Metabolism of 2,3′,4′,5-tetrachlorobiphenyl by cytochrome P450 from rats, guinea pigs and hamsters

The metabolism of 2,3′,4′,5-tetrachlorobiphenyl (TCB) was compared using liver microsomes and six isoforms of cytochrome P450 purified from rats, guinea pigs and hamsters. In microsomal study, the following species differences were observed: 1) Untreated guinea pigs and hamsters but not rats can met...

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Bibliographic Details
Published in:Chemosphere (Oxford) 1998-10, Vol.37 (9), p.1895-1904
Main Authors: Koga, Nobuyuki, Kikuichi, Naoko, Kanamaru, Tomoyo, Kuroki, Hiroaki, Matsusue, Kimihiko, Ishida, Chuzo, Ariyoshi, Noritaka, Oguri, Kazuta, Yoshimura, Hidetoshi
Format: Article
Language:English
Subjects:
Animals
Biological and medical sciences
Chemical and industrial products toxicology. Toxic occupational diseases
Cricetinae
Cytochrome P-450 Enzyme System - metabolism
cytochrome P450
Environmental Pollutants - metabolism
Environmental Pollutants - pharmacokinetics
guinea pig
Guinea Pigs
hamster
Hydroxylation
Isoenzymes
Male
Medical sciences
metabolism
Microsomes, Liver
Polychlorinated Biphenyls - metabolism
Polychlorinated Biphenyls - pharmacokinetics
rat
Rats
Rats, Wistar
TCDD
tetrachlorobiphenyl
Toxicology
Various organic compounds
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Summary:The metabolism of 2,3′,4′,5-tetrachlorobiphenyl (TCB) was compared using liver microsomes and six isoforms of cytochrome P450 purified from rats, guinea pigs and hamsters. In microsomal study, the following species differences were observed: 1) Untreated guinea pigs and hamsters but not rats can metabolize this TCB to 3-hydroxy- or 4-hydroxy-2,3′,4′,5-TCB, 2) Guinea pig microsomes showed only 3-hydroxylatiog activity, whereas hamster microsomes showed higher activity of 4-hydroxylation than that of 3-hydroxylation. In common with three species, the 3-hydroxylation was accelerated by phenobarbital. The 4-hydroxylation in rats and hamsters was increased by pretreatment with 3-methylcholanthrene and 3,3′,4,4′,5-pentachlorobiphenyl. The hydroxylation activities of liver microsomes from the three species could be explained by an involvement of different isoforms of cytochrome P450. In addition, it is apparent that hamster CYP1A2 as well as hamster CYP2A8 is involved in the 4-hydroxylation of 2,3′,4′,5-TCB although it has no activity for 2,2′,5,5′-TCB.
ISSN:0045-6535
1879-1298
DOI:10.1016/S0045-6535(98)00256-2