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Volumn 100, Issue 1-2, 2006, Pages 119-132

Increased expression of iron-containing superoxide dismutase-A (TcFeSOD-A) enzyme in Trypanosoma cruzi population with in vitro-induced resistance to benznidazole

Author keywords

Benznidazole; Differential gene expression; Drug resistance; Iron superoxide dismutase; Trypanosoma cruzi

Indexed keywords

BENZNIDAZOLE; SUPEROXIDE DISMUTASE;

EID: 33751423139     PISSN: 0001706X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.actatropica.2006.10.004     Document Type: Article
Times cited : (50)

References (51)
  • 1
    • 0038362437 scopus 로고    scopus 로고
    • Superoxide dismutase from the oyster parasite Perkinsus marinus: purification, biochemical characterization, and development of a plate microassay for activity
    • Ahmed H., Schott E.T., Gauthier J.D., and Vasta G.R. Superoxide dismutase from the oyster parasite Perkinsus marinus: purification, biochemical characterization, and development of a plate microassay for activity. Anal. Biochem. 318 (2003) 132-141
    • (2003) Anal. Biochem. , vol.318 , pp. 132-141
    • Ahmed, H.1    Schott, E.T.2    Gauthier, J.D.3    Vasta, G.R.4
  • 2
    • 0028206197 scopus 로고
    • Molecular characterization and overexpression of the hypoxantine-guanine phosphoribosyltransferase gene from Trypanosoma cruzi
    • Allen T., and Ullman B. Molecular characterization and overexpression of the hypoxantine-guanine phosphoribosyltransferase gene from Trypanosoma cruzi. Mol. Biochem. Parasitol. 65 (1994) 233-245
    • (1994) Mol. Biochem. Parasitol. , vol.65 , pp. 233-245
    • Allen, T.1    Ullman, B.2
  • 3
    • 0033256228 scopus 로고    scopus 로고
    • Recommendations from a satellite meeting
    • Anonymous. Recommendations from a satellite meeting. Mem. Inst. Oswaldo Cruz. 94 (1999) 429-432
    • (1999) Mem. Inst. Oswaldo Cruz. , vol.94 , pp. 429-432
  • 4
    • 0023463279 scopus 로고
    • Aspects of the structure, function and applications of superoxide dismutase
    • Bannister J.V., Bannister W.H., and Rotilio G. Aspects of the structure, function and applications of superoxide dismutase. Crit. Rev. Biochem. 22 (1987) 111-180
    • (1987) Crit. Rev. Biochem. , vol.22 , pp. 111-180
    • Bannister, J.V.1    Bannister, W.H.2    Rotilio, G.3
  • 5
    • 17644432619 scopus 로고
    • Interactions between immunity and chemotherapy in the treatment of the trypanosomiases and leishmaniases
    • Berger B.J., and Fairlamb A.H. Interactions between immunity and chemotherapy in the treatment of the trypanosomiases and leishmaniases. Parasitology 105 (1992) 871-878
    • (1992) Parasitology , vol.105 , pp. 871-878
    • Berger, B.J.1    Fairlamb, A.H.2
  • 6
    • 0017694023 scopus 로고
    • Hydrogen peroxide generation in Trypanosoma cruzi
    • Boveris A., and Stoppani A.O. Hydrogen peroxide generation in Trypanosoma cruzi. Experienta 33 (1977) 1306-1308
    • (1977) Experienta , vol.33 , pp. 1306-1308
    • Boveris, A.1    Stoppani, A.O.2
  • 7
    • 0022714941 scopus 로고
    • Fumarate reductase and other mitochondrial activities in Trypanosoma cruzi
    • Boveris A., Hertig C.M., and Turrens J.F. Fumarate reductase and other mitochondrial activities in Trypanosoma cruzi. Mol. Biol. Parasitol. 19 (1986) 163-169
    • (1986) Mol. Biol. Parasitol. , vol.19 , pp. 163-169
    • Boveris, A.1    Hertig, C.M.2    Turrens, J.F.3
  • 9
    • 78651145402 scopus 로고
    • Growth and differentiation in Trypanosoma cruzi. I. Origin of metacyclic trypanosomes in liquid media
    • Camargo E. Growth and differentiation in Trypanosoma cruzi. I. Origin of metacyclic trypanosomes in liquid media. Rev. Inst. Med. Trop. 6 (1964) 93-100
    • (1964) Rev. Inst. Med. Trop. , vol.6 , pp. 93-100
