Biotransformation enzyme activities and phase I metabolites analysis in Litopenaeus vannamei following intramuscular administration of T-2 toxin

References

• Anderson, D.W., et al., 1989. Structure-activity studies of trichothecenes: cytotoxicity of analogues and reaction products derived from T-2 toxin and neosolaniol. Journal of Medicinal Chemistry, 32, 555–562.
   PubMed Web of Science ®Google Scholar
• Bernhardt, K., et al., 2016. Determination of T-2 toxin, HT-2 toxin, and three other type A trichothecenes in layer feed by high-performance liquid chromatography-tandem mass spectrometry (LC-MS/MS)-comparison of two sample preparation methods. Mycotoxin Research, 32, 89–97.
   PubMed Web of Science ®Google Scholar
• Bock, B.W., 1977. Dual role of glucuronyl- and sulfotransferases converting xenobiotics into reactive or biologically inactive and easily excretable compounds. Archives of Toxicology, 12, 77–85.
   Web of Science ®Google Scholar
• Cacciatore, L.C., Guerrero, N.V., and Cochon, A.C., 2013. Cholincarboxylesterase and carboxylesterase inhibition in Planorbarius corneus exposed to binary mixtures of azinphos-methyl and chlorpyrifos. Aquatic Toxicology, 128, 124–134.
   PubMed Web of Science ®Google Scholar
• Chatterjee, K., Viscontl, A., and Microcha, C.J., 1986. Deepoxy T-2 tetraol: a metabolite of T-2 toxin found in cow urine. Journal of Agricultural and Food Chemistry, 34, 695–697.
   Web of Science ®Google Scholar
• Chaudhari, M., et al., 2009. Oxidative damage and gene expression profile of antioxidant enzymes after T-2 toxin exposure in mice. Journal of Biochemical and Molecular Toxicology, 23, 212–221.
   PubMed Web of Science ®Google Scholar
• Chaudhary, M. and Rao, P.V., 2010. Brain oxidative stress after dermal and subcutaneous exposure of T-2 toxin in mice. Food and Chemical Toxicology, 48, 34–36.
   Web of Science ®Google Scholar
• Collier, A.C., et al., 2000. A highly sensitive fluorescent microplate method for the determination of UDP-glucuronosyl transferase activity in tissues and placental cell lines. Drug Metabolism & Disposition, 28, 1184–1186.
   PubMed Web of Science ®Google Scholar
• Da Silva, R.A.J., et al., 2012. EROD activity and genotoxicity in the seabob shrimp Xiphopenaeus kroyeri exposed to benzo[a]pyrene (BaP) concentrations. Environmental Toxicology and Pharmacology, 34, 995–1003.
   PubMed Web of Science ®Google Scholar
• Datta, D., Nair, V.R., and Nair, C.R., 1972. Estimation of hepatic bilirubin UDP-glucuronyl transferase in patients with noncirrhotic portal fibrosis and liver disease: significance and limitations. Journal of Digestive Diseases, 10, 961–968.
   Google Scholar
• Desjardins, A.E., Hohn, T.M., and McCormick, S.P., 1993. Trichothecene biosynthesis in Fusarium species: chemistry, genetics, and significance. Microbiological Review, 57, 595–604.
   PubMedGoogle Scholar
• Dixon, D.P., Cole, D.J., and Edwards, R., 2000. Characterisation of a zeta class glutathione transferase from Arabidopsis thaliana with a putative role in tyrosine catabolism. Archives of Biochemisry and Biophysics, 384, 407–412.
   PubMed Web of Science ®Google Scholar
• Dong, K., et al., 2008. The effects of subcutaneous administration of T-2 toxin on liver drug metabolizing enzymes in piglets. Toxicological and Environmental Chemistry, 90, 401–413.
   Google Scholar
• Drobne, D., et al., 2008. Toxicity of imidacloprid to the terrestrial isopod Porcellio scaber (Isopoda, Crustacea). Chemosphere, 71, 1326–1334.
   PubMed Web of Science ®Google Scholar
• Fang, H.Q., et al., 2012. T-2 toxin induces apoptosis in differentiated murine embryonic stem cells through reactive oxygen species-mediated mitochondrial pathway. Apoptosis, 17, 895–907.
   PubMed Web of Science ®Google Scholar
• Fink-Gremmels, J., 1999. Mycotoxins: their implications for human and animal health. Veterinary Quarterly, 21, 115–120.
   PubMed Web of Science ®Google Scholar
• Fonnum, F., et al., 1985. Carboxylesterases, importance for detoxification of organophosphorus anticholinesterases and trichothecenes. Fundamental and Applied Toxicology, 5 (6), 29–38.
   Google Scholar
• Frame, L.T., et al., 2000. A simple colorimetric assay for phenotyping the major human thermostable phenol sulfotransferase (SULT1A1) using platelet cytosols. Drug Metabolism & Disposition, 28, 1063–1068.
