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UDP glucuronosyltransferase 1 family, polypeptide A10

UGT1A10, UDP-glucuronosyltransferase 1A10
This gene encodes a UDP-glucuronosyltransferase, an enzyme of the glucuronidation pathway that transforms small lipophilic molecules, such as steroids, bilirubin, hormones, and drugs, into water-soluble, excretable metabolites. This gene is part of a complex locus that encodes several UDP-glucuronosyltransferases. The locus includes thirteen unique alternate first exons followed by four common exons. Four of the alternate first exons are considered pseudogenes. Each of the remaining nine 5' exons may be spliced to the four common exons, resulting in nine proteins with different N-termini and identical C-termini. Each first exon encodes the substrate binding site, and is regulated by its own promoter. The enzyme encoded by this gene has glucuronidase activity on mycophenolic acid, coumarins, and quinolines. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: UDP-glucuronosyltransferase, UGT1A1, Glucuronosyltransferase, UGT, UGT1A9
Papers on UGT1A10
Glucuronidation of estrone and 16α-hydroxyestrone by human UGT enzymes: The key roles of UGT1A10 and UGT2B7.
Finel et al., Helsinki, Finland. In J Steroid Biochem Mol Biol, Nov 2015
The results revealed that UGT1A10 is by far the most active enzyme in estrone glucuronidation.
Inhibition of Human UDP-Glucuronosyltransferase Enzymes by Canagliflozin and Dapagliflozin: Implications for Drug-Drug Interactions.
Miners et al., Adelaide, Australia. In Drug Metab Dispos, Oct 2015
CNF inhibited all UGT1A subfamily enzymes, but the greatest inhibition was observed with UGT1A1, UGT1A9, and UGT1A10 (IC50 values ≤ 10 µM).
Milk Thistle Constituents Inhibit Raloxifene Intestinal Glucuronidation: A Potential Clinically Relevant Natural Product-Drug Interaction.
Paine et al., Greensboro, United States. In Drug Metab Dispos, Sep 2015
The objective of this work was to evaluate the inhibitory effects of individual milk thistle constituents on the intestinal glucuronidation of raloxifene using human intestinal microsomes and human embryonic kidney cell lysates overexpressing UGT1A1, UGT1A8, and UGT1A10, isoforms highly expressed in the intestine that are critical to raloxifene clearance.
Role of cytochrome P450 and UDP-glucuronosyltransferases in metabolic pathway of homoegonol in human liver microsomes.
Lee et al., Puch'ŏn, South Korea. In Drug Metab Pharmacokinet, Aug 2015
Glucuronidation of homoegonol to M5 was mediated by UGT1A1, UGT1A3, UGT1A4, and UGT2B7 enzymes, whereas M4 was formed from 4-O-demethylhomoegonol by UGT1A1, UGT1A8, UGT1A10, and UGT2B15 enzymes.
Differential expression of the UGT1A family of genes in stomach cancer tissues.
Oztuzcu et al., Ankara, Turkey. In Tumour Biol, Aug 2015
Accordingly, UGT1A1, UGT1A8, and UGT1A10 were found to be upregulated, and UGT1A3, UGT1A5, UGT1A7, and UGT1A9 were downregulated in stomach tumors.
Glucuronidation of OTS167 in Humans Is Catalyzed by UDP-Glucuronosyltransferases UGT1A1, UGT1A3, UGT1A8, and UGT1A10.
Ratain et al., Chicago, United States. In Drug Metab Dispos, Jul 2015
UGT1A1 (64 µl/min/mg) and UGT1A8 (72 µl/min/mg) exhibited the highest intrinsic clearances (CLint) for OTS167, followed by UGT1A3 (51 µl/min/mg) and UGT1A10 (47 µl/min/mg); UGT1A9 was a minor contributor.
Targeted screen for human UDP-glucuronosyltransferases inhibitors and the evaluation of potential drug-drug interactions with zafirlukast.
Nakajima et al., Kanazawa, Japan. In Drug Metab Dispos, Jun 2015
To evaluate potential DDIs caused by inhibition of intestinal UGTs, we assessed inhibitory effects of 578 compounds, including drugs, xenobiotics, and endobiotics, on human UGT1A8 and UGT1A10, which are major contributors to intestinal glucuronidation.
Differences in the glucuronidation of bisphenols F and S between two homologous human UGT enzymes, 1A9 and 1A10.
Finel et al., Ljubljana, Slovenia. In Xenobiotica, 2014
3. The results revealed that UGT1A9, primarily a hepatic enzyme, is mainly responsible for BPS glucuronidation, whereas UGT1A10, an intestine enzyme that is highly homologous to UGT1A9 at the protein level, is by far the most active UGT in BPF glucuronidation.
