메뉴 건너뛰기




Volumn 196, Issue 3-4, 2013, Pages 373-381

Biotransformation of albendazole and activities of selected detoxification enzymes in Haemonchus contortus strains susceptible and resistant to anthelmintics

Author keywords

Drug resistance; Nematodes; Strain differences; UDP glucosyltransferase

Indexed keywords

ALBENDAZOLE; ALBENDAZOLE GLUCOSIDE; ALBENDAZOLE SULFONE; ALBENDAZOLE SULFOXIDE; BENZIMIDAZOLE DERIVATIVE; CATALASE; DRUG METABOLITE; GLUCOSYLTRANSFERASE; PEROXIDASE; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE GLUCOSYLTRANSFERASE;

EID: 84881556939     PISSN: 03044017     EISSN: 18732550     Source Type: Journal    
DOI: 10.1016/j.vetpar.2013.03.018     Document Type: Article
Times cited : (34)

References (34)
  • 1
    • 23944452203 scopus 로고    scopus 로고
    • Altered drug influx/efflux and enhanced metabolic activity in triclabendazole-resistant liver flukes
    • Alvarez L.I., Solana H.D., Mottier M.L., Virkel G.L., Fairweather I., Lanusse C.E. Altered drug influx/efflux and enhanced metabolic activity in triclabendazole-resistant liver flukes. Parasitology 2005, 131:501-510.
    • (2005) Parasitology , vol.131 , pp. 501-510
    • Alvarez, L.I.1    Solana, H.D.2    Mottier, M.L.3    Virkel, G.L.4    Fairweather, I.5    Lanusse, C.E.6
  • 4
    • 77955621566 scopus 로고    scopus 로고
    • In vitro oxidative metabolism of xenobiotics in the lancet fluke (Dicrocoelium dendriticum) and the effects of albendazole and albendazole sulphoxide ex vivo
    • Bártíková H., Vokřál I., Skálová L., Lamka J., Szotáková B. In vitro oxidative metabolism of xenobiotics in the lancet fluke (Dicrocoelium dendriticum) and the effects of albendazole and albendazole sulphoxide ex vivo. Xenobiotica 2010, 40:593-660.
    • (2010) Xenobiotica , vol.40 , pp. 593-660
    • Bártíková, H.1    Vokřál, I.2    Skálová, L.3    Lamka, J.4    Szotáková, B.5
  • 7
    • 0028106482 scopus 로고
    • Cytochrome P450 specificities of alkoxyresorufin O-dealkylation in human and rat liver
    • Burke M.D., Thompson S., Weaver R.J., Wolf C.R., Mayer R.T. Cytochrome P450 specificities of alkoxyresorufin O-dealkylation in human and rat liver. Biochem. Pharmacol. 1994, 48:923-936.
    • (1994) Biochem. Pharmacol. , vol.48 , pp. 923-936
    • Burke, M.D.1    Thompson, S.2    Weaver, R.J.3    Wolf, C.R.4    Mayer, R.T.5
  • 8
    • 0019424957 scopus 로고
    • Microsomal oxidation of thiobenzamide. A photometric assay for the flavin-containing monooxygenase
    • Cashman J.R., Hanzlik R.P. Microsomal oxidation of thiobenzamide. A photometric assay for the flavin-containing monooxygenase. Biochem. Biophys. Res. Commun. 1981, 98:147-153.
    • (1981) Biochem. Biophys. Res. Commun. , vol.98 , pp. 147-153
    • Cashman, J.R.1    Hanzlik, R.P.2
  • 10
    • 42449111601 scopus 로고    scopus 로고
    • LC-MS-MS identification of albendazole and flubendazole metabolites formed ex vivo by Haemonchus contortus
    • Cvilink V., Skálová L., Szotáková B., Lamka J., Kostiainen R., Ketola R.A. LC-MS-MS identification of albendazole and flubendazole metabolites formed ex vivo by Haemonchus contortus. Anal. Bioanal. Chem. 2008, 391:337-343.
    • (2008) Anal. Bioanal. Chem. , vol.391 , pp. 337-343
    • Cvilink, V.1    Skálová, L.2    Szotáková, B.3    Lamka, J.4    Kostiainen, R.5    Ketola, R.A.6
  • 11
    • 67649564531 scopus 로고    scopus 로고
    • Xenobiotic metabolizing enzymes and metabolism of anthelminthics in helminths
    • Cvilink V., Lamka J., Skálová L. Xenobiotic metabolizing enzymes and metabolism of anthelminthics in helminths. Drug Metab. Rev. 2009, 41:8-26.
    • (2009) Drug Metab. Rev. , vol.41 , pp. 8-26
