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Volumn 250, Issue 3, 1997, Pages 670-679

The malaria parasite supplies glutathione to its host cell - Investigation of glutathione transport and metabolism in human erythrocytes infected with Plasmodium falciparum

Author keywords

Glutathione; Oxidative stress; Plasmodium falciparum; Synthesis; Glutamylcysteine

Indexed keywords

GAMMA GLUTAMYLCYSTEINE; GLUTATHIONE; GLUTATHIONE DISULFIDE; GLUTATHIONE SYNTHASE;

EID: 0031574219     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.00670.x     Document Type: Article
Times cited : (138)

References (65)
  • 1
    • 0027430639 scopus 로고
    • Origin of reactive oxygen species in erythrocytes infected with Plasmodium falciparum
    • Atamna, H. & Ginsburg, H. (1993) Origin of reactive oxygen species in erythrocytes infected with Plasmodium falciparum, Mol. Biochem. Parasitol. 61, 231-242.
    • (1993) Mol. Biochem. Parasitol. , vol.61 , pp. 231-242
    • Atamna, H.1    Ginsburg, H.2
  • 2
    • 0028041047 scopus 로고
    • Hexose-monophosphate shunt activity in intact Plasmodium falciparum-infected erythrocytcs and in free parasites
    • Atamna, H., Pascarmona, G. & Ginsburg, H. (1994) Hexose-monophosphate shunt activity in intact Plasmodium falciparum-infected erythrocytcs and in free parasites, Mol. Biochem. Parasitol. 67, 79-89.
    • (1994) Mol. Biochem. Parasitol. , vol.67 , pp. 79-89
    • Atamna, H.1    Pascarmona, G.2    Ginsburg, H.3
  • 3
    • 0019323599 scopus 로고
    • General specificity of thioltransferase (thiol:disulfide oxidoreductase) from rat liver for thiol and disulfide substrates
    • Axelsson, K. & Mannervik, B. (1980) General specificity of thioltransferase (thiol:disulfide oxidoreductase) from rat liver for thiol and disulfide substrates, Biochim. Biophys. Acta 613, 324-336.
    • (1980) Biochim. Biophys. Acta , vol.613 , pp. 324-336
    • Axelsson, K.1    Mannervik, B.2
  • 4
    • 0027244093 scopus 로고
    • Presence of endogenous superoxide dismutase activity in three rodent malaria species
    • Becuwe, P., Slomianny, C., Camus, D. & Dive, D. (1993) Presence of endogenous superoxide dismutase activity in three rodent malaria species, Parasitol. Res. 79, 349-352.
    • (1993) Parasitol. Res. , vol.79 , pp. 349-352
    • Becuwe, P.1    Slomianny, C.2    Camus, D.3    Dive, D.4
  • 5
    • 0002260348 scopus 로고
    • The FMOC-ADAM approach to amino acid analysis
    • Betner I. & Foldi, B. (1988) The FMOC-ADAM approach to amino acid analysis, LC-GC Int. 2, 44-53.
    • (1988) LC-GC Int. , vol.2 , pp. 44-53
    • Betner, I.1    Foldi, B.2
  • 8
    • 0017379264 scopus 로고
    • Comments concerning the fluorometric assay of glutathione
    • Beutler, E. & West, C. (1977) Comments concerning the fluorometric assay of glutathione, Anal. Biochem. 81, 458-460.
    • (1977) Anal. Biochem. , vol.81 , pp. 458-460
    • Beutler, E.1    West, C.2
  • 9
    • 33947476438 scopus 로고
    • Glutathione peroxidase. The primary agent for the elimination of hydrogen peroxide in erythrocytes
    • Cohen, G. & Hochstein, P. (1963) Glutathione peroxidase. The primary agent for the elimination of hydrogen peroxide in erythrocytes, Biochemistry 2, 1420-1428.
    • (1963) Biochemistry , vol.2 , pp. 1420-1428
    • Cohen, G.1    Hochstein, P.2
  • 10
    • 0025937565 scopus 로고
    • Roles of catalase and the glutathione redox cycle in the regulation of anterior-chamber hydrogen peroxide
    • Costarides, A. P., Riley, M. V. & Green, K. (1991) Roles of catalase and the glutathione redox cycle in the regulation of anterior-chamber hydrogen peroxide, Ophthalmic Res. 23, 284-294.
