative stress during energy impairment in mesencephalic cultures is not a downstream consequence of a secondary excitotoxicity
    • Zeevalk G.D., Bernard L.P., and Nicklas W.J. Oxidative stress during energy impairment in mesencephalic cultures is not a downstream consequence of a secondary excitotoxicity. Neuroscience 96 2 (2000) 309
    • (2000) Neuroscience , vol.96 , Issue.2 , pp. 309
    • Zeevalk, G.D.1    Bernard, L.P.2    Nicklas, W.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.