The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Human UDP-Glucuronosyltransferases: Metabolism, Expression, and Disease
Abstract
In vertebrates, the glucuronidation of small lipophilic agents is catalyzed by the endoplasmic reticulum UDP-glucuronosyltransferases (UGTs). This metabolic pathway leads to the formation of water-soluble metabolites originating from normal dietary processes, cellular catabolism, or exposure to drugs and xenobiotics. This classic detoxification process, which led to the discovery nearly 50 years ago of the cosubstrate UDP-glucuronic acid ( 19 ), is now known to be carried out by 15 human UGTs. Characterization of the individual gene products using cDNA expression experiments has led to the identification of over 350 individual compounds that serve as substrates for this superfamily of proteins. This data, coupled with the introduction of sophisticated RNA detection techniques designed to elucidate patterns of gene expression of the UGT superfamily in human liver and extrahepatic tissues of the gastrointestinal tract, has aided in understanding the contribution of glucuronidation toward epithelial first-pass metabolism. In addition, characterization of the UGT1A locus and genetic studies directed at understanding the role of bilirubin glucuronidation and the biochemical basis of the clinical symptoms found in unconjugated hyperbilirubinemia have uncovered the structural gene polymorphisms associated with Crigler-Najjar’s and Gilbert’s syndrome. The role of the UGTs in metabolism and different disease states in humans is the topic of this review.
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Cites
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Metadata
- Authors
- Tukey, R. H., & Strassburg, C. P.
- Venue
- Annual Review of Pharmacology and Toxicology
- Publisher
- Annual Reviews
- Published
- 2000-04
- Volume
- 40
- Issue
- 1
- Pages
- 581-616
- ISSN
- 0362-1642 (ISSN-L)
- 1545-4304
- OpenAlex
- W2132804094
- Cited by
- 1,523
- References
- 1
- FWCI
- 7.66
- Type
- journal article
- Language
- en
- Open access
- closed
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