메뉴 건너뛰기




Volumn 759, Issue 1, 1997, Pages 67-75

Involvement of glutathione peroxidase and catalase in the disposal of exogenous hydrogen peroxide by cultured astroglial cells

Author keywords

Aminotriazole; Astrocyte; Catalase; Glutathione; Glutathione reductase; H2O2; Mercaptosuccinate; Pentose phosphate pathway

Indexed keywords

AMITROLE; CATALASE; GLUCOSE; GLUTATHIONE; GLUTATHIONE PEROXIDASE; GLUTATHIONE REDUCTASE; HYDROGEN PEROXIDE; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; THIOMALIC ACID;

EID: 0030852097     PISSN: 00068993     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-8993(97)00233-3     Document Type: Article
Times cited : (170)

References (54)
  • 1
    • 0000024076 scopus 로고
    • Catalase
    • in: H.U. Bergmeyer, J. Bergmeyer and M. Graßl (Eds.), Verlag Chemie, Weinheim, Germany
    • H.E. Aebi, Catalase, in: H.U. Bergmeyer, J. Bergmeyer and M. Graßl (Eds.), Methods of Enzymatic Analysis, vol. 3, Verlag Chemie, Weinheim, Germany, 1984, pp. 273-286.
    • (1984) Methods of Enzymatic Analysis , vol.3 , pp. 273-286
    • Aebi, H.E.1
  • 2
    • 0025043947 scopus 로고
    • Microtiter plate assay for the measurement of glutathione and glutathione disulfide in large numbers of biological samples
    • Baker M.A., Cerniglia G.J., Zaman A. Microtiter plate assay for the measurement of glutathione and glutathione disulfide in large numbers of biological samples. Anal. Biochem. 190:1990;360-365.
    • (1990) Anal. Biochem. , vol.190 , pp. 360-365
    • Baker, M.A.1    Cerniglia, G.J.2    Zaman, A.3
  • 3
    • 0028648281 scopus 로고
    • Oxidative stress in the central nervous system: Monitoring the metabolic response using the pentose phosphate pathway
    • Ben-Yoseph O., Boxer P.A., Ross B.D. Oxidative stress in the central nervous system: monitoring the metabolic response using the pentose phosphate pathway. Dev. Neurosci. 16:1994;328-336.
    • (1994) Dev. Neurosci. , vol.16 , pp. 328-336
    • Ben-Yoseph, O.1    Boxer, P.A.2    Ross, B.D.3
  • 4
    • 0028952832 scopus 로고
    • Effect of peroxynitrite on the mitochondrial respiratory chain: Differential susceptibility of neurones and astrocytes in primary cultures
    • Bolanos J.P., Heales S.J.R., Land J.M., Clark J.B. Effect of peroxynitrite on the mitochondrial respiratory chain: differential susceptibility of neurones and astrocytes in primary cultures. J. Neurochem. 64:1995;1965-1972.
    • (1995) J. Neurochem. , vol.64 , pp. 1965-1972
    • Bolanos, J.P.1    Heales, S.J.R.2    Land, J.M.3    Clark, J.B.4
  • 5
    • 0028936986 scopus 로고
    • Bioenergetic and oxidative stress in neurodegenerative diseases
    • Bowling A.C., Beal M.F. Bioenergetic and oxidative stress in neurodegenerative diseases. Life Sci. 56:1994;1151-1171.
    • (1994) Life Sci. , vol.56 , pp. 1151-1171
    • Bowling, A.C.1    Beal, M.F.2
  • 6
    • 0019424679 scopus 로고
    • Regional distribution of catalase in the adult rat brain
    • Brannan T.S., Maker H.S., Raes I.P. Regional distribution of catalase in the adult rat brain. J. Neurochem. 36:1981;307-309.
