Full metadata record
DC Field | Value | Language |
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dc.contributor.author | 신윤용 | - |
dc.date.accessioned | 2018-12-26T16:30:02Z | - |
dc.date.available | 2018-12-26T16:30:02Z | - |
dc.date.issued | 1997 | - |
dc.identifier.issn | 0253-6269 | - |
dc.identifier.other | OAK-17374 | - |
dc.identifier.uri | https://dspace.ewha.ac.kr/handle/2015.oak/247935 | - |
dc.description.abstract | Two human liver UDP-glucuronosyltransferase cDNA clones, HLUG25 and UDPGTh2 were previously shown to encode isozymes active in the glucuronidation of hyodeoxycholic acid (HDCA) and certain estrogen derivatives (e.g., estriol and 3,4-catechol estrogens), respectively. In this study we have found that the UDPGTh2-encoded isoform (UDPGTh2) and HLUG25-encoded isoform (UDPGTh1) have parallel aglycone specificities. When expressed in COS 1 cells, each isoform metabolized three types of dihydroxy- or trihydroxy-substituted ring structures, including the 3,4-catechol estrogen (4-hydroxyestrone), estriol, 17-epiestriol, and HDCA, but the UDPGTh2 isozyme was 100-fold more efficient than UDPGTh1. UDPGTh1 and UDPGTh2 were 86% identical overall (76 differences out of 528 amino acids), including 55 differences in the first 300 amino acids of the amino terminus, a domain which conferred the substrate specificity. The data indicated that a high level of conservation in the amino terminus was not required for the preservation of substrate selectivity. Analysis of glucuronidation activity encoded by UDPGTh1/UDPGTh2 chimeric cDNA constructed at their common restriction sites, Sac I (codon 297), Nco I (codon 385), and Hha I (codon 469), showed that nine amino acids between residues 385 and 469 were important for catalytic efficiency, suggesting that this region represented a domain which was critical for the catalysis but distinct from that responsible for aglycone selection. These data indicate that UDPGTh2 is a primary isoform responsible for the detoxification of the bile salt intermediate as well as the active estrogen intermediates. | - |
dc.language | English | - |
dc.title | Comparison of glucuronidating activity of two human cDNAs, UDPGTh2 and UDPGTH2 | - |
dc.type | Review | - |
dc.relation.issue | 5 | - |
dc.relation.volume | 20 | - |
dc.relation.index | SCIE | - |
dc.relation.index | SCOPUS | - |
dc.relation.index | KCI | - |
dc.relation.startpage | 454 | - |
dc.relation.lastpage | 458 | - |
dc.relation.journaltitle | Archives of Pharmacal Research | - |
dc.identifier.scopusid | 2-s2.0-0348185607 | - |
dc.author.google | Kim S.S. | - |
dc.author.google | Owens I.S. | - |
dc.author.google | Sheen Y.Y. | - |
dc.contributor.scopusid | 신윤용(6603872711) | - |
dc.date.modifydate | 20230411104830 | - |