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Volumn 58, Issue 11, 1999, Pages 1791-1799

Nitrofuran drugs as common subversive substrates of Trypanosoma cruzi lipoamide dehydrogenase and trypanothione reductase

Author keywords

Chagas' disease; Lipoamide dehydrogenase; Nitrofurans; Redox cycling; Trypanosoma cruzi; Trypanothione reductase

Indexed keywords

DIHYDROLIPOAMIDE DEHYDROGENASE; FLAVOPROTEIN; GLUTATHIONE REDUCTASE; NIFUROXAZIDE; NIFUROXIME; NITROFURAN DERIVATIVE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; SUPEROXIDE; TRYPANOTHIONE;

EID: 0345035516     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-2952(99)00264-6     Document Type: Article
Times cited : (95)

References (44)
  • 1
    • 0024020604 scopus 로고
    • Toxic effects of nifurtimox and benznidazole, two drugs used against American trypanosomiasis (Chagas' disease)
    • Castro J.A., Diaz de Toranzo E.G. Toxic effects of nifurtimox and benznidazole, two drugs used against American trypanosomiasis (Chagas' disease). Biomed Environ Sci. 1:1988;19-33.
    • (1988) Biomed Environ Sci , vol.1 , pp. 19-33
    • Castro, J.A.1    Diaz De Toranzo, E.G.2
  • 2
    • 0024472574 scopus 로고
    • Thirteenfold increase of chromosomal aberrations non-randomly distributed in chagasic children treated with nifurtimox
    • Gorla N.B., Ledesma O.S., Barbieri G.P., Larripa I.B. Thirteenfold increase of chromosomal aberrations non-randomly distributed in chagasic children treated with nifurtimox. Mutat Res. 224:1989;263-267.
    • (1989) Mutat Res , vol.224 , pp. 263-267
    • Gorla, N.B.1    Ledesma, O.S.2    Barbieri, G.P.3    Larripa, I.B.4
  • 3
    • 0022002912 scopus 로고
    • Trypanothione: A novel bis(glutathionyl)spermidine cofactor for glutathione reductase in trypanosomatids
    • Fairlamb A.H., Blackburn P., Ulrich P., Chait B.T., Cerami A. Trypanothione A novel bis(glutathionyl)spermidine cofactor for glutathione reductase in trypanosomatids . Science. 227:1985;1485-1487.
    • (1985) Science , vol.227 , pp. 1485-1487
    • Fairlamb, A.H.1    Blackburn, P.2    Ulrich, P.3    Chait, B.T.4    Cerami, A.5
  • 4
    • 0023051830 scopus 로고
    • Purification and characterization of trypanothione reductase from Crithidia fasciculata, a newly discovered member of the family of disulfide-containing flavoprotein reductases
    • Shames S.L., Fairlamb A.H., Cerami A., Walsh C.T. Purification and characterization of trypanothione reductase from Crithidia fasciculata, a newly discovered member of the family of disulfide-containing flavoprotein reductases. Biochemistry. 25:1986;3519-3526.
    • (1986) Biochemistry , vol.25 , pp. 3519-3526
    • Shames, S.L.1    Fairlamb, A.H.2    Cerami, A.3    Walsh, C.T.4
  • 5
    • 0023150396 scopus 로고
    • Trypanothione reductase from Trypanosoma cruzi. Purification and characterization of the crystalline enzyme
    • Krauth-Siegel R.L., Enders B., Henderson G.B., Fairlamb A.H., Schirmer R.H. Trypanothione reductase from Trypanosoma cruzi. Purification and characterization of the crystalline enzyme. Eur J Biochem. 164:1987;123-128.
    • (1987) Eur J Biochem , vol.164 , pp. 123-128
    • Krauth-Siegel, R.L.1    Enders, B.2    Henderson, G.B.3    Fairlamb, A.H.4    Schirmer, R.H.5
  • 6
    • 0032955828 scopus 로고    scopus 로고
    • Evidence for the co-existence of glutathione reductase and trypanothione reductase in the non-trypanosomatid Euglenozoa: Euglena gracilis Z
    • Montrichard F., Le Guen F., Laval-Martin D.L., Davioud-Charvet E. Evidence for the co-existence of glutathione reductase and trypanothione reductase in the non-trypanosomatid Euglenozoa Euglena gracilis Z . FEBS Lett. 442:1999;29-33.