    • (1991) Ophthalmic Res. , vol.23 , pp. 284-294
    • Costarides, A.P.1    Riley, M.V.2    Green, K.3
  • 11
    • 0018347488 scopus 로고
    • Dependence of plasmodial glutathione metabolism on the host cell
    • Eckman, J. R. &. Eaton, J. W. (1979) Dependence of plasmodial glutathione metabolism on the host cell, Nature 278, 754-756.
    • (1979) Nature , vol.278 , pp. 754-756
    • Eckman, J.R.1    Eaton, J.W.2
  • 12
    • 0027419774 scopus 로고
    • Secretory processes in Plasmodium
    • Elford, B. C. & Ferguson, D. J. (1993) Secretory processes in Plasmodium, Parasitol. Today 9, 80-81.
    • (1993) Parasitol. Today , vol.9 , pp. 80-81
    • Elford, B.C.1    Ferguson, D.J.2
  • 14
    • 0029908565 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a putative glutathione reductase gene, the PfGR2 gene, from Plasmodium falciparum
    • Farber, P. M., Becker, K., Muller, S., Schirmer, R. H. & Franklin, R. M. (1996) Molecular cloning and characterization of a putative glutathione reductase gene, the PfGR2 gene, from Plasmodium falciparum, Eur. J. Biochem. 239, 655-661.
    • (1996) Eur. J. Biochem. , vol.239 , pp. 655-661
    • Farber, P.M.1    Becker, K.2    Muller, S.3    Schirmer, R.H.4    Franklin, R.M.5
  • 15
    • 0018410383 scopus 로고
    • Oxidant damage mediates variant red cell resistance to malaria
    • Friedman, M. J. (1979) Oxidant damage mediates variant red cell resistance to malaria, Nature 280, 245-247.
    • (1979) Nature , vol.280 , pp. 245-247
    • Friedman, M.J.1
  • 16
    • 0024595407 scopus 로고
    • Catalase and glutathione peroxidase are equally active in the detoxification of hydrogen peroxide in human erythrocytes
    • Gaetani, G. F., Canepa, L., Galiano, S., Ferraris, A. M. & Kirkman, H. N. (1989) Catalase and glutathione peroxidase are equally active in the detoxification of hydrogen peroxide in human erythrocytes, Blood 73, 334-339.
    • (1989) Blood , vol.73 , pp. 334-339
    • Gaetani, G.F.1    Canepa, L.2    Galiano, S.3    Ferraris, A.M.4    Kirkman, H.N.5
  • 17
    • 0028034347 scopus 로고
    • Transport pathways in the malaria-infected erythrocyte - Their characterization and their use as potential targets for chemotherapy
    • Ginsburg, H. (1994) Transport pathways in the malaria-infected erythrocyte - Their characterization and their use as potential targets for chemotherapy, Biochem. Pharmacol. 8, 1847-1856.
    • (1994) Biochem. Pharmacol. , vol.8 , pp. 1847-1856
    • Ginsburg, H.1
  • 18
    • 0023186359 scopus 로고
    • Biophysical analysis of novel transport pathways induced in red blood cell membranes
    • Ginsburg, H. & Stein, W. D. (1987) Biophysical analysis of novel transport pathways induced in red blood cell membranes, J. Membr. Biol. 96, 1-10.
    • (1987) J. Membr. Biol. , vol.96 , pp. 1-10
    • Ginsburg, H.1    Stein, W.D.2
  • 19
    • 85047695929 scopus 로고
    • The redox status of malaria-infected erythrocytes: An overview with an emphasis on unresolved problems
    • Ginsburg, H. & Atamna, H. (1994) The redox status of malaria-infected erythrocytes: An overview with an emphasis on unresolved problems, Parasite 1, 5-13.
    • (1994) Parasite , vol.1 , pp. 5-13
    • Ginsburg, H.1    Atamna, H.2
  • 20
    • 0022628129 scopus 로고
    • Fffect of red blood cell potassium and hypertonicity on the growth of Plasmodium falciparum in culture
    • Ginsburg, H., Handeli, S., Friedman, S., Gorodetski, R. & Krugliak, M. (1986) Fffect of red blood cell potassium and hypertonicity on the growth of Plasmodium falciparum in culture, Z. Parasitenkd. 72, 185-199.