Interaction between oblongifolin C and UDP-glucuronosyltransferase isoforms in human liver and intestine microsomes.
Ma et al., Shanghai, China. In Xenobiotica, 2014
μM, whereas non-competitively inhibited UGT1A10 with a Ki value of 2.12 ± 0.18 μM. 4. Understanding the interaction between OC and UGTs will greatly contribute to future investigations regarding the inter-individual differences in OC metabolism in clinical trials and potential drug-drug interactions.
The Inhibition of the Components from Shengmai Injection towards UDP-Glucuronosyltransferase.
Fang et al., Jinzhou, China. In Evid Based Complement Alternat Med, 2013
Based on the inhibition kinetic investigation results, ophiopogonin D (OD) noncompetitively inhibited UGT1A6 and competitively inhibited UGT1A8, ophiopogonin D' (OD') noncompetitively inhibited UGT1A6 and UGT1A10, and ruscorectal (RU) exhibited competitive inhibition towards UGT1A4.
Identification of UDP-glucuronosyltransferases responsible for the glucuronidation of darexaban, an oral factor Xa inhibitor, in human liver and intestine.
Usui et al., Ōsaka, Japan. In Drug Metab Dispos, 2012
Data suggest that darexaban glucuronidation in jejunum microsomes is mainly catalyzed by UGT1A10; studies include kinetics of recombinant UGT proteins, liver microsomes, and jejunal microsomes (and UGT isoform-specific inhibitors/substrates).
Phenylalanine 93 of the human UGT1A10 plays a major role in the interactions of the enzyme with estrogens.
Finel et al., Helsinki, Finland. In Steroids, 2012
role of Phenylalanine 93 in UGT1A10
In vitro and in vivo small intestinal metabolism of CYP3A and UGT substrates in preclinical animals species and humans: species differences.
Iwaki et al., Ōsaka, Japan. In Drug Metab Rev, 2011
Additionally, the intestinal-specific UGT would be UGT1A10 for humans, UGT1A8 for monkeys, and UGT1A7 for rats.
Use of glucuronidation fingerprinting to describe and predict mono- and dihydroxyflavone metabolism by recombinant UGT isoforms and human intestinal and liver microsomes.
Hu et al., Guangzhou, China. In Mol Pharm, 2010
The results also indicated that UGT1A1, UGT1A7, UGT1A8, UGT1A9, UGT1A10 and UGT2B7 are the most important six UGT isoforms for metabolizing the three dihydroxyflavones and seven monohydroxyflavones.
How many and which amino acids are responsible for the large activity differences between the highly homologous UDP-glucuronosyltransferases (UGT) 1A9 and UGT1A10?
Finel et al., Helsinki, Finland. In Drug Metab Dispos, 2010
it appears that residues within segment C of the N-terminal domain, mainly at positions 152 and 169, contribute to the higher glucuronidation rates of UGT1A10
Glucuronidation of psilocin and 4-hydroxyindole by the human UDP-glucuronosyltransferases.
Finel et al., Helsinki, Finland. In Drug Metab Dispos, 2010
Data point to UGT1A10 as primary UGT isoform metabolizing psilocin (a hallucinogenic indole alkaloid) in small intestine; kinetic studies are included.
Genetic polymorphisms of smoking-related carcinogen detoxifying enzymes and head and neck cancer susceptibility.
Manni et al., Maastricht, Netherlands. In Anticancer Res, 2009
For the UGTs, only variants in UGT1A7 and UGT1A10 have been studied, both of which were associated with an altered risk for SCCHN.
Polymorphism of UDP-glucuronosyltransferase and drug metabolism.
Takeuchi et al., Ōtsu, Japan. In Curr Drug Metab, 2005
Recent studies also revealed a widespread presence of diverse polymorphisms in other isoforms of UGT1 as well as the UGT2 family, including UGT1A6, UGTG1A7, UGT1A8, UGT1A10, UGT2B4, UGT2B7 and UGT2B15.
UDP-glucuronosyltransferases and clinical drug-drug interactions.
Chang et al., Vancouver, Canada. In Pharmacol Ther, 2005
The human UGT superfamily is comprised of 2 families (UGT1 and UGT2) and 3 subfamilies (UGT1A, UGT2A, and UGT2B).
Regulation of UDP glucuronosyltransferases in the gastrointestinal tract.
Mackenzie et al., Australia. In Toxicol Appl Pharmacol, 2004
UGTs such as UGT1A7, UGT1A8, and UGT1A10 are exclusively expressed in gastrointestinal tissues, each with a unique tissue distribution pattern that is subject to interindividual variation.
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