| Name | UGT1A1 |
|---|---|
| Synonyms | Bilirubin specific UDPGT isozyme 1; UGT 1; UGT1; GNT1; HUG BR1; Phenol/billirubinUDP glucuronosyltransferase 1; UDP glycosyltransferase 1 family polypeptide A1; UDP glucuronosyl transferase 1A1… |
| Name | 1-naphthol |
|---|---|
| CAS | 1-naphthalenol |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 12051676 | Dean B, Chang S, Stevens J, Thomas PE, King C: Isolation and characterization of a UDP-glucuronosyltransferase (UGT1A01) cloned from female rhesus monkey. Arch Biochem Biophys. 2002 Jun 15;402(2):289-95. Catalytic activity of UGT1A01 was determined with 7--4-(trifluoromethyl)- and more specific human UGT1A1 substrates (1-naphthol, 17 alpha-ethinylestradiol, and |
83(1,1,1,3) | Details |
| 20145913 | Donato MT, Montero S, Castell JV, Gomez-Lechon MJ, Lahoz A: Validated assay for studying activity profiles of human liver UGTs after drug exposure: inhibition and induction studies. Anal Bioanal Chem. 2010 Mar;396(6):2251-63. Epub 2010 Feb 10. The assays are based on analysis and quantification by high-performance liquid chromatography-tandem mass spectrometry of glucuronides formed from selective probe substrates, namely, (UGT1A1, 3- 1-naphthol (UGT1A6), propofol (UGT1A9), and naloxone (UGT2B7). |
83(1,1,1,3) | Details |
| 17998297 | Fujiwara R, Nakajima M, Yamanaka H, Katoh M, Yokoi T: Product inhibition of UDP-glucuronosyltransferase (UGT) enzymes by UDP obfuscates the inhibitory effects of UGT substrates. Drug Metab Dispos. 2008 Feb;36(2):361-7. Epub 2007 Nov 12. In the present study, we found that UGT1A1-catalyzed 3-O- formation and UGT1A4-catalyzed N- formation in human liver microsomes were prominently decreased in the presence of 1-naphthol, but those by recombinant human UGT1A1 and UGT1A4, respectively, were not. |
70(0,2,3,5) | Details |
| 19487247 | Kerdpin O, Mackenzie PI, Bowalgaha K, Finel M, Miners JO: Influence of N-terminal domain and residues on the substrate selectivities of human UDP-glucuronosyltransferase 1A1, 1A6, 1A9, 2B7, and 2B10. Drug Metab Dispos. 2009 Sep;37(9):1948-55. Epub 2009 Jun 1. The conserved N-terminal domain of UGT1A1, UGT1A6, UGT1A9, and UGT2B7 was mutated to and 34 of UGT2B10 was substituted with and the capacity of the wild-type and mutant proteins to glucuronidate 4MU, 1NP, LTG, TFP, and was characterized. |
4(0,0,0,4) | Details |
| 18004206 | Udomuksorn W, Elliot DJ, Lewis BC, Mackenzie PI, Yoovathaworn K, Miners JO: Influence of mutations associated with Gilbert and Crigler-Najjar type II syndromes on the glucuronidation kinetics of and other UDP-glucuronosyltransferase 1A substrates. Pharmacogenet Genomics. 2007 Dec;17(12):1017-29. OBJECTIVES: UGT1A1 coding region mutations, including UGT1A1*6 (G71R), UGT1A1*7 (Y486D), UGT1A1*27 (P229Q) and UGT1A1*62 (F83L), have been linked to Gilbert syndrome in Asian populations, whereas homozygosity for UGT1A1*7 is associated with the Crigler-Najjar syndrome type II. |
4(0,0,0,4) | Details |