    • (1986) Z. Parasitenkd. , vol.72 , pp. 185-199
    • Ginsburg, H.1    Handeli, S.2    Friedman, S.3    Gorodetski, R.4    Krugliak, M.5
  • 21
    • 0024440219 scopus 로고
    • Oxidant stress and malaria: Host-parasite interrelationships in normal and abnormal erythrocytes
    • Golenser, J. & Chevion, M. (1989) Oxidant stress and malaria: host-parasite interrelationships in normal and abnormal erythrocytes, Semin. Hematol. 26, 313-325.
    • (1989) Semin. Hematol. , vol.26 , pp. 313-325
    • Golenser, J.1    Chevion, M.2
  • 22
    • 0028929633 scopus 로고
    • Plasmodium falciparum and Plasmodium berghei: Effect of magnesium on the development of parasitemia
    • Hess, F. I., Kilian, A., Söllner, W., Nothdurft, H. D., Pröll, S. & Löscher, T. (1995) Plasmodium falciparum and Plasmodium berghei: effect of magnesium on the development of parasitemia, Exp. Parasitol. 80, 186-193.
    • (1995) Exp. Parasitol. , vol.80 , pp. 186-193
    • Hess, F.I.1    Kilian, A.2    Söllner, W.3    Nothdurft, H.D.4    Pröll, S.5    Löscher, T.6
  • 23
    • 0017064979 scopus 로고
    • A fluorometric method for determination of oxidized and reduced glutathione in tissues
    • Hissin, P. J. & Hilf, R. (1976) A fluorometric method for determination of oxidized and reduced glutathione in tissues, Anal. Biochem. 74, 214-226.
    • (1976) Anal. Biochem. , vol.74 , pp. 214-226
    • Hissin, P.J.1    Hilf, R.2
  • 24
    • 0025203611 scopus 로고
    • Oxidative stress and the redox status of malaria-infected erythrocytes
    • N.Y.
    • Hunt, N. H. & Stoker, R. (1990) Oxidative stress and the redox status of malaria-infected erythrocytes, Blood Cells (N.Y.) 16, 499-526.
    • (1990) Blood Cells , vol.16 , pp. 499-526
    • Hunt, N.H.1    Stoker, R.2
  • 25
    • 0014470533 scopus 로고
    • Studies in the enzymology of glutathione metabolism in human erythrocytes
    • Jackson, R. C. (1969) Studies in the enzymology of glutathione metabolism in human erythrocytes, Biochem. J. 111, 309-315.
    • (1969) Biochem. J. , vol.111 , pp. 309-315
    • Jackson, R.C.1
  • 26
    • 0018237740 scopus 로고
    • Concentration from continuous culture of erythrocytes infected with trophozoites and schizonts of Plasmodium falciparum
    • Jensen, J. B. (1978) Concentration from continuous culture of erythrocytes infected with trophozoites and schizonts of Plasmodium falciparum, Am. J. Trop. Med. Hyg. 27, 1274-1276.
    • (1978) Am. J. Trop. Med. Hyg. , vol.27 , pp. 1274-1276
    • Jensen, J.B.1
  • 27
    • 0024584529 scopus 로고
    • Metabolic interconnection between the human malarial parasite Plasmodium falciparum and its host erythrocyte. Regulation of ATP levels by means of adenylate translocator and adenylate kinase
    • Kanaani, J. & Ginsburg, H. (1989) Metabolic interconnection between the human malarial parasite Plasmodium falciparum and its host erythrocyte. Regulation of ATP levels by means of adenylate translocator and adenylate kinase, J. Biol. Chem. 264, 3194-3199.
    • (1989) J. Biol. Chem. , vol.264 , pp. 3194-3199
    • Kanaani, J.1    Ginsburg, H.2
  • 28
    • 0028136546 scopus 로고
    • Transport of diverse substrates into malaria-infected erythrocytes via a pathway showing functional characteristics of a chloride channel
    • Kirk, K., Horner, H. A., Elford, B. C., Ellory, C. L. & Newbold, C. I. (1994) Transport of diverse substrates into malaria-infected erythrocytes via a pathway showing functional characteristics of a chloride channel, J. Biol. Chem. 269, 3339-3347.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3339-3347
    • Kirk, K.1    Horner, H.A.2    Elford, B.C.3    Ellory, C.L.4    Newbold, C.I.5
  • 29
    • 0039476506 scopus 로고
    • Glulathione transport by inside-out vesicles from human erythrocytes
    • Kondo, T., Dale, G. L. & Beutler, E. (1980) Glulathione transport by inside-out vesicles from human erythrocytes, Proc. Natl Acad. Sci. USA 77, 6359-6362.
