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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Bibliographic Details
Published in:Scientific reports 2015-04, Vol.5 (1), p.9627-9627, Article 9627
Main Authors: Jiang, Li, Liang, Si-Cheng, Wang, Chao, Ge, Guang-Bo, Huo, Xiao-Kui, Qi, Xiao-Yi, Deng, Sa, Liu, Ke-Xin, Ma, Xiao-Chi
Format: Article
Language:English
Subjects:
49/47
631/92/607/1172
692/700/565/1436/1983
82/16
82/58
82/80
Bufanolides - chemistry
Bufanolides - metabolism
Detoxification
Enzyme Inhibitors - chemistry
Enzymes
Glucuronosyltransferase
Glucuronosyltransferase - genetics
Glucuronosyltransferase - metabolism
Humanities and Social Sciences
Humans
Kinetics
multidisciplinary
Protein Isoforms - genetics
Protein Isoforms - metabolism
Recombinant Proteins - biosynthesis
Recombinant Proteins - genetics
Science
Substrate Specificity
Uridine
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Summary: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.
ISSN:2045-2322
2045-2322
DOI:10.1038/srep09627