Hepatic demethylation of methoxy-bromodiphenyl ethers and conjugation of the resulting hydroxy-bromodiphenyl ethers in a marine fish, the red snapper, Lutjanus campechanus, and a freshwater fish, the channel catfish, Ictalurus punctatus
| Autor: | Margaret O. James, Katherine V. Cisneros, Laura R. Faux, Claire J. Weaver, Amany Sultan, Vinayak Agarwal, Christiane Hindrichs |
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| Rok vydání: | 2022 |
| Předmět: |
Environmental Engineering
Health Toxicology and Mutagenesis Glucuronidation Lutjanus campechanus Fresh Water chemistry.chemical_compound food Biotransformation Halogenated Diphenyl Ethers Animals Environmental Chemistry Demethylation biology Chemistry Public Health Environmental and Occupational Health General Medicine General Chemistry biology.organism_classification Pollution food.food Ictaluridae Liver Biochemistry Ictalurus Microsomes Liver Freshwater fish Xenobiotic Catfish |
| Zdroj: | Chemosphere. 286:131620 |
| ISSN: | 0045-6535 |
| Popis: | Methoxylated bromodiphenyl ethers (MeO-BDEs), marine natural products, can be demethylated by cytochrome P450 to produce hydroxylated bromodiphenyl ethers (OH-BDEs), potentially toxic metabolites that are also formed by hydroxylation of BDE flame retardants. The OH-BDEs may be detoxified by glucuronidation and sulfonation. This study examined the demethylation of 6-MeO-BDE47, 2′-MeO-BDE68 and 4′-MeO-BDE68, in hepatic microsomes from the red snapper, Lutjanus campechanus, a marine fish likely to be exposed naturally to MeO-BDEs, and the channel catfish, Ictalurus punctatus, a freshwater fish in which pathways of xenobiotic biotransformation have been studied. We further studied the glucuronidation and sulfonation of the resulting OH-BDEs as well as of 6-OH-2′-MeO-BDE68 in hepatic microsomes and cytosol fractions of these fish. The three studied biotransformation pathways were active in both species, with high individual variability. The range of activities overlapped in the two species. Demethylation of MeO-BDEs, studied in the concentration range 10–500 μM, followed Michaelis-Menten kinetics in both fish species, however enzyme efficiencies were low, ranging from 0.024 to 0.334 μL min.mg protein. Conjugation of the studied OH-BDEs followed Michaelis-Menten kinetics in the concentration ranges 1–50 μM (glucuronidation) or 2.5–100 μM (sulfonation). These OH-BDEs were readily glucuronidated and sulfonated in the fish livers of both species, with enzyme efficiencies one to three orders of magnitude higher than for demethylation of the precursor MeO-BDEs. The relatively low efficiencies of demethylation of the MeO-BDEs, compared with higher efficiencies for OH-BDE conjugation, suggests that MeO-BDEs are more likely than OH-BDEs to bioaccumulate in tissues of exposed fish. |
| Databáze: | OpenAIRE |
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