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UDP glucuronosyltransferase 1 family, polypeptide A4

UDP-glucuronosyltransferase, UGT1A4, UGT1A3
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. This enzyme has some glucuronidase activity towards bilirubin, although is is more active on amines, steroids, and sapogenins. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Glucuronosyltransferase, UGT, UGT1A1, ACID, UGT2B7
Papers on UDP-glucuronosyltransferase
Detection of Total UDP-Glucuronosyltransferase (UGT) Activity in Melanoma Cells.
Meyskens et al., Irvine, United States. In Methods Mol Biol, Feb 2016
UNASSIGNED: The UDP-glucuronosyltransferases (UGTs) are integrally involved in the clearance of a wide range of drugs used to combat human diseases.
Efflux Transport Characterization of Resveratrol Glucuronides in UDP-Glucuronosyltransferase 1A1 Transfected Hela Cells: Application of a Cellular Pharmacokinetic Model to Decipher the Contribution of Multidrug Resistance-Associated Protein 4.
Wu et al., Jinan, China. In Drug Metab Dispos, Feb 2016
UNASSIGNED: Resveratrol undergoes extensive metabolism to form biologically active glucuronides in humans.
Albumin's Influence on Carprofen Enantiomers-Hymecromone Interaction.
Wang et al., Xi'an, China. In Chirality, Jan 2016
The inhibition of carprofen enantiomers on the UDP-glucuronosyltransferase (UGT) 2B7-catalyzed glucuronidation of hymecromone was investigated in the UGTs incubation system with and without BSA.
UDP-glucuronosyltransferase 1A1*6 and *28 polymorphisms as indicators of initial dose level of irinotecan to reduce risk of neutropenia in patients receiving FOLFIRI for colorectal cancer.
Manabe et al., Saku, Japan. In Int J Clin Oncol, Jan 2016
BACKGROUND: Irinotecan (CPT-11)-induced neutropenia is associated with UDP-glucuronosyltransferase (UGT) 1A1*6 and *28 polymorphisms.
Two Different UGT1A1 Mutations causing Crigler-Najjar Syndrome types I and II in an Iranian Family.
Salehi et al., Ōtsu, Japan. In J Gastrointestin Liver Dis, Dec 2015
Genetic analysis revealed a mutation in the bilirubin UDP-glucuronosyltransferase (UGT1A1) gene that resulted in residual enzymatic activity.
Clinical use of cobicistat as a pharmacoenhancer of human immunodeficiency virus therapy.
von Hentig, Frankfurt am Main, Germany. In Hiv Aids (auckl), Dec 2015
The outstanding property of cobicistat is its cytochrome P450 3A-selective inhibition of hepatic metabolism of antiretroviral drugs, in contrast with ritonavir, which not only inhibits but also induces a number of cytochrome P450 enzymes, UDP-glucuronosyltransferase, P-glycoprotein, and other cellular transporters.
Irinotecan, a key chemotherapeutic drug for metastatic colorectal cancer.
Sasaki et al., Tokyo, Japan. In World J Gastroenterol, Dec 2015
Clinical pharmacological studies have revealed that such severe toxicity is related to exposure to SN-38 and genetic polymorphisms in UDP-glucuronosyltransferase 1A1 gene.
Role of extrahepatic UDP-glucuronosyltransferase 1A1: Advances in understanding breast milk-induced neonatal hyperbilirubinemia.
Tukey et al., Tokyo, Japan. In Toxicol Appl Pharmacol, Dec 2015
Bilirubin undergoes selective metabolism by UDP-glucuronosyltransferase (UGT) 1A1 and becomes a water soluble glucuronide.
[UGT1A1 Genotyping for Proper Use of Irinotecan].
Ando et al., In Rinsho Byori, Jul 2015
Irinotecan is metabolized to form active SN-38, which is further conjugated and detoxified by the UDP-glucuronosyltransferase (UGT) 1A1 enzyme.
In Vitro and in Vivo Assessments of Drug-induced Hepatotoxicity and Drug Metabolism in Humans.