    • (1999) FEBS Lett , vol.442 , pp. 29-33
    • Montrichard, F.1    Le Guen, F.2    Laval-Martin, D.L.3    Davioud-Charvet, E.4
  • 7
    • 0000208163 scopus 로고
    • The identity of diaphorase and lipoyl dehydrogenase
    • Massey V. The identity of diaphorase and lipoyl dehydrogenase. Biochim Biophys Acta. 37:1960;314-322.
    • (1960) Biochim Biophys Acta , vol.37 , pp. 314-322
    • Massey, V.1
  • 8
    • 0025337155 scopus 로고
    • The mechanism of the quinone reductase reaction of pig heart lipoamide dehydrogenase
    • Vienozinskis J., Butkus A., Cenas N., Kulys J. The mechanism of the quinone reductase reaction of pig heart lipoamide dehydrogenase. Biochem J. 269:1990;101-105.
    • (1990) Biochem J , vol.269 , pp. 101-105
    • Vienozinskis, J.1    Butkus, A.2    Cenas, N.3    Kulys, J.4
  • 9
    • 0025048534 scopus 로고
    • Catalysis of nitrofuran redox-cycling and superoxide anion production by heart lipoamide dehydrogenase
    • Sreider C.M., Grinblat L., Stoppani A.O.M. Catalysis of nitrofuran redox-cycling and superoxide anion production by heart lipoamide dehydrogenase. Biochem Pharmacol. 40:1990;1849-1857.
    • (1990) Biochem Pharmacol , vol.40 , pp. 1849-1857
    • Sreider, C.M.1    Grinblat, L.2    Stoppani, A.O.M.3
  • 10
    • 0026013398 scopus 로고
    • Superoxide anion production by lipoamide dehydrogenase redox-cycling: Effect of enzyme modifiers
    • Grinblat L., Sreider C.M., Stoppani A.O.M. Superoxide anion production by lipoamide dehydrogenase redox-cycling Effect of enzyme modifiers . Biochem Int. 23:1991;83-92.
    • (1991) Biochem Int , vol.23 , pp. 83-92
    • Grinblat, L.1    Sreider, C.M.2    Stoppani, A.O.M.3
  • 11
    • 0000876731 scopus 로고
    • Lipoamide dehydrogenase, glutathione reductase, thioredoxin reductase, and mercuric ion reductase - A family of flavoenzyme transhydrogenases
    • Müller F. Boca Raton: CRC Press
    • Williams C.H. Jr. Lipoamide dehydrogenase, glutathione reductase, thioredoxin reductase, and mercuric ion reductase - a family of flavoenzyme transhydrogenases. Müller F. Chemistry and Biochemistry of Flavoenzymes. Vol. III:1992;121-211 CRC Press, Boca Raton.
    • (1992) Chemistry and Biochemistry of Flavoenzymes , vol.3 , pp. 121-211
    • Williams C.H., Jr.1
  • 12
    • 33748233963 scopus 로고
    • Disulfide reductase inhibitors as chemotherapeutic agents: The design of drugs for trypanosomiasis and malaria
    • Schirmer R.H., Müller J.G., Krauth-Siegel R.L. Disulfide reductase inhibitors as chemotherapeutic agents The design of drugs for trypanosomiasis and malaria . Angew Chem Int Ed Engl. 34:1995;141-154.
    • (1995) Angew Chem Int Ed Engl , vol.34 , pp. 141-154
    • Schirmer, R.H.1    Müller, J.G.2    Krauth-Siegel, R.L.3
  • 13
    • 0025613353 scopus 로고
    • Purification and characterization of lipoamide dehydrogenase from Trypanosoma cruzi
    • Lohrer H., Krauth-Siegel R.L. Purification and characterization of lipoamide dehydrogenase from Trypanosoma cruzi. Eur J Biochem. 194:1990;863-869.
    • (1990) Eur J Biochem , vol.194 , pp. 863-869
    • Lohrer, H.1    Krauth-Siegel, R.L.2
  • 14
    • 0026098498 scopus 로고
    • Cloning, sequencing, overproduction and purification of trypanothione reductase from Trypanosoma cruzi
    • Sullivan F.X., Walsh C.T. Cloning, sequencing, overproduction and purification of trypanothione reductase from Trypanosoma cruzi. Mol Biochem Parasitol. 44:1991;145-147.
