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Vol. 31, Issue 5, 670-676, May 2003

Glucuronidation Activity of the UGT2B17 Enzyme toward Xenobiotics

David Turgeon,1 Jean-Sébastien Carrier,1 Sarah Chouinard, and Alain Bélanger

Oncology and Molecular Endocrinology Research Center, Centre de Recherche de l'Université Laval, Laval University, Québec City, Québec, Canada

UDP-glucuronosyltransferase (UGT) 2B17 is one of the most important conjugating enzymes in androgen metabolism and shares more than 95% homology with UGT2B15. Although UGT2B15 has been fully characterized for its ability to conjugate drugs, environmental pollutants, and dietary components, UGT2B17 received less attention for its capacity to glucuronidate xenobiotics. In the present study, more than 55 exogenous compounds belonging to several categories of compounds were analyzed as potential substrates for UGT2B17. Glucuronidation activity was observed with several coumarins, anthraquinones, and flavonoids. The higher glucuronidation activity was measured with alizarin (125 pmol · min-1 · mg protein-1), whereas UGT2B17 conjugated eugenol, scopoletin, and galangin with glucuronidation rates of 102.5, 102, and 58 pmol · min-1 · mg protein-1, respectively. The characterization of UGT2B17 as a xenobiotics-conjugating enzyme demonstrates that its role is not limited to androgen metabolism and that its specificity for exogenous substrates is different from other UGT2B isoforms. Taken together, these data suggest a role of UGT2B17 for the hepatic detoxification.

1 These authors contributed equally to this work.

Copyright © 2003 by The American Society for Pharmacology and Experimental Therapeutics


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