Kinetics of hepatic phase I and II biotransformation reactions in eight finfish species

Marine Environmental Research

Volumn 67, Issue 4-5, 2009, Pages 183-188

  González, Jaime Fernando ^a   Reimschuessel, Renate ^b   Shaikh, Badar ^b   Kane, Andrew S ^c  

^a UNIVERSIDAD NACIONAL DE COLOMBIA   (Colombia)

^b CENTER FOR DRUG EVALUATION AND RESEARCH   (United States)

^c UNIVERSITY OF FLORIDA   (United States)

Author keywords

Finfish; Hepatic; Kinetics; Phase I and II biotransformation reactions

Indexed keywords

ATLANTIC SALMONS; CATALYTIC EFFICIENCIES; CHANNEL CATFISHES; CYTOSOLS; FINFISH; GLUTATHIONE S TRANSFERASE; HEPATIC; LARGEMOUTH BASS; MICROPTERUS; ONCORHYNCHUS MYKISS; PHASE I AND II BIOTRANSFORMATION REACTIONS; PHASE II; RAINBOW TROUTS; SALMO SALAR;

SYSTEM THEORY;

7 ETHOXYCOUMARIN DEETHYLASE; BENZYLOXYRESORUFIN O DEALKYLASE; ETHOXYRESORUFIN DEETHYLASE; GLUCURONOSYLTRANSFERASE; GLUTATHIONE TRANSFERASE; PENTOXYRESORUFIN DEALKYLASE; SULFOTRANSFERASE; UNCLASSIFIED DRUG; UNCLASSIFIED ENZYME;

BIOTRANSFORMATION; CATALYSIS; ENZYME ACTIVITY; FINFISH; KINETICS; PERCIFORM; SALMONID;

ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; ATLANTIC SALMON; BIOTRANSFORMATION; CHANNEL CATFISH; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME MECHANISM; LARGEMOUTH BASS; LIVER CYTOSOL; LIVER MICROSOME METABOLISM; NONHUMAN; RAINBOW TROUT; SPECIES COMPARISON; STRIPED BASS; TILAPIA; UNITED STATES;

ANIMALS; BIOTRANSFORMATION; CYTOSOL; ENZYMES; FISHES; LIVER; MICROSOMES, LIVER; SPECIES SPECIFICITY;

ICTALURUS PUNCTATUS; LEPOMIS; LEPOMIS MACROCHIRUS; MICROPTERUS; MICROPTERUS SALMOIDES; MORONE; MORONE SAXATILIS; ONCORHYNCHUS MYKISS; OREOCHROMIS; SALMO SALAR; TILAPIA;

EID: 67349173569     PISSN: 01411136     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.marenvres.2009.01.002     Document Type: Article

References (52)