| 17301691 | Kurkela M, Patana AS, Mackenzie PI, Court MH, Tate CG, Hirvonen J, Goldman A, Finel M: Interactions with other human UDP-glucuronosyltransferases attenuate the consequences of the Y485D mutation on the activity and substrate affinity of UGT1A6. Pharmacogenet Genomics. 2007 Feb;17(2):115-26. Using 1-naphthol as the aglycone substrate, the Km of 6YD for the cosubstrate UDP- was about 50 times higher than in UGT1A6. OBJECTIVES: To explore the possible role of hetero-oligomerization among the human UDP-glucuronosyltransferases in attenuating the consequences of the pathological Y486D mutation (UGT1A1 numbering) that often causes hyperbilirubinaemia. |
3(0,0,0,3) | Details |
| 16819192 | Naganuma M, Saruwatari A, Okamura S, Tamura H: and modulate the conjugation of 1-naphthol in Caco-2 cells. Biol Pharm Bull. 2006 Jul;29(7):1476-9. Moreover, and in contrast to the moderate inhibition of UGT activity by and both induce the expression of the UGT1A1 and UGT1A6 genes, revealed by real-time PCR analysis. |
1(0,0,0,1) | Details |
| 17618724 | Lee CH, Ito Y, Yanagiba Y, Yamanoshita O, Kim H, Zhang SY, Kamijima M, Gonzalez FJ, Nakajima T: Pyrene-induced CYP1A2 and SULT1A1 may be regulated by CAR and not by AhR. . Toxicology. 2007 Sep 5;238(2-3):147-56. Epub 2007 Jun 2. In contrast, pyrene exposure increased expression of the UGT1A1 and 1A6, and glucuronidation activities associated with 1-hydroxypyrene and 1-naphthol in the liver only in AhR (-/-) mice, although pyrene treatment dose-dependently decreased the latter activity. |
1(0,0,0,1) | Details |
| 12153725 | Yokota H, Kunimasa Y, Shimoyama Y, Kobayashi T, Matsumoto J, Yuasa A: Effects on extrahepatic UDP-glucuronosyltransferases in hypophysectomized rat. J Biochem. 2002 Aug;132(2):265-70. UDP-glucuronosyltransferase activities toward 1-naphthol decreased to 20-30% of control in the liver, kidney, lung, and testis. The mRNA of UGT1A1, which is an isoform contributing to the glucuronidation of increased significantly in the liver and slightly in the kidney after hypophysectomy. |
1(0,0,0,1) | Details |
| 15980103 | Tochigi Y, Yamashiki N, Ohgiya S, Ganaha S, Yokota H: Isoform-specific expression and induction of udp-glucuronosyltransferase in immunoactivated peritoneal macrophages of the rat. Drug Metab Dispos. 2005 Sep;33(9):1391-8. Epub 2005 Jun 24. Expressions of UGT1A1, 1A6, and 1A7 were observed in macrophages by immunohistochemical staining and reverse transcriptase-polymerase chain reaction. When macrophage cells cultured in plates were exposed to 1-naphthol and 3-hydroxybenzo-[a] pyrene (3-OH-B [a] P), these glucuronides increased in the medium, indicating that macrophages glucuronidated the chemicals. |
1(0,0,0,1) | Details |
| 15684482 | Okamura S, Suzuki K, Yanase M, Koizumi M, Tamura HO: The effects of coffee on conjugation reactions in human colon carcinoma cells. Biol Pharm Bull. 2005 Feb;28(2):271-4. After supplementing Caco-2 cultures with both 1-naphthol (200 microM) and various concentrations of coffee, the accumulation of 1-naphthyl and in the growth medium was determined by analytical HPLC over a 24-h period. |
0(0,0,0,0) | Details |
| 12814968 | Chen C, Staudinger JL, Klaassen CD: Nuclear receptor, pregname X receptor, is required for induction of UDP-glucuronosyltranferases in mouse liver by -16 alpha-carbonitrile. Drug Metab Dispos. 2003 Jul;31(7):908-15. In wild-type mice, PCN treatment significantly increased UGT activities toward 1-naphthol, chloramphenicol, and |
0(0,0,0,0) | Details |