    • (1981) J. Neurochem. , vol.36 , pp. 307-309
    • Brannan, T.S.1    Maker, H.S.2    Raes, I.P.3
  • 7
    • 0027263652 scopus 로고
    • Oxidative stress in a clonal line of neuronal origin: Effects of antioxidant enzyme modulation
    • Buckman T.D., Sutphin M.S., Mitrovic B. Oxidative stress in a clonal line of neuronal origin: effects of antioxidant enzyme modulation. J. Neurochem. 60:1993;2046-2058.
    • (1993) J. Neurochem. , vol.60 , pp. 2046-2058
    • Buckman, T.D.1    Sutphin, M.S.2    Mitrovic, B.3
  • 8
    • 0025915964 scopus 로고
    • The effect of xanthine/xanthine oxidase generated reactive oxygen species on synaptic transmission
    • Colton C., Yao J., Grossman Y., Gilbert D. The effect of xanthine/xanthine oxidase generated reactive oxygen species on synaptic transmission. Free Rad. Res. Commun. 14:1991;385-393.
    • (1991) Free Rad. Res. Commun. , vol.14 , pp. 385-393
    • Colton, C.1    Yao, J.2    Grossman, Y.3    Gilbert, D.4
  • 9
    • 0026633956 scopus 로고
    • Free radical scavenging systems of rat astroglial cells in primary culture: Effect of anoxia and drug treatment
    • Copin J.C., Ledig M., Tholey G. Free radical scavenging systems of rat astroglial cells in primary culture: effect of anoxia and drug treatment. Neurochem. Res. 17:1992;677-682.
    • (1992) Neurochem. Res. , vol.17 , pp. 677-682
    • Copin, J.C.1    Ledig, M.2    Tholey, G.3
  • 11
    • 0029990439 scopus 로고    scopus 로고
    • Astrocytes protect neurons from hydrogen peroxide toxicity
    • Desagher S., Glowinski J., Premont J. Astrocytes protect neurons from hydrogen peroxide toxicity. J. Neurosci. 16:1996;2553-2562.
    • (1996) J. Neurosci. , vol.16 , pp. 2553-2562
    • Desagher, S.1    Glowinski, J.2    Premont, J.3
  • 12
    • 0027274778 scopus 로고
    • Glutathione metabolism in primary astrocyte cultures: Flow cytometric evidence of heterogeneous distribution of GSH content
    • Devesa A., O'Connor J.E., Garcia C., Puertes I.R., Vina J.R. Glutathione metabolism in primary astrocyte cultures: flow cytometric evidence of heterogeneous distribution of GSH content. Brain Res. 618:1993;181-189.
    • (1993) Brain Res. , vol.618 , pp. 181-189
    • Devesa, A.1    O'Connor, J.E.2    Garcia, C.3    Puertes, I.R.4    Vina, J.R.5
  • 13
    • 0026513876 scopus 로고
    • Glucose, insulin and insulin-like growth factor I regulate the glycogen content of astroglia-rich primary cultures
    • Dringen R., Hamprecht B. Glucose, insulin and insulin-like growth factor I regulate the glycogen content of astroglia-rich primary cultures. J. Neurochem. 58:1992;511-517.
    • (1992) J. Neurochem. , vol.58 , pp. 511-517
    • Dringen, R.1    Hamprecht, B.2
  • 14
    • 0029836312 scopus 로고    scopus 로고
    • Glutathione content as an indicator for the presence of metabolic pathways of amino acids in astroglial cultures
    • Dringen R., Hamprecht B. Glutathione content as an indicator for the presence of metabolic pathways of amino acids in astroglial cultures. J. Neurochem. 67:1996;1375-1382.
    • (1996) J. Neurochem. , vol.67 , pp. 1375-1382
    • Dringen, R.1    Hamprecht, B.2
  • 15
    • 0027216810 scopus 로고
    • Glycogen in astrocytes: Possible function as lactate supply for neighboring cells
    • Dringen R., Gebhardt R., Hamprecht B. Glycogen in astrocytes: possible function as lactate supply for neighboring cells. Brain Res. 623:1993;208-214.