    • Camargo, E.1
  • 10
    • 0033953484 scopus 로고    scopus 로고
    • Separation of NADH-fumarate reductase and succinate dehydrogenase activities in Trypanosoma cruzi
    • Christmas P.B., and Turrens J.F. Separation of NADH-fumarate reductase and succinate dehydrogenase activities in Trypanosoma cruzi. FEMS Microb. Letters 183 (2000) 225-228
    • (2000) FEMS Microb. Letters , vol.183 , pp. 225-228
    • Christmas, P.B.1    Turrens, J.F.2
  • 11
    • 0021401673 scopus 로고
    • Free radical metabolites in the mode of action of chemotherapeutic agents and phagocytic cells on Trypanosoma cruzi
    • Docampo R., and Moreno S.N. 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.2
  • 12
    • 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
  • 13
    • 0033057735 scopus 로고    scopus 로고
    • Polymorphisms at the topoisomerase II gene locus provide more evidence for the partition of Trypanosoma cruzi into two major groups
    • Dos Santos W., and Buck G. Polymorphisms at the topoisomerase II gene locus provide more evidence for the partition of Trypanosoma cruzi into two major groups. J. Euk. Microbiol. 46 (1999) 17-23
    • (1999) J. Euk. Microbiol. , vol.46 , pp. 17-23
    • Dos Santos, W.1    Buck, G.2
  • 14
    • 30344443401 scopus 로고    scopus 로고
    • The presence of four iron-containing superoxide dismutase isozymes in Trypanosomatidae: characterization, subcellular localization, and phylogenetic origin in Trypanosoma brucei
    • Dufernez F., Yernaux C., Gerbod D., Noël C., Chauvenet M., Wintjens R., Edgcomb V.P., Capron M., Opperdoes F.R., and Viscogliosi E. The presence of four iron-containing superoxide dismutase isozymes in Trypanosomatidae: characterization, subcellular localization, and phylogenetic origin in Trypanosoma brucei. Free Rad. Biol. Med. 40 (2006) 210-225
    • (2006) Free Rad. Biol. Med. , vol.40 , pp. 210-225
    • Dufernez, F.1    Yernaux, C.2    Gerbod, D.3    Noël, C.4    Chauvenet, M.5    Wintjens, R.6    Edgcomb, V.P.7    Capron, M.8    Opperdoes, F.R.9    Viscogliosi, E.10
  • 15
    • 0034008682 scopus 로고    scopus 로고
    • Upregulation of the secretory pathway in cisteine proteaese inhibitor-resistant Trypanosoma cruzi
    • Engel J., Garcia C., Hsieh I., Doyle P., and Mckerrow J. Upregulation of the secretory pathway in cisteine proteaese inhibitor-resistant Trypanosoma cruzi. J. Cell Sci. 113 (2000) 1345-1354
    • (2000) J. Cell Sci. , vol.113 , pp. 1345-1354
    • Engel, J.1    Garcia, C.2    Hsieh, I.3    Doyle, P.4    Mckerrow, J.5
  • 16
    • 0023609713 scopus 로고
    • Susceptibility and natural resistance of Trypanosoma cruzi strains to drugs used clinically in Chagas disease
    • Filardi L., and Brener Z. Susceptibility and natural resistance of Trypanosoma cruzi strains to drugs used clinically in Chagas disease. Trans. R. Soc. Trop. Med. Hyg. 81 (1987) 755-759
    • (1987) Trans. R. Soc. Trop. Med. Hyg. , vol.81 , pp. 755-759
    • Filardi, L.1    Brener, Z.2
  • 19
  • 20
    • 0035890678 scopus 로고    scopus 로고
    • Identification of a developmentally regulated iron superoxide dismutase of Trypanosoma brucei
    • Kabiri M., and Steverding D. Identification of a developmentally regulated iron superoxide dismutase of Trypanosoma brucei. Biochem. J. 360 (2001) 173-177
    • (2001) Biochem. J. , vol.360 , pp. 173-177
    • Kabiri, M.1    Steverding, D.2
  • 21
    • 0032053836 scopus 로고    scopus 로고
    • Representation of differential expression: a new approach to study differential gene expression in trypanosomatids
    • Krieger M.A., and Goldenberg S. Representation of differential expression: a new approach to study differential gene expression in trypanosomatids. Parasitol. Today 14 (1998) 163-166