    • (1991) Mol Biochem Parasitol , vol.44 , pp. 145-147
    • Sullivan, F.X.1    Walsh, C.T.2
  • 15
    • 0031024753 scopus 로고    scopus 로고
    • Cloning, sequencing and functional expression of dihydrolipoamide dehydrogenase from the human pathogen Trypanosoma cruzi
    • Schöneck R., Billaut-Mulot O., Numrich P., Ouaissi M.A., Krauth-Siegel R.L. Cloning, sequencing and functional expression of dihydrolipoamide dehydrogenase from the human pathogen Trypanosoma cruzi. Eur J Biochem. 243:1997;739-747.
    • (1997) Eur J Biochem , vol.243 , pp. 739-747
    • Schöneck, R.1    Billaut-Mulot, O.2    Numrich, P.3    Ouaissi, M.A.4    Krauth-Siegel, R.L.5
  • 16
    • 0029360570 scopus 로고
    • Trypanothione reductase and lipoamide dehydrogenase as targets for a structure-based drug design
    • Krauth-Siegel R.L., Schöneck R. Trypanothione reductase and lipoamide dehydrogenase as targets for a structure-based drug design. FASEB J. 9:1995;1138-1146.
    • (1995) FASEB J , vol.9 , pp. 1138-1146
    • Krauth-Siegel, R.L.1    Schöneck, R.2
  • 17
    • 0026793462 scopus 로고
    • Metabolism and functions of trypanothione in the kinetoplastida
    • Fairlamb A.H., Cerami A. Metabolism and functions of trypanothione in the kinetoplastida. Annu Rev Microbiol. 46:1992;695-729.
    • (1992) Annu Rev Microbiol , vol.46 , pp. 695-729
    • Fairlamb, A.H.1    Cerami, A.2
  • 18
    • 0026445175 scopus 로고
    • Reduction of nitrofuran compounds by heart lipoamide dehydrogenase: Role of flavin and the reactive disulfide groups
    • Sreider C.M., Grinblat L., Stoppani A.O.M. Reduction of nitrofuran compounds by heart lipoamide dehydrogenase Role of flavin and the reactive disulfide groups . Biochem Int. 28:1992;323-334.
    • (1992) Biochem Int , vol.28 , pp. 323-334
    • Sreider, C.M.1    Grinblat, L.2    Stoppani, A.O.M.3
  • 19
    • 0018682874 scopus 로고
    • Generation of superoxide anion and hydrogen peroxide induced by nifurtimox in Trypanosoma cruzi
    • Docampo R., Stoppani A.O.M. Generation of superoxide anion and hydrogen peroxide induced by nifurtimox in Trypanosoma cruzi. Arch Biochem Biophys. 197:1979;317-321.
    • (1979) Arch Biochem Biophys , vol.197 , pp. 317-321
    • Docampo, R.1    Stoppani, A.O.M.2
  • 20
    • 0025166484 scopus 로고
    • Sensitivity of parasites to free radical damage by antiparasitic drugs
    • Docampo R. Sensitivity of parasites to free radical damage by antiparasitic drugs. Chem Biol Interact. 73:1990;1-27.
    • (1990) Chem Biol Interact , vol.73 , pp. 1-27
    • Docampo, R.1
  • 21
    • 0021401673 scopus 로고
    • Free radical metabolites in the mode of action of chemotherapeutic agents and phagocytic cells on Trypanosoma cruzi
    • Docampo R., Moreno S.N.J. Free radical metabolites in the mode of action of chemotherapeutic agents and phagocytic cells on Trypanosoma cruzi. Rev Infect Dis. 6:1984;223-238.
    • (1984) Rev Infect Dis , vol.6 , pp. 223-238
    • Docampo, R.1    Moreno, S.N.J.2
  • 22
    • 0030911717 scopus 로고    scopus 로고
    • Effects of nifurtimox and benznidazole upon glutathione and trypanothione content in epimastigote, trypomastigote and amastigote forms of Trypanosoma cruzi
    • Maya J.D., Repetto Y., Agosin M., Ojeda J.M., Tellez R., Gaule C., Morello A. Effects of nifurtimox and benznidazole upon glutathione and trypanothione content in epimastigote, trypomastigote and amastigote forms of Trypanosoma cruzi. Mol Biochem Parasitol. 86:1997;101-106.