    • Cvilink, V.1    Lamka, J.2    Skálová, L.3
  • 12
    • 57749100364 scopus 로고    scopus 로고
    • Phase I biotransformation of albendazole in lancet fluke (Dicrocoelium dendriticum)
    • Cvilink V., Szotakova B., Krizova V., Lamka J., Skalova L. Phase I biotransformation of albendazole in lancet fluke (Dicrocoelium dendriticum). Res. Vet. Sci. 2009, 86:49-55.
    • (2009) Res. Vet. Sci. , vol.86 , pp. 49-55
    • Cvilink, V.1    Szotakova, B.2    Krizova, V.3    Lamka, J.4    Skalova, L.5
  • 13
    • 77953321062 scopus 로고    scopus 로고
    • Potentiation of triclabendazole sulphoxide-induced tegumental disruption by methimazole in a triclabendazole-resistant isolate of Fasciola hepatica
    • Devine C., Brennan G.P., Lanusse C.E., Alvarez L.I., Trudgett A., Hoey E., Fairweather I. Potentiation of triclabendazole sulphoxide-induced tegumental disruption by methimazole in a triclabendazole-resistant isolate of Fasciola hepatica. Parasitol. Res. 2010, 106:1351-1363.
    • (2010) Parasitol. Res. , vol.106 , pp. 1351-1363
    • Devine, C.1    Brennan, G.P.2    Lanusse, C.E.3    Alvarez, L.I.4    Trudgett, A.5    Hoey, E.6    Fairweather, I.7
  • 14
    • 77955472548 scopus 로고    scopus 로고
    • Enhancement of the drug susceptibility of a triclabendazole-resistant isolate of Fasciola hepatica using the metabolic inhibitor ketoconazole
    • Devine C., Brennan G.P., Lanusse C.E., Alvarez L.I., Trudgett A., Hoey E., Fairweather I. Enhancement of the drug susceptibility of a triclabendazole-resistant isolate of Fasciola hepatica using the metabolic inhibitor ketoconazole. Parasitol. Res. 2010, 107:337-353.
    • (2010) Parasitol. Res. , vol.107 , pp. 337-353
    • Devine, C.1    Brennan, G.P.2    Lanusse, C.E.3    Alvarez, L.I.4    Trudgett, A.5    Hoey, E.6    Fairweather, I.7
  • 15
    • 0019738962 scopus 로고
    • Glutathione S-transferases (rat and human)
    • Habig W.H., Jakoby W.B. Glutathione S-transferases (rat and human). Methods Enzymol. 1981, 77:218-231.
    • (1981) Methods Enzymol. , vol.77 , pp. 218-231
    • Habig, W.H.1    Jakoby, W.B.2
  • 16
    • 0037389552 scopus 로고    scopus 로고
    • Catalase induction protects Haemonchus contortus against hydrogen peroxide in vitro
    • Kotze A.C. Catalase induction protects Haemonchus contortus against hydrogen peroxide in vitro. Int. J. Parasitol. 2003, 33:393-400.
    • (2003) Int. J. Parasitol. , vol.33 , pp. 393-400
    • Kotze, A.C.1
  • 17
    • 0035216159 scopus 로고    scopus 로고
    • Haemonchus contortus utilizes catalase in defense against exogenous hydrogen peroxide in vitro
    • Kotze A.C., McClure S.J. Haemonchus contortus utilizes catalase in defense against exogenous hydrogen peroxide in vitro. Int. J. Parasitol. 2001, 31:1563-1571.
    • (2001) Int. J. Parasitol. , vol.31 , pp. 1563-1571
    • Kotze, A.C.1    McClure, S.J.2
  • 18
    • 78649847015 scopus 로고    scopus 로고
    • Characterization of the xenobiotic response of Caenorhabditis elegans to anthelmintic drug albendazole a the identification of novel drug glucoside metabolites
    • Laing S.T., Ivens A., Laing R., Ravikumar S., Butler V., Woods D.J., Gilleard J.S. Characterization of the xenobiotic response of Caenorhabditis elegans to anthelmintic drug albendazole a the identification of novel drug glucoside metabolites. Biochem. J. 2010, 432:505-514.
    • (2010) Biochem. J. , vol.432 , pp. 505-514
    • Laing, S.T.1    Ivens, A.2    Laing, R.3    Ravikumar, S.4    Butler, V.5    Woods, D.J.6    Gilleard, J.S.7
  • 19
    • 0020433107 scopus 로고