    • (1998) Parasitol. Today , vol.14 , pp. 163-166
    • Krieger, M.A.1    Goldenberg, S.2
  • 22
    • 0021099089 scopus 로고
    • Iron-containing superoxide dismutase from Crithidia fasciculata. Purification, characterisation, and similarity to the leishmanial and trypanosomal enzymes
    • Le Trant N., Meshnick S.R., Kitchener K., Eaton J.W., and Cerami A. Iron-containing superoxide dismutase from Crithidia fasciculata. Purification, characterisation, and similarity to the leishmanial and trypanosomal enzymes. J. Biol. Chem. 258 (1983) 125-130
    • (1983) J. Biol. Chem. , vol.258 , pp. 125-130
    • Le Trant, N.1    Meshnick, S.R.2    Kitchener, K.3    Eaton, J.W.4    Cerami, A.5
  • 23
    • 0030911717 scopus 로고    scopus 로고
    • Effects of nifurtimox and benznidazole upon glutathione and trypanothione in epimastigote, trypomastigote and amastigote forms of Trypanosoma cruzi
    • Maya J.D., Repetto Y., Agosín M., Ojeda J.M., Tellez R., Gaule C., and Morillo A. Effects of nifurtimox and benznidazole upon glutathione and trypanothione 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    Agosín, M.3    Ojeda, J.M.4    Tellez, R.5    Gaule, C.6    Morillo, A.7
  • 25
    • 1842583981 scopus 로고    scopus 로고
    • Superoxide dismutases: active sites that save, but a protein that kills
    • Miller A.F. Superoxide dismutases: active sites that save, but a protein that kills. Curr. Opin. Chem. Biol. 8 (2004) 1-7
    • (2004) Curr. Opin. Chem. Biol. , vol.8 , pp. 1-7
    • Miller, A.F.1
  • 26
    • 0024315776 scopus 로고
    • Detection of Trypanosoma cruzi by DNA amplification using the polymerase chain reaction
    • Moser D.R., Kirchhoff L.V., and Donelson J.E. Detection of Trypanosoma cruzi by DNA amplification using the polymerase chain reaction. J. Clin. Microbiol. 27 (1989) 1477-1482
    • (1989) J. Clin. Microbiol. , vol.27 , pp. 1477-1482
    • Moser, D.R.1    Kirchhoff, L.V.2    Donelson, J.E.3
  • 27
    • 0023945781 scopus 로고
    • The biochemistry of the mode of action of drugs and the detoxication mechanisms in Trypanosoma cruzi
    • Morello A. The biochemistry of the mode of action of drugs and the detoxication mechanisms in Trypanosoma cruzi. Comp. Biochem. Physiol. C 90 (1988) 1-12
    • (1988) Comp. Biochem. Physiol. C , vol.90 , pp. 1-12
    • Morello, A.1
  • 28
    • 0020455681 scopus 로고
    • Different behaviours of benznidazole as free radical generator with mammalian and Trypanosoma cruzi microsomal preparations
    • Moreno S.N., Docampo R., Mason R.P., Leon W., and Stoppani A.O. Different behaviours of benznidazole as free radical generator with mammalian and Trypanosoma cruzi microsomal preparations. Arch. Biochem. Biophys. 218 (1982) 585-591
    • (1982) Arch. Biochem. Biophys. , vol.218 , pp. 585-591
    • Moreno, S.N.1    Docampo, R.2    Mason, R.P.3    Leon, W.4    Stoppani, A.O.5
  • 29
    • 0031984626 scopus 로고    scopus 로고
    • In vivo selection of a population of Trypanosoma cruzi and clones resistant to benznidazole
    • Murta S.M.F., and Romanha A.J. In vivo selection of a population of Trypanosoma cruzi and clones resistant to benznidazole. Parasitology 116 (1998) 165-171
    • (1998) Parasitology , vol.116 , pp. 165-171
    • Murta, S.M.F.1    Romanha, A.J.2
  • 30
    • 17344379918 scopus 로고    scopus 로고
    • Molecular characterization of susceptible and naturally resistant strains of Trypanosoma cruzi to benznidazole and nifurtimox
    • Murta S.M.F., Gazzinelli R., Brener Z., and Romanha A.J. Molecular characterization of susceptible and naturally resistant strains of Trypanosoma cruzi to benznidazole and nifurtimox. Mol. Biochem. Parasitol. 93 (1998) 203-214
    • (1998) Mol. Biochem. Parasitol. , vol.93 , pp. 203-214
