ArticleDrug metabolism and disposition: the biological fate of chemicals2015
Xenobiotic Metabolism in Mice Lacking the UDP-Glucuronosyltransferase 2 Family.
Article in Drug metabolism and disposition: the biological fate of chemicals, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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The trial behind it
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Who cites it
10 citing papers in PubMed, 24 citations in OpenAlex.
- Comparative Analysis of Selected UGT and SULT mRNA Expression in Non-Obese Rat Models of Metabolic Syndrome.Biomedicines · 2026Article
- Analysis of in vitro and in vivo metabolism of zidovudine and gemfibrozil in trans-chromosomic mouse line expressing human UGT2 enzymes.Pharmacology research & perspectives · 2022Article
- Convergent copy number increase of genes associated with freshwater colonization in fishes.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2022Article
- Can Antioxidants Reduce the Toxicity of Bisphenol?Antioxidants (Basel, Switzerland) · 2022Review
- Animal models of endocrine disruption.Best practice & research. Clinical endocrinology & metabolism · 2018Review
- Species differences in drug glucuronidation: Humanized UDP-glucuronosyltransferase 1 mice and their application for predicting drug glucuronidation and drug-induced toxicity in humans.Drug metabolism and pharmacokinetics · 2018Review
- Article
- Hepatic Detoxification of Bisphenol A is Retinoid-Dependent.Toxicological sciences : an official journal of the Society of Toxicology · 2017Article
- Bisphenol-A glucuronidation in human liver and breast: identification of UDP-glucuronosyltransferases (UGTs) and influence of genetic polymorphisms.Xenobiotica; the fate of foreign compounds in biological systems · 2017Article
- Structure and Protein-Protein Interactions of Human UDP-Glucuronosyltransferases.Frontiers in pharmacology · 2016Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
UDP-Glucuronosyltransferases (UGTs) conjugate a glucuronyl group from glucuronic acid to a wide range of lipophilic substrates to form a hydrophilic glucuronide conjugate. The glucuronide generally has decreased bioactivity and increased water solubility to facilitate excretion. Glucuronidation represents an important detoxification pathway for both endogenous waste products and xenobiotics, including drugs and harmful industrial chemicals. Two clinically significant families of UGT enzymes are present in mammals: UGT1s and UGT2s. Although the two families are distinct in gene structure, studies using recombinant enzymes have shown considerable overlap in their ability to glucuronidate many substrates, often obscuring the relative importance of the two families in the clearance of particular substrates in vivo. To address this limitation, we have generated a mouse line, termed ΔUgt2, in which the entire Ugt2 gene family, extending over 609 kilobase pairs, is excised. This mouse line provides a means to determine the contributions of the two UGT families in vivo. We demonstrate the utility of these animals by defining for the first time the in vivo contributions of the UGT1 and UGT2 families to glucuronidation of the environmental estrogenic agent bisphenol A (BPA). The highest activity toward this chemical is reported for human and rodent UGT2 enzymes. Surprisingly, our studies using the ΔUgt2 mice demonstrate that, while both UGT1 and UGT2 isoforms can conjugate BPA, clearance is largely dependent on UGT1s.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.