    • (1993) Brain Res. , vol.623 , pp. 208-214
    • Dringen, R.1    Gebhardt, R.2    Hamprecht, B.3
  • 16
    • 0021345735 scopus 로고
    • Oxidation of glutathione during hydroperoxide metabolism. A study using isolated hepatocytes and the glutathione reductase inhibitor 1,3-bis(2-chloroethyl)-1-nitrosourea
    • Eklöw L., Moldeus P., Orrenius S. Oxidation of glutathione during hydroperoxide metabolism. A study using isolated hepatocytes and the glutathione reductase inhibitor 1,3-bis(2-chloroethyl)-1-nitrosourea. Eur. J. Biochem. 138:1984;459-463.
    • (1984) Eur. J. Biochem. , vol.138 , pp. 459-463
    • Eklöw, L.1    Moldeus, P.2    Orrenius, S.3
  • 17
    • 0021288821 scopus 로고
    • Assay for glutathione peroxidase
    • Flohe L., Günzler W.A. Assay for glutathione peroxidase. Methods Enzymol. 105:1984;114-121.
    • (1984) Methods Enzymol. , vol.105 , pp. 114-121
    • Flohe, L.1    Günzler, W.A.2
  • 19
    • 85047694372 scopus 로고
    • Subcellular distribution of D-amino acid oxidase and catalase in rat brain
    • Gaunt G.L., De Duve C. Subcellular distribution of D-amino acid oxidase and catalase in rat brain. J. Neurochem. 26:1976;749-759.
    • (1976) J. Neurochem. , vol.26 , pp. 749-759
    • Gaunt, G.L.1    De Duve, C.2
  • 20
    • 0019167355 scopus 로고
    • Determination of glutathione and glutathione disulfide using glutathione reductase and 2-vinylpyridine
    • Griffith O.W. Determination of glutathione and glutathione disulfide using glutathione reductase and 2-vinylpyridine. Anal. Biochem. 106:1980;207-212.
    • (1980) Anal. Biochem. , vol.106 , pp. 207-212
    • Griffith, O.W.1
  • 21
    • 0018666729 scopus 로고
    • Potent and specific inhibition of glutathione synthesis by buthionine sulfoximine (S-n-butyl homocysteine sulfoximine)
    • Griffith O.W., Meister A. Potent and specific inhibition of glutathione synthesis by buthionine sulfoximine (S-n-butyl homocysteine sulfoximine). J. Biol. Chem. 254:1979;7558-7560.
    • (1979) J. Biol. Chem. , vol.254 , pp. 7558-7560
    • Griffith, O.W.1    Meister, A.2
  • 22
    • 0026754574 scopus 로고
    • Reactive oxygen species and the central nervous system
    • Halliwell B. Reactive oxygen species and the central nervous system. J. Neurochem. 59:1992;1609-1623.
    • (1992) J. Neurochem. , vol.59 , pp. 1609-1623
    • Halliwell, B.1
  • 23
    • 0002200343 scopus 로고
    • Energy metabolism
    • In H. Kettenmann and B.R. Ransom (Eds.), Oxford University Press, New York, NY
    • B. Hamprecht and R. Dringen, Energy metabolism. In H. Kettenmann and B.R. Ransom (Eds.), Neuroglia, Oxford University Press, New York, NY, 1995, pp. 473-487.
    • (1995) Neuroglia , pp. 473-487
    • Hamprecht, B.1    Dringen, R.2
  • 24
    • 0021893839 scopus 로고
    • Primary glial cultures as a model system for studying hormone action
    • Hamprecht B., Löffler F. Primary glial cultures as a model system for studying hormone action. Methods Enzymol. 109:1985;341-345.
    • (1985) Methods Enzymol. , vol.109 , pp. 341-345
    • Hamprecht, B.1    Löffler, F.2
  • 25
    • 0343374214 scopus 로고
    • Glucose metabolism in brain tissue: The hexosemonophosphate shunt and its role in glutathione reduction
    • Hotta S.S. Glucose metabolism in brain tissue: the hexosemonophosphate shunt and its role in glutathione reduction. J. Neurochem. 9:1962;43-51.