    • (1997) Mol Biochem Parasitol , vol.86 , pp. 101-106
    • Maya, J.D.1    Repetto, Y.2    Agosin, M.3    Ojeda, J.M.4    Tellez, R.5    Gaule, C.6    Morello, A.7
  • 24
    • 0024521456 scopus 로고
    • Trypanothione reductase from Trypanosoma cruzi. Catalytic properties of the enzyme and inhibition studies with trypanocidal compounds
    • Jockers-Scherübl M.C., Schirmer R.H., Krauth-Siegel R.L. Trypanothione reductase from Trypanosoma cruzi. Catalytic properties of the enzyme and inhibition studies with trypanocidal compounds. Eur J Biochem. 180:1989;267-272.
    • (1989) Eur J Biochem , vol.180 , pp. 267-272
    • Jockers-Scherübl, M.C.1    Schirmer, R.H.2    Krauth-Siegel, R.L.3
  • 26
    • 0023810590 scopus 로고
    • "subversive" substrates for the enzyme trypanothione disulfide reductase: Alternative approach to chemotherapy of Chagas disease
    • Henderson G.B., Ulrich P., Fairlamb A.H., Rosenberg I., Pereira M., Sela M., Cerami A. "Subversive" substrates for the enzyme trypanothione disulfide reductase Alternative approach to chemotherapy of Chagas disease . Proc Natl Acad Sci USA. 85:1988;5374-5378.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 5374-5378
    • Henderson, G.B.1    Ulrich, P.2    Fairlamb, A.H.3    Rosenberg, I.4    Pereira, M.5    Sela, M.6    Cerami, A.7
  • 28
    • 0001752523 scopus 로고
    • Studies on the nature and reactions of protein-bound lipoic acid
    • Reed L.J., Koike M., Levitch M.E., Leach F.R. Studies on the nature and reactions of protein-bound lipoic acid. J Biol Chem. 232:1958;143-158.
    • (1958) J Biol Chem , vol.232 , pp. 143-158
    • Reed, L.J.1    Koike, M.2    Levitch, M.E.3    Leach, F.R.4
  • 29
    • 0027407908 scopus 로고
    • Crystallization and preliminary crystallographic analysis of trypanothione reductase from Trypanosoma cruzi, the causative agent of Chagas' disease
    • Krauth-Siegel R.L., Sticherling C., Jöst J., Walsh C.T., Pai E.F., Kabsch W., Lantwin C.B. Crystallization and preliminary crystallographic analysis of trypanothione reductase from Trypanosoma cruzi, the causative agent of Chagas' disease. FEBS Lett. 317:1993;105-108.
    • (1993) FEBS Lett , vol.317 , pp. 105-108
    • Krauth-Siegel, R.L.1    Sticherling, C.2    Jöst, J.3    Walsh, C.T.4    Pai, E.F.5    Kabsch, W.6    Lantwin, C.B.7
  • 30
    • 0027190591 scopus 로고
    • Folding of the four domains and dimerization are impaired by the Gly446→Glu exchange in human glutathione reductase. Implications for the design of antiparasitic drugs
    • Nordhoff A., Bücheler U.S., Werner D., Schirmer R.H. Folding of the four domains and dimerization are impaired by the Gly446→Glu exchange in human glutathione reductase. Implications for the design of antiparasitic drugs. Biochemistry. 32:1993;4060-4066.
    • (1993) Biochemistry , vol.32 , pp. 4060-4066
    • Nordhoff, A.1    Bücheler, U.S.2    Werner, D.3    Schirmer, R.H.4
  • 31
    • 0024948840 scopus 로고
    • Continuous cultivation of Trypanosoma brucei blood stream forms in a medium containing a low concentration of serum protein without feeder cell layers
    • Hirumi H., Hirumi K. Continuous cultivation of Trypanosoma brucei blood stream forms in a medium containing a low concentration of serum protein without feeder cell layers. J Parasitol. 75:1989;985-989.
