Abstract
The substrate specificity of human gastric and intestinal UDP-glucuronosyltransferases (UGTs) toward catechols was investigated and compared to that of liver UGTs. Small catechols were efficiently glucuronidated by stomach (0.8–10.2 nmol/mg protein·min) and intestine (0.9–7.7 nmol/mg protein·min) with activities in a range similar to those found in liver (2.9–19 nmol/mg protein·min). Large interindividual variations were observed among the samples. Immunoblot analysis demonstrated the presence of UGT1A6 and UGT2B7 in stomach and throughout the intestine. Recombinant human UGT1A6, 1A9, and 2B7, stably expressed in mammalian cells, all effectively catalyzed catechol glucuronidation. K m values (0.09–13.6 mM) indicated low affinity for UGTs and V max values ranged from 0.51 to 64.0 nmol/mg protein·min. These results demonstrate for the first time glucuronidation of catechols by gastric and intestinal microsomal UGTs and three human recombinant UGT isoforms.
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