    • (1962) J. Neurochem. , vol.9 , pp. 43-51
    • Hotta, S.S.1
  • 26
    • 0014238709 scopus 로고
    • The hexosemonophosphate shunt and glutathione reduction in guinea pig brain tissue: Changes caused by chlorpromazine, amytal, amd malonate
    • Hotta S.S., Seventko J.M. Jr. The hexosemonophosphate shunt and glutathione reduction in guinea pig brain tissue: changes caused by chlorpromazine, amytal, amd malonate. Arch. Biochem. Biophys. 123:1968;104-108.
    • (1968) Arch. Biochem. Biophys. , vol.123 , pp. 104-108
    • Hotta, S.S.1    Seventko J.M., Jr.2
  • 27
    • 0029050628 scopus 로고
    • Distribution of glutathione and glutathione-related enzyme systems in mitochondria and cytosol of cultured cerebellar astrocytes and granule cells
    • Huang J., Philbert M.A. Distribution of glutathione and glutathione-related enzyme systems in mitochondria and cytosol of cultured cerebellar astrocytes and granule cells. Brain Res. 680:1995;16-22.
    • (1995) Brain Res. , vol.680 , pp. 16-22
    • Huang, J.1    Philbert, M.A.2
  • 30
    • 0025293777 scopus 로고
    • Hydrogen peroxide production during experimental protein glycation
    • Jiang Z.-Y., Woollard A.C.S., Wolff S.P. Hydrogen peroxide production during experimental protein glycation. FEBS Lett. 268:1990;69-71.
    • (1990) FEBS Lett. , vol.268 , pp. 69-71
    • Jiang, Z.-Y.1    Woollard, A.C.S.2    Wolff, S.P.3
  • 31
    • 0343985338 scopus 로고    scopus 로고
    • Glutathione release and catabolism during energy substrate restriction in astrocytes
    • Juurlink B.H.J., Schültke E., Hertz L. Glutathione release and catabolism during energy substrate restriction in astrocytes. Brain Res. 710:1996;229-233.
    • (1996) Brain Res. , vol.710 , pp. 229-233
    • Juurlink, B.H.J.1    Schültke, E.2    Hertz, L.3
  • 32
    • 0027465673 scopus 로고
    • Purification of cytosolic malic enzyme from bovine brain, generation of monoclonal antibodies, and immunocytochemical localization of the enzyme in glial cells of neural primary cultures
    • Kurz G.M., Wiesinger H., Hamprecht B. Purification of cytosolic malic enzyme from bovine brain, generation of monoclonal antibodies, and immunocytochemical localization of the enzyme in glial cells of neural primary cultures. J. Neurochem. 60:1993;1467-1474.
    • (1993) J. Neurochem. , vol.60 , pp. 1467-1474
    • Kurz, G.M.1    Wiesinger, H.2    Hamprecht, B.3
  • 33
    • 0029002838 scopus 로고
    • Cultured rat striatal and cortical astrocytes protect mesencephalic dopaminergic neurons against hydrogen peroxide toxicity independent of their effect on neuronal development
    • Langeveld C.H., Jongenelen C.A.M., Schepens E., Stoof J.C., Bast A., Drukarch B. Cultured rat striatal and cortical astrocytes protect mesencephalic dopaminergic neurons against hydrogen peroxide toxicity independent of their effect on neuronal development. Neurosci. Lett. 192:1995;13-16.
    • (1995) Neurosci. Lett. , vol.192 , pp. 13-16
    • Langeveld, C.H.1    Jongenelen, C.A.M.2    Schepens, E.3    Stoof, J.C.4    Bast, A.5    Drukarch, B.6
  • 35
    • 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., 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;45-53.