    • Correlation of drug conjugative metabolism rates between in vivo and in vitro: glucuronidation and sulfation of p-nitrophenol as a model compound in rat
    • Mizuma T., Machida M., Hayashi M., Awazu S. Correlation of drug conjugative metabolism rates between in vivo and in vitro: glucuronidation and sulfation of p-nitrophenol as a model compound in rat. J. Pharmacobiodyn. 1982, 5:811-817.
    • (1982) J. Pharmacobiodyn. , vol.5 , pp. 811-817
    • Mizuma, T.1    Machida, M.2    Hayashi, M.3    Awazu, S.4
  • 20
    • 0028812229 scopus 로고
    • Chiral sulfoxidation of albendazole by the flavin adenine dinucleotide-containing and cytochrome P450-dependent monooxygenases from rat liver microsomes
    • Moroni P., Buronfosse T., Longin-Sauvageon C., Delatour P., Benoit E. Chiral sulfoxidation of albendazole by the flavin adenine dinucleotide-containing and cytochrome P450-dependent monooxygenases from rat liver microsomes. Drug Metab. Dispos. 1995, 23:160-165.
    • (1995) Drug Metab. Dispos. , vol.23 , pp. 160-165
    • Moroni, P.1    Buronfosse, T.2    Longin-Sauvageon, C.3    Delatour, P.4    Benoit, E.5
  • 21
    • 11244299723 scopus 로고    scopus 로고
    • Triclabendazole biotransformation and comparative diffusion of the parent drug and its oxidized metabolites into Fasciola hepatica
    • Mottier L., Virkel G., Solana H., Alvarez L., Salles J., Lanusse C. Triclabendazole biotransformation and comparative diffusion of the parent drug and its oxidized metabolites into Fasciola hepatica. Xenobiotica 2004, 34:1043-1057.
    • (2004) Xenobiotica , vol.34 , pp. 1043-1057
    • Mottier, L.1    Virkel, G.2    Solana, H.3    Alvarez, L.4    Salles, J.5    Lanusse, C.6
  • 23
    • 1242292998 scopus 로고    scopus 로고
    • The comparative metabolism of triclabendazole sulphoxide by triclabendazole-susceptible and triclabendazole-resistant Fasciola hepatica
    • Robinson M.W., Lawson J., Trudgett A., Hoey E.M., Fairweather I. The comparative metabolism of triclabendazole sulphoxide by triclabendazole-susceptible and triclabendazole-resistant Fasciola hepatica. Parasitol. Res. 2004, 92:205-210.
    • (2004) Parasitol. Res. , vol.92 , pp. 205-210
    • Robinson, M.W.1    Lawson, J.2    Trudgett, A.3    Hoey, E.M.4    Fairweather, I.5
  • 24
    • 0346727213 scopus 로고    scopus 로고
    • Genetic analysis of inbreeding of two strains of the parasitic nematode Haemonchus contortus
    • Roos M.H., Otsen M., Hoekstra R., Veenstra J.G., Lenstra J.A. Genetic analysis of inbreeding of two strains of the parasitic nematode Haemonchus contortus. Int. J. Parasitol. 2004, 34:109-115.
    • (2004) Int. J. Parasitol. , vol.34 , pp. 109-115
    • Roos, M.H.1    Otsen, M.2    Hoekstra, R.3    Veenstra, J.G.4    Lenstra, J.A.5
  • 25
    • 0030901902 scopus 로고    scopus 로고
    • Haemonchus contortus: the uptake and metabolism of closantel
    • Rothwell J., Sangster N. Haemonchus contortus: the uptake and metabolism of closantel. Int. J. Parasitol. 1997, 27:313-319.
    • (1997) Int. J. Parasitol. , vol.27 , pp. 313-319
    • Rothwell, J.1    Sangster, N.2
  • 26
    • 0035090015 scopus 로고    scopus 로고
    • Comparative metabolism of albendazole and albendazole sulphoxide by different helminth parasites
    • Solana H.D., Rodriguez J.A., Lanusse C.E. Comparative metabolism of albendazole and albendazole sulphoxide by different helminth parasites. Parasitol. Res. 2001, 87:275-280.
    • (2001) Parasitol. Res. , vol.87 , pp. 275-280
    • Solana, H.D.1    Rodriguez, J.A.2    Lanusse, C.E.3
  • 27
    • 81055155878 scopus 로고    scopus 로고
    • Expression differential of microsomal and cytosolic glutathione S-transferases in Fasciola hepatica resistant at triclabendazole