    • Murta, S.M.F.1    Gazzinelli, R.2    Brener, Z.3    Romanha, A.J.4
  • 31
    • 0034788472 scopus 로고    scopus 로고
    • Drug resistance in Trypanosoma cruzi is not associated with amplification or overexpression of phosphoglycoprotein (PGP) genes
    • Murta S.M.F., Dos Santos W.G., Anacleto C., Nirdé P., Moreira E.S.A., and Romanha A.J. Drug resistance in Trypanosoma cruzi is not associated with amplification or overexpression of phosphoglycoprotein (PGP) genes. Mol. Biochem. Parasitol. 117 (2001) 223-228
    • (2001) Mol. Biochem. Parasitol. , vol.117 , pp. 223-228
    • Murta, S.M.F.1    Dos Santos, W.G.2    Anacleto, C.3    Nirdé, P.4    Moreira, E.S.A.5    Romanha, A.J.6
  • 34
    • 0023804393 scopus 로고
    • Comparative studies of drug susceptibility of five strains of Trypanosoma cruzi in vitro and in vivo
    • Neal R.A., and Van Bueren J. Comparative studies of drug susceptibility of five strains of Trypanosoma cruzi in vitro and in vivo. Trans. R. Soc. Trop. Med. Hyg. 82 (1988) 709-714
    • (1988) Trans. R. Soc. Trop. Med. Hyg. , vol.82 , pp. 709-714
    • Neal, R.A.1    Van Bueren, J.2
  • 35
    • 0029610833 scopus 로고
    • Drug-resistant epimastigotes of Trypanosoma cruzi and persistence of this phenotype after differentiation into amastigotes
    • Nirdé P., Larroque C., and Barnabé C. Drug-resistant epimastigotes of Trypanosoma cruzi and persistence of this phenotype after differentiation into amastigotes. CR Acad. Sci. Ser. III 318 (1995) 1239-1244
    • (1995) CR Acad. Sci. Ser. III , vol.318 , pp. 1239-1244
    • Nirdé, P.1    Larroque, C.2    Barnabé, C.3
  • 36
    • 0029680737 scopus 로고    scopus 로고
    • Cellular and molecular biological analyses of nifurtimox resistance in Trypanosoma cruzi
    • Nozaki T., Engel J., and Dvorak J. Cellular and molecular biological analyses of nifurtimox resistance in Trypanosoma cruzi. Am. J. Med. Hyg. 55 (1996) 111-117
    • (1996) Am. J. Med. Hyg. , vol.55 , pp. 111-117
    • Nozaki, T.1    Engel, J.2    Dvorak, J.3
  • 37
    • 0031455412 scopus 로고    scopus 로고
    • Cloning, characterization and overexpression of two iron superoxide dismutase cDNAs from Leishmania chagasi: role in pathogenesis
    • Paramchuk W.J., Ismail S.O., Bhatia A., and Gedamu L. Cloning, characterization and overexpression of two iron superoxide dismutase cDNAs from Leishmania chagasi: role in pathogenesis. Mol. Biochem. Parasitol. 90 (1997) 203-221
    • (1997) Mol. Biochem. Parasitol. , vol.90 , pp. 203-221
    • Paramchuk, W.J.1    Ismail, S.O.2    Bhatia, A.3    Gedamu, L.4
  • 39
    • 0035991711 scopus 로고    scopus 로고
    • Thiol metabolism of the trypanosomatids as potential drug targets
    • Steenkamp D.J. Thiol metabolism of the trypanosomatids as potential drug targets. IUBMB Life 53 (2002) 243-248
    • (2002) IUBMB Life , vol.53 , pp. 243-248
    • Steenkamp, D.J.1
  • 40
    • 0029917178 scopus 로고    scopus 로고
    • Cloning of an Fe-superoxide dismutase gene homologue from Trypanosoma cruzi
    • Temperton N.J., Wilkinson S.R., and Kelly J.M. Cloning of an Fe-superoxide dismutase gene homologue from Trypanosoma cruzi. Mol. Biochem. Parasitol. 76 (1996) 339-343
    • (1996) Mol. Biochem. Parasitol. , vol.76 , pp. 339-343
    • Temperton, N.J.1    Wilkinson, S.R.2    Kelly, J.M.3
  • 41
    • 0032582844 scopus 로고    scopus 로고
    • Overexpression of superoxide dismutase in Trypanosoma cruzi results in increased sensitivity to the trypanocidal agents gentian violet and benznidazole
    • Temperton N.J., Wilkinson S.R., Meyer D.J., and Kelly J.M. Overexpression of superoxide dismutase in Trypanosoma cruzi results in increased sensitivity to the trypanocidal agents gentian violet and benznidazole. Mol. Biochem. Parasitol. 96 (1998) 167-176