    • (1989) J Parasitol , vol.75 , pp. 985-989
    • Hirumi, H.1    Hirumi, K.2
  • 32
    • 0017165455 scopus 로고
    • Glutathione reductase from human erythrocytes. Catalytic properties and aggregation
    • Worthington D.J., Rosemeyer M.A. Glutathione reductase from human erythrocytes. Catalytic properties and aggregation. Eur J Biochem. 67:1976;231-238.
    • (1976) Eur J Biochem , vol.67 , pp. 231-238
    • Worthington, D.J.1    Rosemeyer, M.A.2
  • 33
    • 0344993123 scopus 로고
    • Cytochrome c (Mammals)
    • Paul K.G. Cytochrome c (Mammals). Methods Enzymol. 2:1955;749-755.
    • (1955) Methods Enzymol , vol.2 , pp. 749-755
    • Paul, K.G.1
  • 34
    • 0021590709 scopus 로고
    • An in vitro system for determining the activity of compounds against the intracellular amastigote form of Leishmania donovani
    • Neal R.A., Croft S.L. An in vitro system for determining the activity of compounds against the intracellular amastigote form of Leishmania donovani. J Antimicrob Chemother. 14:1984;312-317.
    • (1984) J Antimicrob Chemother , vol.14 , pp. 312-317
    • Neal, R.A.1    Croft, S.L.2
  • 35
    • 0027429249 scopus 로고
    • A colorimetric assay for trypanosome viability and metabolic function
    • Ellis J.A., Fish W.R., Sileghem M., McOdimba F. A colorimetric assay for trypanosome viability and metabolic function. Vet Parasitol. 50:1993;143-149.
    • (1993) Vet Parasitol , vol.50 , pp. 143-149
    • Ellis, J.A.1    Fish, W.R.2    Sileghem, M.3    McOdimba, F.4
  • 36
    • 0024517136 scopus 로고
    • One- And two-electron reduction of quinones by glutathione reductase
    • Cenas N.K., Rakauskiene G.A., Kulys J.J. One- and two-electron reduction of quinones by glutathione reductase. Biochim Biophys Acta. 973:1989;399-404.
    • (1989) Biochim Biophys Acta , vol.973 , pp. 399-404
    • Cenas, N.K.1    Rakauskiene, G.A.2    Kulys, J.J.3
  • 37
    • 0028331764 scopus 로고
    • Mechanism of reduction of quinones by Trypanosoma congolense trypanothione reductase
    • Cenas N.K., Arscott D., Williams C.H. Jr, Blanchard J.S. Mechanism of reduction of quinones by Trypanosoma congolense trypanothione reductase. Biochemistry. 33:1994;2509-2515.
    • (1994) Biochemistry , vol.33 , pp. 2509-2515
    • Cenas, N.K.1    Arscott, D.2    Williams C.H., Jr.3    Blanchard, J.S.4
  • 38
    • 0013815696 scopus 로고
    • Studies on menadione reductase of bakers' yeast
    • Misaka E., Kawahara Y., Nakanishi K. Studies on menadione reductase of bakers' yeast. J Biochem. 58:1965;436-443.
    • (1965) J Biochem , vol.58 , pp. 436-443
    • Misaka, E.1    Kawahara, Y.2    Nakanishi, K.3
  • 40
    • 0024959343 scopus 로고
    • A crystallographic study of the glutathione binding site of glutathione reductase at 0.3-nm resolution
    • Karplus P.A., Pai E.F., Schulz G.E. A crystallographic study of the glutathione binding site of glutathione reductase at 0.3-nm resolution. Eur J Biochem. 178:1989;693-703.
    • (1989) Eur J Biochem , vol.178 , pp. 693-703
    • Karplus, P.A.1    Pai, E.F.2    Schulz, G.E.3
  • 41
    • 0022364492 scopus 로고
    • The activity of plumbagin and other electron carriers against Leishmania donovani and Leishmania mexicana amazonensis
    • Croft S.L., Evans A.T., Neal R.A. The activity of plumbagin and other electron carriers against Leishmania donovani and Leishmania mexicana amazonensis. Ann Trop Med Parasitol. 79:1985;651-653.
    • (1985) Ann Trop Med Parasitol , vol.79 , pp. 651-653
    • Croft, S.L.1    Evans, A.T.2    Neal, R.A.3


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