    • Scarella S., Lamenza P., Virkel G., Solana H. Expression differential of microsomal and cytosolic glutathione S-transferases in Fasciola hepatica resistant at triclabendazole. Mol. Biochem. Parasitol. 2012, 181:37-39.
    • (2012) Mol. Biochem. Parasitol. , vol.181 , pp. 37-39
    • Scarella, S.1    Lamenza, P.2    Virkel, G.3    Solana, H.4
  • 29
    • 38349159585 scopus 로고    scopus 로고
    • Glutathione transferases from parasites: a biochemical view
    • Torres-Rivera A., Landa A. Glutathione transferases from parasites: a biochemical view. Acta Trop. 2008, 105:99-112.
    • (2008) Acta Trop. , vol.105 , pp. 99-112
    • Torres-Rivera, A.1    Landa, A.2
  • 30
    • 0023802099 scopus 로고
    • Resistance of field strains of Haemonchus contortus to ivermectin, closantel, rafoxanide and the benzimidazoles in South Africa
    • Van Wyk J.A., Malan F.S. Resistance of field strains of Haemonchus contortus to ivermectin, closantel, rafoxanide and the benzimidazoles in South Africa. Vet. Rec. 1988, 123:226-228.
    • (1988) Vet. Rec. , vol.123 , pp. 226-228
    • Van Wyk, J.A.1    Malan, F.S.2
  • 31
    • 0019064954 scopus 로고
    • A technique for recovery of nematodes from ruminants by migration from gastro-intestinal ingesta gelled in agar: large-scale application
    • Van Wyk J.A., Gerber H.M., Groeneveld H.T. A technique for recovery of nematodes from ruminants by migration from gastro-intestinal ingesta gelled in agar: large-scale application. Onderstepoort J. Vet. Res. 1980, 47:147-158.
    • (1980) Onderstepoort J. Vet. Res. , vol.47 , pp. 147-158
    • Van Wyk, J.A.1    Gerber, H.M.2    Groeneveld, H.T.3
  • 32
    • 84866135502 scopus 로고    scopus 로고
    • The metabolism of flubendazole and the activities of selected biotransformation enzymes in Haemonchus contortus strains susceptible and resistant to anthelmintics
    • Vokřál I., Bártíková H., Prchal L., Stuchlíková L., Skálová L., Szotáková B., Lamk J., Várady M., Kubíček V. The metabolism of flubendazole and the activities of selected biotransformation enzymes in Haemonchus contortus strains susceptible and resistant to anthelmintics. Parasitology 2012, 139:1309-1316.
    • (2012) Parasitology , vol.139 , pp. 1309-1316
    • Vokřál, I.1    Bártíková, H.2    Prchal, L.3    Stuchlíková, L.4    Skálová, L.5    Szotáková, B.6    Lamk, J.7    Várady, M.8    Kubíček, V.9
  • 33
    • 0028226507 scopus 로고
    • A comparative study of constitutive and induced alkoxyresorufin O-dealkylation and individual cytochrome-P450 forms in cynomolgus monkey (Macaca fascicularis), human, mouse, rat and hamster liver-microsomes
    • Weaver R.J., Thompson S., Smith G., Dickins M., Elcombe C.R., Mayer R.T., Burke M.D. A comparative study of constitutive and induced alkoxyresorufin O-dealkylation and individual cytochrome-P450 forms in cynomolgus monkey (Macaca fascicularis), human, mouse, rat and hamster liver-microsomes. Biochem. Pharmacol. 1994, 47:763-773.
    • (1994) Biochem. Pharmacol. , vol.47 , pp. 763-773
    • Weaver, R.J.1    Thompson, S.2    Smith, G.3    Dickins, M.4    Elcombe, C.R.5    Mayer, R.T.6    Burke, M.D.7
  • 34
    • 0042195923 scopus 로고    scopus 로고
    • Determination of the activity of catalase using a europium(III)-tetracycline-derived fluorescent substrate
    • Wu M., Lin Z.H., Wolfbeis O.S. Determination of the activity of catalase using a europium(III)-tetracycline-derived fluorescent substrate. Anal. Biochem. 2003, 320:129-135.
    • (2003) Anal. Biochem. , vol.320 , pp. 129-135
    • Wu, M.1    Lin, Z.H.2    Wolfbeis, O.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.