   PubMed Web of Science ®Google Scholar
• Gallucci, E., et al., 1989. The effect of T-2 toxin on active sodium transport across frog skin in the presence of ADH and amphotericin B. Comparative Biochemistry and Physiology A, 93, 33–36.
   PubMed Web of Science ®Google Scholar
• Galtier, P., et al., 1989. Comparative effects of T-2 toxin and diacetoxyscirpenol on drug metabolizing enzymes in rat tissues. Food and Chemical Toxicology, 27, 215–220.
   PubMed Web of Science ®Google Scholar
• Guerre, P., et al., 2000. The effects of T-2 toxin exposure on liver drug metabolizing enzymes in rabbit. Food Additives & Contaminants A, 17, 1019–1026.
   PubMed Web of Science ®Google Scholar
• Habig, W.H., Pabst, M.J., and Jakoby, W.B., 1974. Glutathione S-transferases. The first enzymatic step in mercapturic acid formation. Journal of Biological Chemistry, 249, 7130–7139.
   PubMed Web of Science ®Google Scholar
• He, C.H., et al., 2010. The individual and combined effects of deoxynivalenol and aflatoxin B1 on primary hepatocytes of Prinus carpio. International Journal of Molecular Science, 11, 3760–3768.
   PubMed Web of Science ®Google Scholar
• Hurk, P.V.D., et al., 2007. Activity patterns of biotransformation enzymes in juvenile chickens after in ovo dosage of PCB126. Comparative Biochemistry and Physiology C, 146, 301–307.
   Web of Science ®Google Scholar
• Islam, Z., et al., 1998. Structure-function relationship of T-2 toxin and its metabolites in inducing thymic apoptosis in vivo in mice. Bioscience Biotechnology and Biochemistry, 62, 1492–1497.
   PubMed Web of Science ®Google Scholar
• Izzo, A.A. and Ernst, E., 2009. Interactions between herbal medicines and prescribed drugs: an updated systematic review. Drugs, 69, 1777–1798.
   PubMed Web of Science ®Google Scholar
• James, M.O., 2011. Steroid catabolism in marine and freshwater fish. Journal of Steroid Biochemisty, 127, 167–175.
   Google Scholar
• James, M.O. and Boyle, S.M., 1998. Cytochromes P450 in crustacea. Comparative Biochemistry and Physiology Part C, 121, 157–172.
   PubMed Web of Science ®Google Scholar
• Johnsen, H., et al., 1988. Metabolism of T-2 toxin by blood cell carboxylesterases. Biochemical Pharmacology, 37, 3193–3197.
   PubMed Web of Science ®Google Scholar
• Johnsen, H., et al., 1986. Metabolism of T-2 toxin by rat liver carboxylesterase. Biochemical Pharmacology, 35, 1469–1473.
   PubMed Web of Science ®Google Scholar
• Khoa, L., Hatai, V.K., and Aoki, T., 2004. Fusarium incarnatum isolated from black tiger shrimp, Penaeus monodon Fabricius, with black gill disease cultured in Vietnam. Journal of Fish Diseases, 27, 507–515.
   PubMed Web of Science ®Google Scholar
• Kravchenko, L.V., et al., 2001. Effect of nutritional indoles on activity of xenobiotic metabolism enzymes and T-2 toxicity in rats. Bulletin of Experimental Biology and Medicine, 31, 544–547.
   Web of Science ®Google Scholar
• Ku, P.J., et al., 2014. Effects of triclosan on the detoxification system in the yellow catfish (Pelteobagrus fulvidraco): Expressions of CYP and GST genes and corresponding enzyme activity in phase I, II and antioxidant system. Toxicology and Applied Pharmacology, 166, 105–111.
   Google Scholar
• Leal, M., et al., 1999. Effect of lycopene on lipid peroxidation and glutathione-dependent enzymes induced by T-2 toxin in vivo. Toxicology Letters, 1, 1–10.
   Web of Science ®Google Scholar
• Ljungquist, A. and Augustinsson, K.B., 1971. Purification and properties of two carboxylesterases from rat-liver microsomes. Europeaan Journal of Biochemistry, 23, 303–313.
   PubMedGoogle Scholar
• Lowry, O.H., et al., 1951. Protein measurement with the Folin Phenol reagent. Journal of Biological Chemistry, 193, 265–275.
   PubMed Web of Science ®Google Scholar
• Lu, P.L., et al., 2016. A sensitive and validated method for determination of T-2 and HT-2 toxin residues in shrimp tissues by LC-MS/MS. Food Analytical Methods, 9, 1580–1596.
   Web of Science ®Google Scholar
• Mayer, R.T., et al., 1990. 7-Alkoxyquinolines: new fluorescent substrates for cytochrome P450 monooxygenases. Biochemical Pharmacology, 40, 1645–1655.
   PubMed Web of Science ®Google Scholar
• Meissonnier, G.M., et al., 2008. Subclinical doses of T-2 toxin impair acquired immune response and liver cytochrome P450 in pigs. Toxicology, 1, 46–54.