    • (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.L.6
  • 36
    • 0027972577 scopus 로고
    • Kinetic studies on the removal of extracellular hydrogen peroxide by cultured fibroblasts
    • Makino M., Mochizuki Y., Bannai S., Sugita Y. Kinetic studies on the removal of extracellular hydrogen peroxide by cultured fibroblasts. J. Biol. Chem. 269:1994;1020-1025.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1020-1025
    • Makino, M.1    Mochizuki, Y.2    Bannai, S.3    Sugita, Y.4
  • 37
    • 0017106394 scopus 로고
    • Microperoxisome distribution in the central nervous system of the rat
    • McKenna O., Arnold G., Holtzman E. Microperoxisome distribution in the central nervous system of the rat. Brain Res. 117:1976;181-194.
    • (1976) Brain Res. , vol.117 , pp. 181-194
    • McKenna, O.1    Arnold, G.2    Holtzman, E.3
  • 38
    • 0026555334 scopus 로고
    • Depletion of brain glutathione by buthionine sulfoximine enhances cerebral ischemic injury in rats
    • Mizui T., Kinouchi H., Chan P.H. Depletion of brain glutathione by buthionine sulfoximine enhances cerebral ischemic injury in rats. Am. J. Physiol. 262:1992;H313-H317.
    • (1992) Am. J. Physiol. , vol.262
    • Mizui, T.1    Kinouchi, H.2    Chan, P.H.3
  • 39
    • 0028088924 scopus 로고
    • Astrocytes and catalase prevent the toxicity of catecholamines to oligodendrocytes
    • Noble P.G., Antel J.P., Yong V.W. Astrocytes and catalase prevent the toxicity of catecholamines to oligodendrocytes. Brain Res. 633:1994;83-90.
    • (1994) Brain Res. , vol.633 , pp. 83-90
    • Noble, P.G.1    Antel, J.P.2    Yong, V.W.3
  • 40
    • 0028999165 scopus 로고
    • Biosynthesis and maintenance of GSH in primary astrocyte cultures: Role of cystine and ascorbate
    • O'Connor E., Devesa A., Garcia C., Puertes I.R., Pellin A., Vina J.R. Biosynthesis and maintenance of GSH in primary astrocyte cultures: role of cystine and ascorbate. Brain Res. 680:1995;157-163.
    • (1995) Brain Res. , vol.680 , pp. 157-163
    • O'Connor, E.1    Devesa, A.2    Garcia, C.3    Puertes, I.R.4    Pellin, A.5    Vina, J.R.6
  • 41
    • 0025912678 scopus 로고
    • Free radicals accelerate the decay of long-term potentiation in field CA1 of guinea-pig hippocampus
    • Pellmar T.C., Hollinden G.E., Sarvey J.M. Free radicals accelerate the decay of long-term potentiation in field CA1 of guinea-pig hippocampus. Neuroscience. 44:1991;353-359.
    • (1991) Neuroscience , vol.44 , pp. 353-359
    • Pellmar, T.C.1    Hollinden, G.E.2    Sarvey, J.M.3
  • 42
    • 0024537271 scopus 로고
    • Reduction of brain glutathione by L-buthionine sulfoximine potentiates the dopamine-depletion action of 6-hydroxydopamine in rat striatum
    • Pileblad E., Magnuson T., Fornstedt B. Reduction of brain glutathione by L-buthionine sulfoximine potentiates the dopamine-depletion action of 6-hydroxydopamine in rat striatum. J. Neurochem. 52:1989;978-980.
    • (1989) J. Neurochem. , vol.52 , pp. 978-980
    • Pileblad, E.1    Magnuson, T.2    Fornstedt, B.3
  • 43
    • 0027421350 scopus 로고
    • Maintenance of neuronal glutathione by glial cells
    • Sagara J., Miura K., Bannai S. Maintenance of neuronal glutathione by glial cells. J. Neurochem. 61:1993;1672-1676.