1. Ankley G.T., and Agosin M. Comparative aspects of hepatic UDP-glucuronosyltransferases and glutathione-s-transferases in bluegill and channel catfish. Comparative Biochemistry and Physiology B 87 (1987) 671-673
2. Arukwe A., Nordtug T., Kortner T.M., Mortensen A.S., and Brakstad O.G. Modulation of steroidogenesis and xenobiotic biotransformation responses in zebrafish (Dario rerio) exposed to water-soluble fraction of crude oil. Environmental Research 107 (2008) 362-370
3. Beckmann J.D. Continuous fluorometric assay of phenol sulfotransferase. Analytical Biochemistry 197 (1991) 408-411
4. Clarke D.J., George S.G., and Burchell B. Glucuronidation in fish. Aquatic Toxicology 20 (1991) 35-56
5. Cornish-Bowden A. Fundamentals of Enzyme Kinetics (1995), Portland Press, London pp. 55-72
6. Cravedi J.P., Heuillet G., Peleran J.C., and Wal J.M. Disposition and metabolism of chloramphenicol in trout. Xenobiotica 15 (1985) 115-121
7. Cravedi J.P., Perdu-Durand E., and Paris A. Cytochrome P450-dependent metabolic pathways and glucuronidation in trout liver slices. Comparative Biochemistry and Physiology C 121 (1998) 267-275
8. Eggens M.L., and Galgani F. Ethoxyresorufin-o-deethylase (EROD) activity in flatfish: fast determination with a fluorescence plate reader. Marine Environment Research 33 (1992) 213-221
9. Elcombe C.R., and Lech J.J. Induction and characterization of hemoproteins P450 and monooxygenation in rainbow trout, Salmo gairdneri. Toxicology and Applied Pharmacology 49 (1979) 437-450
10. Finnson K.W., and Eales J.G. Glucuronidation of thyroxine and 3,5,3′-triiodothyronine by hepatic microsomes in rainbow trout, Oncorhynchus mykiss. Comparative Biochemistry and Physiology C 117 (1997) 193-199
11. Finnson K.W., and Eales J.G. Sulfation of thyroid hormones by liver of rainbow trout, Oncorhynchus mykiss. Comparative Biochemistry and Physiology C 120 (1998) 415-420
12. Gadagbui B., Addy M., and Goksøyr A. Species characteristics of hepatic biotransformation enzymes in two tropical freshwater teleosts, tilapia (Oreochromis niloticus) and mudfish (Clarias anguillaris). Comparative Biochemistry and Physiology C 114 (1996) 201-211
13. Gallagher E.P., and Di Giulio R.T. A comparison of glutathione-dependent enzymes in liver, gills and posterior kidney of channel catfish (Ictalurus punctatus). Comparative Biochemistry and Physiology C 102 (1992) 543-547
14. Gallagher E.P., Sheehy K.M., Lame M.W., and Segall H.J. In vitro kinetics of hepatic glutathione-s-transferase conjugation in largemouth bass and brown bullheads. Environmental Toxicology and Chemistry 19 (2000) 319-326
15. Gallagher E.P., Stapleton P.L., Slone D.H., Schlenk D., and Eaton D.L. Channel catfish glutathione-s-transferase isoenzyme activity toward (±)-anti-benzo[a]pyrene-trans-7,8-dihydrodiol-9,10-epoxide. Aquatic Toxicology 34 (1996) 135-150
16. George S. Enzymology and molecular biology of phase II xenobiotic-conjugating enzymes in fish. In: Marlins D.C., and Ostrander G.K. (Eds). Aquatic Toxicology: Molecular, Biochemical, and Cellular Perspectives (1994), Lewis Publishers, Boca Raton, FL 27-86
17. Haasch M.L., Graf W.K., Quardokus E.M., Mayer R.T., and Lech J.J. Use of 7-alkoxyphenoxazones, 7-alkyloxycoumarins and 7-alkoxyquinolines as fluorescent substrates for rainbow trout hepatic microsomes after treatment with various inducers. Biochemical Pharmacology 47 (1994) 893-903
18. Habig W.H., Pabst M.J., and Jakoby W.B. Glutathione-s-transferases: the first enzymatic step in mercapturic acid formation. Journal of Biological Chemistry 249 (1974) 7130-7139
19. Kane A.S., Kahng M.W., Reimschuessel R., Nhamburo P.T., and Lipsky M.M. UDP-glucuronosyltransferase kinetics for 3-trifluoromethyl-4-nitrophenol (TFM) in fish. Transactions of the American Fisheries Society 123 (1994) 217-222
20. Kasper C.B., and Henton D. Glucuronidation. In: Jacoby W.B. (Ed). Enzymatic Basis of Detoxification vol. II (1980), Academic Press, New York 3-36
21. 2+ homeostasis in fish and mammals via receptor-independent mechanisms. Comparative Biochemistry and Physiology A 135 (2003) 1-8
22. Kleinow K., Haasch M.L., Williams D.E., and Lech J.J. A comparison of hepatic P450 induction in rat and trout (Oncorhynchus mykiss): delineation of the site of resistance of fish to phenobarbital-type inducers. Comparative Biochemistry and Physiology C 96 (1990) 259-270
23. Laurén D.J., Halarnkar P.P., Hammock B.D., and Hinton D.E. Microsomal and cytosolic epoxide hydrolase and glutathione S-transferase activities in the gill, liver, and kidney of the rainbow trout, Salmo gairdneri. Baseline levels and optimization of assay conditions. Biochemical Pharmacology 38 (1989) 881-887
24. Lech J.J. Isolation and identification of 3-trifluoromethyl-4-nitrophenol glucuronide from bile of rainbow trout exposed to 3-fluromethyl-4-nitrophenol. Toxicology and Applied Pharmacology 24 (1973) 114-124
25. 3H] aflatoxin B1 and effects of dietary β-naphthoflavone. Comparative Biochemistry and Physiology C 78 (1984) 13-19
26. Mansui D. The great diversity of reactions catalyzed by cytochromes P450. Comparative Biochemistry and Physiology C 121 (1998) 5-14
27. Mortensen A.S., and Arukwe A. Effects of 17 α-ethynylestradiol on hormonal responses and xenobiotic biotransformation system of Atlantic salmon (Salmo salar). Aquatic Toxicology 85 (2007) 113-123
