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• W2136434035 abstract "Metabolism of polychlorinated dibenzo-<i>p</i>-dioxins by cytochrome P450 (P450) and UDP-glucuronosyltransferase (UGT) was examined using a recombinant enzyme system and human liver microsomes. We analyzed the glucuronidation of 2,3,7-trichlorodibenzo-<i>p</i>-dioxin (2,3,7-triCDD) by rat CYP1A1 expressed in yeast microsomes and human UGT expressed in baculovirus-infected insect cells. Multiple UGT isozymes showed glucuronidation activity toward 8-hydroxy-2,3,7-triCDD (8-OH-2,3,7-triCDD), which was produced by CYP1A1. Of these UGTs, UGT1A1, 1A9, and 2B7, which are constitutively expressed in human livers, showed remarkable activity toward 8-OH-2,3,7-triCDD. The apparent kinetic parameters of glucuronidation, <i>K</i>_m and <i>k</i>_cat, were estimated to be 0.8 μM and 1.8 min^-1, respectively, for UGT1A1, 0.8 μM and 1.8 min^-1, respectively, for UGT1A9, and 3.9 μM and 7.0 min^-1, respectively, for UGT2B7. In human liver microsomes with NADPH and UDP-glucuronic acid, 2,3,7-triCDD was first converted to 8-OH-2,3,7-triCDD, then further converted to its glucuronide. We compared the ability of 10 human liver microsomes to metabolize 2,3,7-triCDD and observed a significant difference in the glucuronidation of 2,3,7-triCDD that originated from the difference of the P450-dependent hydroxylation of 2,3,7-triCDD." @default.
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• W2136434035 date "2004-07-16" @default.
• W2136434035 modified "2023-10-18" @default.
• W2136434035 title "SEQUENTIAL METABOLISM OF 2,3,7-TRICHLORODIBENZO-<i>P</i>-DIOXIN (2,3,7-triCDD) BY CYTOCHROME P450 AND UDP-GLUCURONOSYLTRANSFERASE IN HUMAN LIVER MICROSOMES" @default.
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• W2136434035 doi "https://doi.org/10.1124/dmd.32.8.870" @default.
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