    • (1993) J. Neurochem. , vol.61 , pp. 1672-1676
    • Sagara, J.1    Miura, K.2    Bannai, S.3
  • 44
    • 0029988384 scopus 로고    scopus 로고
    • Glutathione efflux from cultured astrocytes
    • Sagara J., Makino N., Bannai S. Glutathione efflux from cultured astrocytes. J. Neurochem. 66:1996;1876-1881.
    • (1996) J. Neurochem. , vol.66 , pp. 1876-1881
    • Sagara, J.1    Makino, N.2    Bannai, S.3
  • 45
    • 0018853019 scopus 로고
    • Hydrogen peroxide production by rat brain in vivo
    • Sinet P.M., Heikkila R.E., Cohen G. Hydrogen peroxide production by rat brain in vivo. J. Neurochem. 34:1980;1421-1428.
    • (1980) J. Neurochem. , vol.34 , pp. 1421-1428
    • Sinet, P.M.1    Heikkila, R.E.2    Cohen, G.3
  • 46
    • 0016218384 scopus 로고
    • Useful agents for the study of glutathione metabolism in erythrocytes
    • Srivastava S.K., Awasthi Y.C., Beutler E. Useful agents for the study of glutathione metabolism in erythrocytes. Biochem. J. 139:1974;289-295.
    • (1974) Biochem. J. , vol.139 , pp. 289-295
    • Srivastava, S.K.1    Awasthi, Y.C.2    Beutler, E.3
  • 47
    • 0021923805 scopus 로고
    • Endogenous defenses against cytotoxicity of hydrogen peroxide in cultured rat hepatocytes
    • Starke P.E., Farber J.L. Endogenous defenses against cytotoxicity of hydrogen peroxide in cultured rat hepatocytes. J. Biol. Chem. 260:1985;86-92.
    • (1985) J. Biol. Chem. , vol.260 , pp. 86-92
    • Starke, P.E.1    Farber, J.L.2
  • 48
    • 0021660653 scopus 로고
    • Selenium-glutathione peroxidase: Properties and synthesis
    • Tappel A.L. Selenium-glutathione peroxidase: properties and synthesis. Curr. Top. Cell. Regul. 24:1984;87-97.
    • (1984) Curr. Top. Cell. Regul. , vol.24 , pp. 87-97
    • Tappel, A.L.1
  • 49
    • 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. Enzymic method for quantitative determination of nanogram amounts of total and oxidized glutathione: applications to mammalian blood and other tissues. Anal. Biochem. 27:1969;502-522.
    • (1969) Anal. Biochem. , vol.27 , pp. 502-522
    • Tietze, F.1
  • 50
    • 0000191753 scopus 로고
    • Lactate dehydrogenase: UV-method with pyruvate and NADH
    • In H.U. Bergmeyer (Ed.), Verlag Chemie, Weinheim, Germany
    • A. Vassault, Lactate dehydrogenase: UV-method with pyruvate and NADH. In H.U. Bergmeyer (Ed.), Methods of Enzymatic Analysis, Vol. 3, Verlag Chemie, Weinheim, Germany, 1983, pp. 118-126.
    • (1983) Methods of Enzymatic Analysis , vol.3 , pp. 118-126
    • Vassault, A.1
  • 51
    • 0028072369 scopus 로고
    • The pathophysiology of reactive oxygen intermediates in the central nervous system
    • Weber G.F. The pathophysiology of reactive oxygen intermediates in the central nervous system. Med. Hypoth. 43:1994;223-230.
    • (1994) Med. Hypoth. , vol.43 , pp. 223-230
    • Weber, G.F.1
  • 52
    • 0023033372 scopus 로고
    • Multiple NADPH-producing pathways control glutathione (GSH) content in retina
    • Winkler B.S., DeSantis N., Solomon F. Multiple NADPH-producing pathways control glutathione (GSH) content in retina. Exp. Eye Res. 43:1986;829-847.
    • (1986) Exp. Eye Res. , vol.43 , pp. 829-847
    • Winkler, B.S.1    Desantis, N.2    Solomon, F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.