Identifying and applying a highly selective probe to simultaneously determine the O-glucuronidation activity of human UGT1A3 and UGT1A4

Glucuronidation mediated by uridine 5′-diphospho (UDP)-glucuronosyltransferase is an important detoxification pathway. However, identifying a selective probe of UDP- glucuronosyltransferase is complicated because of the significant overlapping substrate specificity displayed by the enzyme. In this p...

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Autores principales: Jiang, Li, Liang, Si-Cheng, Wang, Chao, Ge, Guang-Bo, Huo, Xiao-Kui, Qi, Xiao-Yi, Deng, Sa, Liu, Ke-Xin, Ma, Xiao-Chi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2015
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4401096/
https://www.ncbi.nlm.nih.gov/pubmed/25884245
http://dx.doi.org/10.1038/srep09627
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author Jiang, Li
Liang, Si-Cheng
Wang, Chao
Ge, Guang-Bo
Huo, Xiao-Kui
Qi, Xiao-Yi
Deng, Sa
Liu, Ke-Xin
Ma, Xiao-Chi
author_facet Jiang, Li
Liang, Si-Cheng
Wang, Chao
Ge, Guang-Bo
Huo, Xiao-Kui
Qi, Xiao-Yi
Deng, Sa
Liu, Ke-Xin
Ma, Xiao-Chi
author_sort Jiang, Li
collection PubMed
description Glucuronidation mediated by uridine 5′-diphospho (UDP)-glucuronosyltransferase is an important detoxification pathway. However, identifying a selective probe of UDP- glucuronosyltransferase is complicated because of the significant overlapping substrate specificity displayed by the enzyme. In this paper, desacetylcinobufagin (DACB) 3-O- and 16-O-glucuronidation were found to be isoform-specific probe reactions for UGT1A4 and UGT1A3, respectively. DACB was well characterized as a probe for simultaneously determining the catalytic activities of O-glucuronidation mediated by UGT1A3 and UGT1A4 from various enzyme sources, through a sensitive analysis method.
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spelling pubmed-44010962015-04-24 Identifying and applying a highly selective probe to simultaneously determine the O-glucuronidation activity of human UGT1A3 and UGT1A4 Jiang, Li Liang, Si-Cheng Wang, Chao Ge, Guang-Bo Huo, Xiao-Kui Qi, Xiao-Yi Deng, Sa Liu, Ke-Xin Ma, Xiao-Chi Sci Rep Article Glucuronidation mediated by uridine 5′-diphospho (UDP)-glucuronosyltransferase is an important detoxification pathway. However, identifying a selective probe of UDP- glucuronosyltransferase is complicated because of the significant overlapping substrate specificity displayed by the enzyme. In this paper, desacetylcinobufagin (DACB) 3-O- and 16-O-glucuronidation were found to be isoform-specific probe reactions for UGT1A4 and UGT1A3, respectively. DACB was well characterized as a probe for simultaneously determining the catalytic activities of O-glucuronidation mediated by UGT1A3 and UGT1A4 from various enzyme sources, through a sensitive analysis method. Nature Publishing Group 2015-04-17 /pmc/articles/PMC4401096/ /pubmed/25884245 http://dx.doi.org/10.1038/srep09627 Text en Copyright © 2015, Macmillan Publishers Limited. All rights reserved http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder in order to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
spellingShingle Article
Jiang, Li
Liang, Si-Cheng
Wang, Chao
Ge, Guang-Bo
Huo, Xiao-Kui
Qi, Xiao-Yi
Deng, Sa
Liu, Ke-Xin
Ma, Xiao-Chi
Identifying and applying a highly selective probe to simultaneously determine the O-glucuronidation activity of human UGT1A3 and UGT1A4
title Identifying and applying a highly selective probe to simultaneously determine the O-glucuronidation activity of human UGT1A3 and UGT1A4
title_full Identifying and applying a highly selective probe to simultaneously determine the O-glucuronidation activity of human UGT1A3 and UGT1A4
title_fullStr Identifying and applying a highly selective probe to simultaneously determine the O-glucuronidation activity of human UGT1A3 and UGT1A4
title_full_unstemmed Identifying and applying a highly selective probe to simultaneously determine the O-glucuronidation activity of human UGT1A3 and UGT1A4
title_short Identifying and applying a highly selective probe to simultaneously determine the O-glucuronidation activity of human UGT1A3 and UGT1A4
title_sort identifying and applying a highly selective probe to simultaneously determine the o-glucuronidation activity of human ugt1a3 and ugt1a4
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4401096/
https://www.ncbi.nlm.nih.gov/pubmed/25884245
http://dx.doi.org/10.1038/srep09627
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