ArticleEuropean journal of drug metabolism and pharmacokinetics2019
Glucuronidation of D-Luciferin In Vitro: Isoform Selectivity and Kinetics Characterization.
Article in European journal of drug metabolism and pharmacokinetics, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
1 citing paper in PubMed, 2 citations in OpenAlex.
- Bioluminescence in Clinical and Point-of-Care Testing.Biosensors · 2025Review
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2 authors at 2 institutions in 1 country.
Funding
Abstract
backgroundD-luciferin is one of the most commonly used substrates in bioluminescence imaging for real-time monitoring of sophisticated biological processes in models of human biology or disease in vitro and in vivo. D-luciferin is rapidly cleared from blood circulation after being exogenously delivered in vivo and the presence of phenolic groups indicates that glucuronide conjugation is a possible metabolic pathway for the compound.
objectivesThis study aimed to characterize the glucuronidation pathway of D-luciferin in human liver microsomes (HLM) and human intestine microsomes (HIM).
methodsHLM and HIM were employed to catalyze the glucuronidation of D-luciferin in vitro. The activity of recombinant uridine-diphospho-glucuronosyltransferase (UGT) isoforms towards D-luciferin glucuronidation was screened. Chemical inhibition assay and kinetic analysis was combined to determine the UGT isoforms responsible for the formation of D-luciferin glucuronide in HLM and HIM.
resultsD-luciferin could be catalyzed to form one mono-glucuronide which was characterized as 6'-O-glucuronide in HLM and HIM. UGT1A1, 1A3, 1A6, 1A8, 1A9 and 1A10 participated in the formation of D-luciferin glucuronide, with UGT1A1 exhibiting the highest catalytic activity. Both chemical inhibition assays and kinetic analysis showed that UGT1A1 and UGT1A3 played important roles in D-luciferin-6'-O-glucuronidation in HLM and HIM, with UGT1A6 also giving a non-negligible contribution to this biotransformation in HLM.
conclusionsUGT1A1, UGT1A3 and UGT1A6 were responsible for 6'-O-glucuronidation of D-luciferin in HLM, while UGT1A1 and UGT1A3 were the major contributors to this biotransformation in HIM.
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