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| Subject | Predicate | Object |
|---|---|---|
| http://purl.uniprot.org/citations/18719240 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/18719240 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/18719240 | http://www.w3.org/2000/01/rdf-schema#comment | "The glucuronidation of 17beta-estradiol (beta-estradiol) and 17alpha-estradiol (epiestradiol) was studied to elucidate how the orientation of the 17-OH group affects conjugation at the 3-OH or the 17-OH of either diastereomer. Recombinant human UDP-glucuronosyltransferases (UGTs) UGT1A1, UGT1A3, UGT1A7, UGT1A8, and UGT1A10 conjugated one or both diastereomers, mainly at the 3-OH. The activity of UGT1A4 was low and unique because it was directed merely toward the 17-OH of both aglycones. UGT1A10 exhibited particularly high estradiol glucuronidation activity, the rate and affinity of which were significantly higher in the case of beta-estradiol than with epiestradiol. UGT1A9 did not catalyze estradiol glucuronidation, but UGT1A9-catalyzed scopoletin glucuronidation was competitively inhibited by beta-estradiol. UGT2B4, UGT2B7, and UGT2B17 exclusively conjugated the estradiols at the 17-OH position in a highly stereoselective fashion. UGT2B4 was specific for epiestradiol; UGT2B7 glucuronidated both diastereomers, with high affinity for epiestradiol, whereas UGT2B17 only glucuronidated beta-estradiol. UGT2B15 glucuronidated both estradiols at the 3-OH, with a strong preference for epiestradiol. Human UGT2A1 and UGT2A2 glucuronidated both diastereoisomers at both hydroxyl groups. Microsomal studies revealed that human liver mainly yielded epiestradiol 17-O-glucuronide, and human intestine primarily yielded beta-estradiol 3-O-glucuronide, whereas rat liver preferentially formed beta-estradiol 17-O-glucuronide. Of the three recombinant rat UGTs that were examined in this study, rUGT2B1 was specific for the 17-OH of beta-estradiol, rUGT2B2 did not catalyze estradiol glucuronidation, whereas rUGT2B3 exhibited high activity toward the 17-OH in both diastereoisomers. The results show that although many UGTs can catalyze estradiol glucuronidation, there are marked differences in their kinetics, regioselectivity, and stereoselectivity."xsd:string |
| http://purl.uniprot.org/citations/18719240 | http://purl.org/dc/terms/identifier | "doi:10.1124/dmd.108.022731"xsd:string |
| http://purl.uniprot.org/citations/18719240 | http://purl.org/dc/terms/identifier | "doi:10.1124/dmd.108.022731"xsd:string |
| http://purl.uniprot.org/citations/18719240 | http://purl.uniprot.org/core/author | "Finel M."xsd:string |
| http://purl.uniprot.org/citations/18719240 | http://purl.uniprot.org/core/author | "Finel M."xsd:string |
| http://purl.uniprot.org/citations/18719240 | http://purl.uniprot.org/core/author | "Ikushiro S."xsd:string |
| http://purl.uniprot.org/citations/18719240 | http://purl.uniprot.org/core/author | "Ikushiro S."xsd:string |
| http://purl.uniprot.org/citations/18719240 | http://purl.uniprot.org/core/author | "Miners J.O."xsd:string |
| http://purl.uniprot.org/citations/18719240 | http://purl.uniprot.org/core/author | "Miners J.O."xsd:string |
| http://purl.uniprot.org/citations/18719240 | http://purl.uniprot.org/core/author | "Itaeaho K."xsd:string |
| http://purl.uniprot.org/citations/18719240 | http://purl.uniprot.org/core/author | "Itaeaho K."xsd:string |
| http://purl.uniprot.org/citations/18719240 | http://purl.uniprot.org/core/author | "Mackenzie P.I."xsd:string |
| http://purl.uniprot.org/citations/18719240 | http://purl.uniprot.org/core/author | "Mackenzie P.I."xsd:string |
| http://purl.uniprot.org/citations/18719240 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
| http://purl.uniprot.org/citations/18719240 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
| http://purl.uniprot.org/citations/18719240 | http://purl.uniprot.org/core/name | "Drug Metab. Dispos."xsd:string |
| http://purl.uniprot.org/citations/18719240 | http://purl.uniprot.org/core/name | "Drug Metab. Dispos."xsd:string |
| http://purl.uniprot.org/citations/18719240 | http://purl.uniprot.org/core/pages | "2307-2315"xsd:string |
| http://purl.uniprot.org/citations/18719240 | http://purl.uniprot.org/core/pages | "2307-2315"xsd:string |
| http://purl.uniprot.org/citations/18719240 | http://purl.uniprot.org/core/title | "The configuration of the 17-hydroxy group variably influences the glucuronidation of beta-estradiol and epiestradiol by human UDP-glucuronosyltransferases."xsd:string |
| http://purl.uniprot.org/citations/18719240 | http://purl.uniprot.org/core/title | "The configuration of the 17-hydroxy group variably influences the glucuronidation of beta-estradiol and epiestradiol by human UDP-glucuronosyltransferases."xsd:string |
| http://purl.uniprot.org/citations/18719240 | http://purl.uniprot.org/core/volume | "36"xsd:string |
| http://purl.uniprot.org/citations/18719240 | http://purl.uniprot.org/core/volume | "36"xsd:string |