    • (1998) Mol. Biochem. Parasitol. , vol.96 , pp. 167-176
    • Temperton, N.J.1    Wilkinson, S.R.2    Meyer, D.J.3    Kelly, J.M.4
  • 42
    • 21444445416 scopus 로고    scopus 로고
    • Genetic diversity and drug resistance in Trypanosoma cruzi, the agent of Chagas disease
    • Toledo M., Tafuri W., Bahia M.T., Tibayrenc M., and Lana M. Genetic diversity and drug resistance in Trypanosoma cruzi, the agent of Chagas disease. Antimicrob. Agents Chemother. 4 (2004) 11-22
    • (2004) Antimicrob. Agents Chemother. , vol.4 , pp. 11-22
    • Toledo, M.1    Tafuri, W.2    Bahia, M.T.3    Tibayrenc, M.4    Lana, M.5
  • 43
    • 0030581690 scopus 로고    scopus 로고
    • Inhibition of Trypanosoma cruzi and T. brucei NADH fumarate reductase by benznidazole anthelmintic imidazole derivates
    • Turrens J.F., Watts Jr. B.P., Zhong L., and Docampo R. Inhibition of Trypanosoma cruzi and T. brucei NADH fumarate reductase by benznidazole anthelmintic imidazole derivates. Mol. Biochem. Parasitol. 82 (1996) 125-129
    • (1996) Mol. Biochem. Parasitol. , vol.82 , pp. 125-129
    • Turrens, J.F.1    Watts Jr., B.P.2    Zhong, L.3    Docampo, R.4
  • 44
    • 0028922077 scopus 로고
    • Multidrug resistance and P-glicoprotein in parasitic Protozoa
    • Ullman B. Multidrug resistance and P-glicoprotein in parasitic Protozoa. J. Bioenerg. Biomembr. 27 (1995) 77-84
    • (1995) J. Bioenerg. Biomembr. , vol.27 , pp. 77-84
    • Ullman, B.1
  • 45
    • 0142227145 scopus 로고    scopus 로고
    • Specific chemotherapy of Chagas disease: controversies and advances
    • Urbina J.A., and Docampo R. Specific chemotherapy of Chagas disease: controversies and advances. Trends Parasitol. 19 (2003) 495-501
    • (2003) Trends Parasitol. , vol.19 , pp. 495-501
    • Urbina, J.A.1    Docampo, R.2
  • 46
    • 0029014312 scopus 로고
    • Control of gene expression in Trypanosomes
    • Vanhame L., and Pays E. Control of gene expression in Trypanosomes. Microbiol. Rev. 59 (1995) 223-240
    • (1995) Microbiol. Rev. , vol.59 , pp. 223-240
    • Vanhame, L.1    Pays, E.2
  • 48
    • 0033543649 scopus 로고    scopus 로고
    • Metronidazole resistance in the protozoan parasite Entamoeba histolytica is associated with increased expression of iron-containing superoxide dismutase and peroxiredoxin and decreased expression of ferredoxin 1 and flavin reductase
    • Wassmann C., Hellberg A., Tannich E., and Bruchhaus I. Metronidazole resistance in the protozoan parasite Entamoeba histolytica is associated with increased expression of iron-containing superoxide dismutase and peroxiredoxin and decreased expression of ferredoxin 1 and flavin reductase. J. Biol. Chem. 37 (1999) 26051-26056
    • (1999) J. Biol. Chem. , vol.37 , pp. 26051-26056
    • Wassmann, C.1    Hellberg, A.2    Tannich, E.3    Bruchhaus, I.4
  • 50
    • 1542305367 scopus 로고    scopus 로고
    • Specificity and phenetic relationships of iron- and manganese-containing superoxide dismutase on the basis of structure and sequence comparisons
    • Wintjens R., Noël C., May A.C.W., Gerbod D., Dufernez F., Capron M., Viscogliosi E., and Rooman M. Specificity and phenetic relationships of iron- and manganese-containing superoxide dismutase on the basis of structure and sequence comparisons. J. Biol. Chem. 279 (2004) 9248-9254
    • (2004) J. Biol. Chem. , vol.279 , pp. 9248-9254
    • Wintjens, R.1    Noël, C.2    May, A.C.W.3    Gerbod, D.4    Dufernez, F.5    Capron, M.6    Viscogliosi, E.7    Rooman, M.8
  • 51
    • 33751417082 scopus 로고    scopus 로고
    • World Health Organization. 2002. Online: http://www.who.int/ctd/chagas/burdens.htm and http://www.who.int/tdr/diseases/chagas/direction.htm. Accessed November 25, 2005.


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