Sanoh, Hiroshima, Japan. In Yakugaku Zasshi, 2014
We found that drug metabolism and pharmacokinetics mediated by CYP and non-CYP enzymes, such as UDP-glucuronosyltransferase and aldehyde oxidase, in chimeric mice with humanized liver were similar to those in humans.
UGT1A4*3 encodes significantly increased glucuronidation of olanzapine in patients on maintenance treatment and in recombinant systems.
Eliasson et al., Oslo, Norway. In Clin Pharmacol Ther, 2012
Polymorphic glucuronidation of olanzapine by uridine diphosphate glucuronosyltransferase 1A4 (UGT1A4) was investigated retrospectively in patient samples
UDP-glucuronosyltransferase 1A4 (UGT1A4) polymorphisms in a Jordanian population.
Ismail et al., Amman, Jordan. In Mol Biol Rep, 2012
study to determine the allelic frequency of two most common defective alleles: UGT1A4*2 and UGT1A4*3 in a Jordanian population
Functional analysis of UGT1A4(P24T) and UGT1A4(L48V) variant enzymes.
Remmel et al., United States. In Pharmacogenomics, 2011
UGT1A4(P24T) and UGT1A4(L48V) on LTG glucuronidation may lead to interindividual variations in lamotrigine metabolism in vivo
The relationship between UGT1A4 polymorphism and serum concentration of lamotrigine in patients with epilepsy.
Onat et al., İstanbul, Turkey. In Epilepsy Res, 2011
The frequencies of the heterozygous alleles for L48V or P24T polymorphisms were 22.4% and 3.8%, respectively. L48V polymorphism was found to decrease the serum lamotrigine concentration in Turkish epilepsy patients on monotherapy or polytherapy.
Regulation of the human bile acid UDP-glucuronosyltransferase 1A3 by the farnesoid X receptor and bile acids.
Strassburg et al., Hannover, Germany. In J Hepatol, 2010
Transcriptional regulation of the human bile acid and xenobiotic UGT1A3 by its substrate CDCA and FXR is shown
UGT1A1 promoter genotype correlates with SN-38 pharmacokinetics, but not severe toxicity in patients receiving low-dose irinotecan.
McGregor et al., Memphis, United States. In J Clin Oncol, 2007
PURPOSE: To study the association between UDP-glucuronosyltransferase 1A1 (UGT1A1) genotypes and severe toxicity as well as irinotecan disposition in pediatric patients with solid tumors receiving low-dose, protracted irinotecan (15 to 75 mg/m2 daily for 5 days for 2 consecutive weeks).
Genetic variants in the UDP-glucuronosyltransferase 1A1 gene predict the risk of severe neutropenia of irinotecan.
Ratain et al., Chicago, United States. In J Clin Oncol, 2004
UDP-glucuronosyltransferase 1A1 (UGT1A1) catalyzes the glucuronidation of the active metabolite SN-38.
Predicting human drug glucuronidation parameters: application of in vitro and in silico modeling approaches.
Mackenzie et al., Adelaide, Australia. In Annu Rev Pharmacol Toxicol, 2003
Cytochrome P450 (CYP) and UDP-glucuronosyltransferase (UGT), which both exist as enzyme "superfamilies," are together responsible for the metabolism of most hepatically cleared drugs.
The genetic basis of the reduced expression of bilirubin UDP-glucuronosyltransferase 1 in Gilbert's syndrome.
Oude Elferink et al., Amsterdam, Netherlands. In N Engl J Med, 1995
METHODS: We sequenced the coding and promoter regions of the gene for bilirubin UDP-glucuronosyltransferase 1 (bilirubin/uridine diphosphoglucuronate-glucuronosyltransferase 1)--the only enzyme that contributes substantially to bilirubin glucuronidation--in 10 unrelated patients with Gilbert's syndrome, 16 members of a kindred with a history of Crigler-Najjar syndrome type II, and 55 normal subjects.
Analysis of genes for bilirubin UDP-glucuronosyltransferase in Gilbert's syndrome.
Sato et al., Japan. In Lancet, 1995
Gilbert's and Crigler-Najjar syndromes are characterised by unconjugated hyperbilirubinaemia due to complete and partial absence of bilirubin UDP-glucuronosyltransferase (UGT).
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