   Web of Science ®Google Scholar
• Mulder, G.J., Dawson, J.R., and Pang, K.S., 1984. Competition between sulphation and glucuronidation in the rat in vivo: enzyme kinetics and pharmacokinetics of conjugation. Biochemical Society Transactions, 12, 17–20.
   PubMed Web of Science ®Google Scholar
• Oost, R.V.D., Beyer, J., and Vermeulen, N.P.E., 2003. Fish bioaccumulation and biomarkers in environmental risk assessment: a review. Environmental Toxicology and Pharmacology, 13, 57–149.
   PubMed Web of Science ®Google Scholar
• Parrilla-Tayor, D.P., Zenteno-Savin, T., and Magallón-Barajas, F.J., 2013. Antioxidant enzyme activity in pacific whiteleg shrimp (Litopenaeus vannamei) in response to infection with white spot syndrome virus. Aquaculture, 380, 41–46.
   Web of Science ®Google Scholar
• Prough, R.A., Burke, M.D., and Mayer, R.T., 1978. Direct fluorometric methods for measuring mixed function oxidase activity. Methods in Enzymology, 52, 372–377.
   PubMedGoogle Scholar
• Ren, X.Y., Pan, L.Q., and Wang, L., 2014. Metabolic enzyme activities, metabolism-related genes expression and bioaccumulation in juvenile white shrimp Litopenaeus vannamei exposed to benzo[a]pyrene. Ecotoxicology and Environmental Safety, 104, 79–86.
   PubMed Web of Science ®Google Scholar
• Ren, X.Y., Pan, L.Q., and Wang, L., 2015. The detoxification process, bioaccumulation and damage effect in juvenile white shrimp Litopenaeus vannamei exposed to chrysene. Ecotoxicology and Environmental Safety, 114, 44–51.
   PubMed Web of Science ®Google Scholar
• Rey-Salgueiro, L., et al., 2011. Evaluation of 3-hydroxy-benzo[a]pyrene levels in Nile tilapia (Oreochromis niloticus) after waterborne exposure to benzo[a]pyrene. Environmental Toxicology and Chemistry, 93, 9–10.
   Google Scholar
• Sun, L.Y., et al., 2012. T-2 toxin contamination in grains and selenium concentration in drinking water and grains in Kaschin-Beck disease endemic areas of Qinghai Province. Biological Trace Element Research, 150, 371–375.
   PubMed Web of Science ®Google Scholar
• Sun, Y.X., et al., 2014. Liquid chromatography–tandem mass spectrometry method for toxicokinetics, tissue distribution, and excretion studies of T-2 toxin and its major metabolites in pigs. Journal of Chromatography B, 958, 75–82.
   PubMed Web of Science ®Google Scholar
• Wang, H.J., et al., 2014. Advance on researches of production, toxicity and detoxification of T-2 toxin. Journal of Food Quality and Safety, 1674, 2392–2398. [in Chinese with English abstract]
   Google Scholar
• Wang, X.C., et al., 2012. Contamination level of T-2 and HT-2 toxin in cereal crops from Aba Area in Sichuan Province, China. Bulletin of Environmental Contamination and Toxicology, 88, 396–400.
   PubMed Web of Science ®Google Scholar
• Welsch, T. and Humpf, H.U., 2012. HT-2 Toxin 4-Glucuronide as new T-2 toxin metabolite: Enzymatic synthesis, analysis, and species specific formation of T-2 and HT-2 toxin glucuronides by rat, mouse, pig, and human liver microsomes. Journal of Agricultural and Food Chemistry, 40, 10170–10178.
   Web of Science ®Google Scholar
• Wepener, V., et al., 2005. Active biomonitoring in freshwater environments: early warning signals from biomarkers in assessing biological effects of diffuse sources of pollutants. Physics and Chemistry of the Earth A, 30, 751–761.
   Web of Science ®Google Scholar
• Wu, Q.H., et al., 2012. Intestinal metabolism of T-2 toxin in the pig cecum model. Mycotoxin Research, 28, 191–198.
   PubMedGoogle Scholar
• Wu, Q.H., et al., 2011. A comparison of hepatic in vitro metabolism of T-2 toxin in rats, pigs, chickens, and carp. Xenobiotica, 41, 863–873.
   PubMed Web of Science ®Google Scholar
• Xie, G., et al., 2013. Comparative in vitro metabolism of phospho-tyrosol-indomethacin by mice, rats and humans. Biochemical Pharmacology, 85, 1195–1202.
   PubMed Web of Science ®Google Scholar
• Yoshizawa, T., et al., 1982. 3′-hydroxy T-2 and 3′-OH-HT-2 561 toxins: new metabolites of T-2 toxin, a trichothecene mycotoxin, in animals. Agricultural and Biological Chemistry, 46, 2613–2615.
   Web of Science ®Google Scholar
• Yuan, Y.Y., et al., 2013. T-2 toxin is hydroxylated by chicken CYP3A37. Food and Chemical Toxicology, 62, 622–627.
   PubMed Web of Science ®Google Scholar