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. 2019 Sep:131:110542.
doi: 10.1016/j.fct.2019.05.050. Epub 2019 Jun 1.

S-equol glucuronidation in liver and intestinal microsomes of humans, monkeys, dogs, rats, and mice

Affiliations

S-equol glucuronidation in liver and intestinal microsomes of humans, monkeys, dogs, rats, and mice

Takashi Isobe et al. Food Chem Toxicol. 2019 Sep.

Abstract

S-equol, an active metabolite of the soy isoflavone daidzein, is mainly metabolized into glucuronide(s) by UDP-glucuronosyltransferase (UGT) enzymes in mammals. In the present study, S-equol glucuronidation was examined in the liver and intestinal microsomes of humans, monkeys, dogs, rats, and mice using a kinetic analysis. CLint values for 7- and 4'-glucuronidation by liver microsomes were higher than those by intestinal microsomes in all species. CLint values for total glucuronidation (sum of 7- and 4'-glucuronidation) were rats (7.6) > monkeys (5.8) > mice (4.9) > dogs (2.8) > humans (1.0) for liver microsomes, and rats (9.6) > mice (2.8) > dogs (1.3) ≥ monkeys (1.2) > humans (1.0) for intestinal microsomes, respectively. Regarding regioselective glucuronidation by liver and intestinal microsomes, CLint values were 7-glucuronidation > 4'-glucuronidation for humans, monkeys, dogs, and mice, and 4'-glucuronidation > 7-glucuronidation for rats. These results suggest that the metabolic abilities of UGT enzymes toward S-equol in the liver and intestines markedly differ among humans, monkeys, dogs, rats, and mice.

Keywords: Glucuronidation; Intestinal microsomes; Liver microsomes; S-equol; UDP-Glucuronosyltransferase (UGT).

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