    • (1980) Proc. Natl Acad. Sci. USA , vol.77 , pp. 6359-6362
    • Kondo, T.1    Dale, G.L.2    Beutler, E.3
  • 31
    • 0029197016 scopus 로고
    • Thiol transport from human red blood cells
    • Kondo, T., Dale, G. L. & Beutler, E. (1995) Thiol transport from human red blood cells, Methods Enzymol. 252, 72-82.
    • (1995) Methods Enzymol. , vol.252 , pp. 72-82
    • Kondo, T.1    Dale, G.L.2    Beutler, E.3
  • 32
    • 0026253211 scopus 로고
    • Calcium transport and compartment analysis of free and exchangeable calcium in Plasmodium falciparum-infected red blood cells
    • Kramer, R. & Ginsburg, H. (1991) Calcium transport and compartment analysis of free and exchangeable calcium in Plasmodium falciparum-infected red blood cells, J. Protozool. 38, 594-601.
    • (1991) J. Protozool. , vol.38 , pp. 594-601
    • Kramer, R.1    Ginsburg, H.2
  • 34
    • 0030025118 scopus 로고    scopus 로고
    • Glutathione reductase and glutamate dehydrogenase of Plasmodium falciparum, the causative agent of tropical malaria
    • Krauth-Siegel, R. L., Muller, J. G., Lottspeich, F. & Schirmer, R. H. (1996) Glutathione reductase and glutamate dehydrogenase of Plasmodium falciparum, the causative agent of tropical malaria, Eur. J. Biochem. 235, 345-350.
    • (1996) Eur. J. Biochem. , vol.235 , pp. 345-350
    • Krauth-Siegel, R.L.1    Muller, J.G.2    Lottspeich, F.3    Schirmer, R.H.4
  • 35
    • 0028035077 scopus 로고
    • Glutathione regeneration in calcium-loaded erythrocytes: A possible relationship among calcium accumulation, ATP decrement and oxidative damage
    • Kurata, M. & Suzuki, S. (1994) Glutathione regeneration in calcium-loaded erythrocytes: a possible relationship among calcium accumulation, ATP decrement and oxidative damage, Comp. Biochem. Physiol. 109B, 305-312.
    • (1994) Comp. Biochem. Physiol. , vol.109 B , pp. 305-312
    • Kurata, M.1    Suzuki, S.2
  • 36
    • 0022378096 scopus 로고
    • Characterization of permeation pathways in the plasma membrane of human erythrocytes infected with early stages of Plasmodium falciparum: Association with parasite development
    • Kutner, S., Breuer, W. V., Ginsburg, H., Aley, S. B. & Cabantchik, Z. I. (1985) Characterization of permeation pathways in the plasma membrane of human erythrocytes infected with early stages of Plasmodium falciparum: association with parasite development, J. Cell. Physiol. 125, 521-527.
    • (1985) J. Cell. Physiol. , vol.125 , pp. 521-527
    • Kutner, S.1    Breuer, W.V.2    Ginsburg, H.3    Aley, S.B.4    Cabantchik, Z.I.5
  • 37
    • 0023145791 scopus 로고
    • On the mode of action of phlorizin as an antimalarial agent in in vitro cultures of Plasmodium falciparum
    • Kutner, S., Breuer, W. V., Ginsburg, H. & Cabantchik, Z. I. (1987) On the mode of action of phlorizin as an antimalarial agent in in vitro cultures of Plasmodium falciparum, Biochem. Pharmacol. 36, 123-129.
    • (1987) Biochem. Pharmacol. , vol.36 , pp. 123-129
    • Kutner, S.1    Breuer, W.V.2    Ginsburg, H.3    Cabantchik, Z.I.4
  • 38
    • 0018704491 scopus 로고
    • Synchronization of Plasmodium falciparum erythrocytic stages in culture
    • Lambros, C. & Vanderberg, J. (1979) Synchronization of Plasmodium falciparum erythrocytic stages in culture, J. Parasitol. 65, 418-420.
    • (1979) J. Parasitol. , vol.65 , pp. 418-420
    • Lambros, C.1    Vanderberg, J.2
  • 39
    • 0023774774 scopus 로고
    • X-ray microanalysis of Plasmodium falciparum and infected red blood cells: Effects of qinghaosu and chloroquine on potassium, sodium and phosphorous composition
    • Lee, P., Ye, Z., van Dyke, K. & Kirk, R. (1988) X-ray microanalysis of Plasmodium falciparum and infected red blood cells: effects of qinghaosu and chloroquine on potassium, sodium and phosphorous composition, Am. J. Trop. Med. Hyg. 39, 157-165.
