| http://purl.uniprot.org/citations/20007297 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/20007297 | http://www.w3.org/2000/01/rdf-schema#comment | "The extrahepatic UDP-glucuronosyltransferase 1A10 (UGT1A10) is a phase II metabolizing enzyme that is active against a number of potent carcinogens. In the present study, UGT1A10 was examined for activity against 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanol (NNAL), the major procarcinogenic metabolite of the potent tobacco-specific nitrosamine 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone, and the promoter region of UGT1A10 was examined for variants that could lead to altered UGT1A10 expression. UGT1A10-overexpressing cell homogenates exhibited high O-glucuronidation activity against NNAL (K(M) = 5.95 mM). A 2000-base pair (bp) product corresponding to the UGT1A10 proximal promoter region was polymerase chain reaction (PCR)-amplified using genomic DNA from 97 white subjects, and 42 of these were sequenced. In addition to a previously reported C/G single-nucleotide polymorphism at -1271 bp (rs2741032), a novel 1664-bp deletion located between nucleotides -190 to -1856 relative to the UGT1A10 translation start site was identified. Using real-time multiplex PCR, this deletion exhibited a prevalence of 0.022 in whites (n = 156) and 0.056 in blacks (n = 133). To determine whether either polymorphism altered gene expression, in vitro assays were performed using luciferase constructs containing up to 2000 bp of the proximal UGT1A10 promoter. Constructs containing the 1664-bp deletion exhibited a significant (p = 0.009) 3-fold increase in luciferase activity compared with constructs containing the wild-type UGT1A10 promoter. No effect on luciferase activity was observed for the UGT1A10(-1271G) promoter variant. These data are consistent with previous studies that indicate the presence of a transcriptional repressor element within the newly identified deletion and that this deletion polymorphism may contribute to altered UGT1A10 expression and altered carcinogen detoxification between individuals."xsd:string |
| http://purl.uniprot.org/citations/20007297 | http://purl.org/dc/terms/identifier | "doi:10.1124/dmd.109.030569"xsd:string |
| http://purl.uniprot.org/citations/20007297 | http://purl.uniprot.org/core/author | "Chen G."xsd:string |
| http://purl.uniprot.org/citations/20007297 | http://purl.uniprot.org/core/author | "Dellinger R.W."xsd:string |
| http://purl.uniprot.org/citations/20007297 | http://purl.uniprot.org/core/author | "Lazarus P."xsd:string |
| http://purl.uniprot.org/citations/20007297 | http://purl.uniprot.org/core/author | "Balliet R.M."xsd:string |
| http://purl.uniprot.org/citations/20007297 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
| http://purl.uniprot.org/citations/20007297 | http://purl.uniprot.org/core/name | "Drug Metab Dispos"xsd:string |
| http://purl.uniprot.org/citations/20007297 | http://purl.uniprot.org/core/pages | "484-490"xsd:string |
| http://purl.uniprot.org/citations/20007297 | http://purl.uniprot.org/core/title | "UDP-glucuronosyltransferase 1A10: activity against the tobacco-specific nitrosamine, 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanol, and a potential role for a novel UGT1A10 promoter deletion polymorphism in cancer susceptibility."xsd:string |
| http://purl.uniprot.org/citations/20007297 | http://purl.uniprot.org/core/volume | "38"xsd:string |
| http://purl.uniprot.org/citations/20007297 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/20007297 |
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| http://purl.uniprot.org/uniprot/Q13406 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/20007297 |