28. Nelson D.R. Metazoan cytochrome P450 evolution. Comparative Biochemistry and Physiology C 121 (1998) 15-22
29. Nishiyama T., Ogura K., Nakano H., Kaku T., Takahashi E., Ohkubo Y., Sekine K., Hiratsuka A., Kadota S., and Watabe T. Sulfation of environmental estrogens by cytosolic human sulfotransferases. Journal of Drug Metabolism and Pharmacokinetics 17 (2002) 221-228
30. Nóvoa-Valiñas M.C., Pérez-López M., and Melgar M.J. Comparative study of purification and characterization of the cytosolic glutathione S-transferases from two salmonid species: Atlantic salmon (Salmo salar) and brown trout (Salmo trutta). Comparative Biochemistry and Physiology C 131 (2002) 207-213
31. Ohkimoto K., Sughara T., Sakakibara Y., Suizo M., Liu M.-Y., Carter G., and Liu M.-C. Sulfonation of environmental estrogens by zebrafish cytosolic sulfotransferases. Biochemical and Biophysical Research Communications 309 (2003) 7-11
32. Osborn R.H., and Simpson T.H. Thyroxine metabolism in plaice, Pleuronectes platessa. General and Comparative Endocrinology 13 (1969) 524
33. Otto D.M.E., and Moon T.W. Phase I and II enzymes and antioxidant responses in different tissues of brown bullheads from relatively polluted and non-polluted systems. Archives of Environment Contamination and Toxicology 31 (1996) 141-147
34. Parkinson A. Biotransformation of xenobiotics. In: Klaassen C.D. (Ed). Casarett and Doull's Toxicology. sixth ed. (2001), McGraw-Hill, New York 133-224
35. Pathiratne A., and George S. Comparison of xenobiotic metabolizing enzymes of tilapia with those of other fish species and interspecies relationships between gene families. Marine Environment Research 42 (1996) 293-296
36. Pérez-López M., Anglade P., and Bec-Ferté M.P. Characterization of hepatic and extrahepatic glutathione-s-transferases in rainbow trout (Oncorhynchus mykiss) and their induction by 3,3′,4,4′-tetrachlorobiphenyl. Fish Physiology and Biochemistry 22 (2000) 21-32
37. Perkins, E.J., 1999. Characterization of the hepatic cytochrome P450 monooxygenase system and its role in the metabolism, toxicokinetics, and toxicity of aldicarb in channel catfish (Ictalurus punctatus). Ph.D. dissertation. University of Mississippi, Oxford (MS).
38. Perkins E.J., DeBusk B.C., and Schlenk D. Isolation of a novel hepatic CYP2-related protein from channel catfish, Ictalurus punctatus. Fish Physiology and Biochemistry 22 (2000) 199-206
39. Pham R.T., Gardner J.L., and Gallagher E.P. Conjugation of 4-hydroxynonenal by largemouth bass (Micropterus salmoides) glutathione-s-transferases. Marine Environment Research 54 (2002) 291-295
40. Reynaud S., Raveton M., and Ravanel P. Interactions between immune and biotransformation systems in fish: a review. Aquatic Toxicology 87 (2008) 139-145
41. Schell Jr. J.D., and James M.O. Glucose and sulfate conjugation of phenolic compounds by the spiny lobster (Panulirus argus). Journal of Biochemical Toxicology 4 (1989) 133-138
42. Schlenk D., DeBusk B., and Perkins E.J. 2-Methylisoborneol disposition in three strains of catfish: absence of biotransformation. Fish Physiology and Biochemistry 23 (2000) 225-232
43. Shailaja M.S., and D'Silva C. Evaluation of impact of PAH on a tropical fish, Oreochromis mossambicus using multiple biomarkers. Chemosphere 53 (2003) 835-841
44. Stephensen E., Sturve J., and Förlin L. Effects of redox cycling compounds on glutathione content and activity of glutathione-related enzymes in rainbow trout liver. Comparative Biochemistry and Physiology C 133 (2002) 435-442
45. Takimoto T., Oshima M., and Miyamato J. Comparative metabolism of fenitrothion in aquatic organisms. I. Metabolism in the euryhaline fish, Oryzias latipes and Mugil cephalus. Ecotoxicology and Environment Safety 13 (1987) 104-117
46. Ueng T.H., Ueng Y.F., and Park S.S. Comparative induction of cytochrome P450-dependent monooxygenases in the livers and gills of tilapia and carp. Aquatic Toxicology 23 (1992) 49-64
47. Ueng Y.F., and Ueng T.H. Induction and purification of cytochrome P4501A1 from 3-methylcholanthrene-treated tilapia, Oreochromis niloticus × Oreochromis aureus. Archives of Biochemistry and Biophysics 322 (1995) 347-356
48. Vaccaro E., Giorgi M., Longo V., Mengozzi G., and Gervasi P.G. Inhibition of cytochrome P450 enzymes by enrofloxacin in the sea bass (Dicentrarchus labrax). Aquatic Toxicology 62 (2003) 27-33
49. Vodicnik M.J., Elcombe C.R., and Lech J.J. The effect of various types of inducing agents on hepatic microsomal monooxygenase activity in rainbow trout. Toxicology and Applied Pharmacology 59 (1981) 364-374
50. Whyte J.J., Jung R.E., Schmitt C.J., and Tillitt D.E. Ethoxyresorufin-O-deethylase (EROD) activity in fish as a biomarker of chemical exposure. Critical Reviews in Toxicology 30 (2000) 347-570
51. Yamazaki H., Inoue K., Mimura M., Oda Y., Guenguerich F.P., and Shimada T. 7-Ethoxycoumarin O-deethylation catalyzed by cytochromes P450 1A2 and 2E1 in human liver microsomes. Biochemical Pharmacology 51 (1996) 313-319
52. Yun C.H., Shimada T., and Guengerich F. Purification and characterization of human liver microsomal cytochrome P4502A6. Molecular Pharmacology 40 (1991) 679-685