    • (1988) Am. J. Trop. Med. Hyg. , vol.39 , pp. 157-165
    • Lee, P.1    Ye, Z.2    Van Dyke, K.3    Kirk, R.4
  • 40
    • 0018750970 scopus 로고
    • Transport accounts for glutathione turnover in human erythrocytes
    • Lunn, G., Dale, G. L. & Beutler, E. (1979) Transport accounts for glutathione turnover in human erythrocytes, Blood 54, 238-244.
    • (1979) Blood , vol.54 , pp. 238-244
    • Lunn, G.1    Dale, G.L.2    Beutler, E.3
  • 41
    • 0027408401 scopus 로고
    • Magnesium deficiency affects malaria susceptibility in mice
    • Maurois, P., Gueux, E. & Rayssiguier, Y. (1993) Magnesium deficiency affects malaria susceptibility in mice, J. Am Coll. Nutr. 1, 21-25.
    • (1993) J. Am Coll. Nutr. , vol.1 , pp. 21-25
    • Maurois, P.1    Gueux, E.2    Rayssiguier, Y.3
  • 42
    • 77956912564 scopus 로고
    • Glutathione synthesis
    • Meister, A. (1974) Glutathione synthesis, Enzymes 10, 671-697.
    • (1974) Enzymes , vol.10 , pp. 671-697
    • Meister, A.1
  • 43
    • 0025895933 scopus 로고
    • Thioltransferase in human red blood cells: Purification and properties
    • Mieyal, J. J., Starke, D. W., Gravina, S. A., Dothey, C. & Chung, J. S. (1991) Thioltransferase in human red blood cells: purification and properties, J. Biol. Chem. 30, 6088-6097.
    • (1991) J. Biol. Chem. , vol.30 , pp. 6088-6097
    • Mieyal, J.J.1    Starke, D.W.2    Gravina, S.A.3    Dothey, C.4    Chung, J.S.5
  • 44
    • 0021264559 scopus 로고
    • Plasmodium falciparum: Thiol status and growth in normal and glucose-6-phosphate deficient human erythrocytes
    • Miller, J., Golenser, J., Spira, D. T. & Kosower, N. S. (1984) Plasmodium falciparum: thiol status and growth in normal and glucose-6-phosphate deficient human erythrocytes, Exp. Parasitol. 57, 239-247.
    • (1984) Exp. Parasitol. , vol.57 , pp. 239-247
    • Miller, J.1    Golenser, J.2    Spira, D.T.3    Kosower, N.S.4
  • 45
    • 0024810732 scopus 로고
    • Reduced glutathione in combination with superoxide dismutase as an important biological antioxidant defense mechanism
    • Munday, R. & Winterbourn, C. C. (1989) Reduced glutathione in combination with superoxide dismutase as an important biological antioxidant defense mechanism, Biochem. Pharmacol. 38, 4349-4352.
    • (1989) Biochem. Pharmacol. , vol.38 , pp. 4349-4352
    • Munday, R.1    Winterbourn, C.C.2
  • 46
    • 0024322509 scopus 로고
    • Glutathione measurement by high performance liquid chromatography separation and fluorometric detection of the glutathione orthophtalaldehyde adduct
    • Neuschwander-Tetri, B. A. & Roll, F. J. (1989) Glutathione measurement by high performance liquid chromatography separation and fluorometric detection of the glutathione orthophtalaldehyde adduct, Anal. Biochem. 179, 236-241.
    • (1989) Anal. Biochem. , vol.179 , pp. 236-241
    • Neuschwander-Tetri, B.A.1    Roll, F.J.2
  • 47
    • 0016796892 scopus 로고
    • Glutathionestatus of Plasmodium vinckei parasitized erythrocytes in correlation to the intraerythrocytic development of the parasite
    • Pickard-Moreau, A., Hempelmann, E., Krammer, G., Jackisch, R. & Jung, A. (1975) Glutathionestatus of Plasmodium vinckei parasitized erythrocytes in correlation to the intraerythrocytic development of the parasite, Tropenmed. Parasitol. 26, 405-416.
    • (1975) Tropenmed. Parasitol. , vol.26 , pp. 405-416
    • Pickard-Moreau, A.1    Hempelmann, E.2    Krammer, G.3    Jackisch, R.4    Jung, A.5
  • 49
    • 0025317268 scopus 로고
    • Glutathione: Toxicological implications
    • Reed, D. J. (1990) Glutathione: toxicological implications, Annu. Rev. Pharmacol. Toxicol. 30, 603-631.
    • (1990) Annu. Rev. Pharmacol. Toxicol. , vol.30 , pp. 603-631
    • Reed, D.J.1
  • 50
    • 0020262488 scopus 로고
    • Glutahione stability and oxidative stress in Plasmodium falciparum infection vitro: Response of normal and G6PD deficient cells
    • Roth, E. F., Raventos-Suarez C., Perkins, M. & Nagel, R. L. (1982) Glutahione stability and oxidative stress in Plasmodium falciparum infection vitro: response of normal and G6PD deficient cells, Biochem. Biophys. Res. Commun. 109, 355-362.
    • (1982) Biochem. Biophys. Res. Commun. , vol.109 , pp. 355-362
    • Roth, E.F.1    Raventos-Suarez, C.2    Perkins, M.3    Nagel, R.L.4
  • 51
    • 0022592318 scopus 로고
    • Pathways for the reduction of oxidized glutathione in the Plasmodium falciparum-infected erythrocyte: Can parasite enzymes replace host red cell glucose-6-phosphate dehydrogenase?
    • Roth, E. F. Jr, Schulman, S., Vanderberg, J. & Olson, J. A. (1986a) Pathways for the reduction of oxidized glutathione in the Plasmodium falciparum-infected erythrocyte: can parasite enzymes replace host red cell glucose-6-phosphate dehydrogenase? Blood 67, 827-830.
    • (1986) Blood , vol.67 , pp. 827-830
    • Roth Jr., E.F.1    Schulman, S.2    Vanderberg, J.3    Olson, J.A.4
  • 52
    • 0022553044 scopus 로고
    • Ribose metabolism and nucleic acid synthesis in normal and glucose-6-phosphate dehydrogenase-deficient human erythrocytes infected with Plasmodium falciparum
    • Roth, E. F. Jr, Ruprecht, R. M., Schulman, S., Vanderberg, J. & Olson, J. A. (1986b) Ribose metabolism and nucleic acid synthesis in normal and glucose-6-phosphate dehydrogenase-deficient human erythrocytes infected with Plasmodium falciparum, J. Clin. Invest. 77, 1129-1135.
    • (1986) J. Clin. Invest. , vol.77 , pp. 1129-1135
    • Roth Jr., E.F.1    Ruprecht, R.M.2    Schulman, S.3    Vanderberg, J.4    Olson, J.A.5
  • 53
    • 85044684616 scopus 로고
    • Malarial parasite hexokinase-dependent glutathione reduction in the Plasmodium falciparum-infected human erythrocyte
    • Roth, E. F. Jr (1987) Malarial parasite hexokinase-dependent glutathione reduction in the Plasmodium falciparum-infected human erythrocyte, J. Biol. Chem. 262, 15678-15682.
    • (1987) J. Biol. Chem. , vol.262 , pp. 15678-15682
    • Roth Jr., E.F.1
  • 54
    • 0025831956 scopus 로고
    • NADPH, not glutathione, status modulates oxidant sensitivity in normal and glucose-6-phosphate dehydrogenase-deficient erythrocytes
    • Scott, M. D., Zuo, L., Lubin, B. H. & Chiu, D. T.-Y. (1991a) NADPH, not glutathione, status modulates oxidant sensitivity in normal and glucose-6-phosphate dehydrogenase-deficient erythrocytes, Blood 77, 2059-2064.
    • (1991) Blood , vol.77 , pp. 2059-2064
    • Scott, M.D.1    Zuo, L.2    Lubin, B.H.3    Chiu, D.T.-Y.4
  • 55
    • 0025827312 scopus 로고
    • Erythrocyte defense against hydrogen peroxide: Preeminent importance of catalase
    • Scott, M. D., Lubin, B. H., Zuo, L. & Kuypers, F. A. (1991b) Erythrocyte defense against hydrogen peroxide: preeminent importance of catalase, J. Lab. Clin. Med. 118, 7-16.
    • (1991) J. Lab. Clin. Med. , vol.118 , pp. 7-16
    • Scott, M.D.1    Lubin, B.H.2    Zuo, L.3    Kuypers, F.A.4
  • 56
    • 0022339848 scopus 로고
    • Plasmodium berghei: Oxidant defense system
    • Seth, R. K., Saini, A. & Jaswal, T. (1985) Plasmodium berghei: oxidant defense system, Exp. Parasitol. 60, 414-416.
    • (1985) Exp. Parasitol. , vol.60 , pp. 414-416
    • Seth, R.K.1    Saini, A.2    Jaswal, T.3
  • 58
    • 0006750037 scopus 로고
    • Synthesis of glutathione from γ-glutamylcysteine
    • Snoke, J. E., Yanari, S. & Bloch, K. (1953) Synthesis of glutathione from γ-glutamylcysteine, J. Biol. Chem. 201, 573-586.
    • (1953) J. Biol. Chem. , vol.201 , pp. 573-586
    • Snoke, J.E.1    Yanari, S.2    Bloch, K.3
  • 59
    • 0014669262 scopus 로고
    • The transport of oxidized glutathione from human erythrocytes
    • Srivastava, S. K. & Beutler, E. (1969) The transport of oxidized glutathione from human erythrocytes, J. Biol. Chem. 244, 9-16.
    • (1969) J. Biol. Chem. , vol.244 , pp. 9-16
    • Srivastava, S.K.1    Beutler, E.2
  • 60
    • 0029015864 scopus 로고
    • Protein sulfhydryls and their role in the antioxidant function of protein S-thiolation
    • Thomas, J. A., Poland, B. & Honzatko, R. (1995) Protein sulfhydryls and their role in the antioxidant function of protein S-thiolation, Arch. Biochem. Biophys. 319, 1-9.
    • (1995) Arch. Biochem. Biophys. , vol.319 , pp. 1-9
    • Thomas, J.A.1    Poland, B.2    Honzatko, R.3
  • 61
    • 0345033959 scopus 로고
    • Energy sources in glutathione synthesis
    • Yanari, S., Snoke, J. E. & Block, K. (1953) Energy sources in glutathione synthesis, J. Biol. Chem. 201, 561-571.
    • (1953) J. Biol. Chem. , vol.201 , pp. 561-571
    • Yanari, S.1    Snoke, J.E.2    Block, K.3
  • 62
    • 0345652158 scopus 로고
    • Identification of the acidic compartment of Plasmodium falciparum-infected human erythrocytes as the target of the antimalarial drug chloroquine
    • Yayon, A., Cabantchik, Z. I. & Ginsburg, H. (1984) Identification of the acidic compartment of Plasmodium falciparum-infected human erythrocytes as the target of the antimalarial drug chloroquine, EMBO J. 3, 2695-2700.
    • (1984) EMBO J. , vol.3 , pp. 2695-2700
    • Yayon, A.1    Cabantchik, Z.I.2    Ginsburg, H.3
  • 63
    • 0023853092 scopus 로고
    • Glutathione reductase inhibitors as potential antimalarial drugs. Effects of nitro-soureas on Plasmodium falciparum in vitro
    • Zhang, Y., Hempelmann, E. & Schirmer, R. H. (1988a) Glutathione reductase inhibitors as potential antimalarial drugs. Effects of nitro-soureas on Plasmodium falciparum in vitro, Biochem. Pharmacol. 37, 855-860.
    • (1988) Biochem. Pharmacol. , vol.37 , pp. 855-860
    • Zhang, Y.1    Hempelmann, E.2    Schirmer, R.H.3
  • 64
    • 0023831311 scopus 로고
    • Glutathione reductase-deficient erythrocytes as host cells of malarial parasites
    • Zhang, Y., König, J. & Schirmer, R. H. (1988b) Glutathione reductase-deficient erythrocytes as host cells of malarial parasites, Biochem. Pharmacol. 37, 861-865.
    • (1988) Biochem. Pharmacol. , vol.37 , pp. 861-865
    • Zhang, Y.1    König, J.2    Schirmer, R.H.3
  • 65
    • 0021891877 scopus 로고
    • Role of reversible oxidation-reduction of enzyme thiols-disulfides in metabolic regulation
    • Ziegler, D. M. (1985) Role of reversible oxidation-reduction of enzyme thiols-disulfides in metabolic regulation, Annu. Rev. Biochem. 54, 305-329.
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 305-329
    • Ziegler, D.M.1


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