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Gene Review

UGT1A10  -  UDP glucuronosyltransferase 1 family,...

Homo sapiens

Synonyms: GNT1, UDP-glucuronosyltransferase 1-10, UDP-glucuronosyltransferase 1-J, UDP-glucuronosyltransferase 1A10, UDPGT, ...
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Disease relevance of UGT1A10


High impact information on UGT1A10

  • BACKGROUND & AIMS: Approximately 13% of patients with chronic hepatitis D virus (HDV) infection have liver-kidney microsomal antibodies type 3 (LKM-3) directed against family 1 uridine 5'-diphosphate-glucuronosyl-transferases (UGT-1) [6].
  • Inhibition of cellular UGT1A7 and UGT1A10 activities and of [33P]orthophosphate incorporation into immunoprecipitable proteins after exposure to curcumin or calphostin-C indicated that the isozymes are phosphorylated [7].
  • UGT1A10, a newly discovered UGT1A gene product, is expressed only in biliary and not hepatocellular tissue and is also significantly down-regulated in cholangiocellular carcinoma [8].
  • In Tg-UGT1 mice, the UGT1A proteins are differentially expressed in the liver and gastrointestinal tract [9].
  • In addition, the selective induction of glucuronidation activity toward lamotrigine, ethinyl estradiol, chenodeoxycholic acid, and lithocholic acid by either PCN or TCDD in small intestine from Tg-UGT1 mice corresponded to expression of the locus in this tissue [9].

Biological context of UGT1A10

  • In summary, our results suggest gastrointestinally distributed UGT1A10 is important for detoxifying estrogens/phytoestrogens and aromatic acids with complementary activity by UGT1A7, -1A8, -1A3, and/or -1A1 evidently dependent upon phosphorylation [10].
  • The kinetics of the troglitazone glucuronidation in the recombinant UGT1A10 and UGT1A1 exhibited an atypical pattern of substrate inhibition when the substrate concentration was over 200 micro M [11].
  • In this study, UGT1 and UGT2 gene expression was investigated in human oesophageal epithelium and squamous-cell carcinoma in addition to the characterization of individual UGT isoforms using recombinant protein [1].
  • UGT1 consists of 5 exons and has a unique gene structure [12].
  • Each isoform of UGT1 results from differential splicing of exon1s to common exon 2-5, and has an unique spectrum of substrate specificity [12].

Anatomical context of UGT1A10


Associations of UGT1A10 with chemical compounds

  • Additionally UGT1A10-expressing cultures glucuronidated 17beta-[(14)C]estradiol, whereas cultures containing null mutants at protein kinase C sites showed no estrogen conversion [10].
  • Finally UGT1A10, -1A7, -1A8, and -1A3 converted plant-based salicylic acids; methylsalicylic acid was transformed at high levels, and acetylsalicylic (aspirin) and salicylic acid were transformed at moderate to low levels [10].
  • The ability of UGT1A10 to glucuronidate estrone represents only the second example of a human estrone UGT [16].
  • The troglitazone glucuronosyltransferase activity in human jejunum microsomes was strongly inhibited by emodin (IC(50) = 15.6 micro M), a typical substrate of UGT1A8 and UGT1A10, rather than by bilirubin (IC(50) = 154.0 micro M) [11].
  • With a Michaelis-Menten equation at 6 to 200 micro M troglitazone, the K(m) value was 11.1 +/- 5.8 micro M and the V(max) value was 33.6 +/- 3.7 pmol/min/mg protein in recombinant UGT1A10 [11].

Other interactions of UGT1A10


Analytical, diagnostic and therapeutic context of UGT1A10


  1. Regulation and function of family 1 and family 2 UDP-glucuronosyltransferase genes (UGT1A, UGT2B) in human oesophagus. Strassburg, C.P., Strassburg, A., Nguyen, N., Li, Q., Manns, M.P., Tukey, R.H. Biochem. J. (1999) [Pubmed]
  2. UGT1A10 is responsible for SN-38 glucuronidation and its expression in human lung cancers. Oguri, T., Takahashi, T., Miyazaki, M., Isobe, T., Kohno, N., Mackenzie, P.I., Fujiwara, Y. Anticancer Res. (2004) [Pubmed]
  3. Molecular analysis of patients of Sardinian descent with Crigler-Najjar syndrome type I. Rosatelli, M.C., Meloni, A., Faa, V., Saba, L., Crisponi, G., Clemente, M.G., Meloni, G., Piga, M.T., Cao, A. J. Med. Genet. (1997) [Pubmed]
  4. Coinheritance of variant UDP-glucuronosyl transferase 1A1 gene and glucose-6-phosphate dehydrogenase deficiency in adults with hyperbilirubinemia. Huang, M.J., Yang, Y.C., Yang, S.S., Lin, M.S., Chen, E.S., Huang, C.S. Pharmacogenetics (2002) [Pubmed]
  5. Regulation of the human bilirubin UDP-glucuronosyltransferase gene. Brierley, C.H., Senafi, S.B., Clarke, D., Hsu, M.H., Johnson, E.F., Burchell, B. Adv. Enzyme Regul. (1996) [Pubmed]
  6. Autoantibodies against glucuronosyltransferases differ between viral hepatitis and autoimmune hepatitis. Strassburg, C.P., Obermayer-Straub, P., Alex, B., Durazzo, M., Rizzetto, M., Tukey, R.H., Manns, M.P. Gastroenterology (1996) [Pubmed]
  7. Phosphorylation of a UDP-glucuronosyltransferase regulates substrate specificity. Basu, N.K., Kovarova, M., Garza, A., Kubota, S., Saha, T., Mitra, P.S., Banerjee, R., Rivera, J., Owens, I.S. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  8. Differential down-regulation of the UDP-glucuronosyltransferase 1A locus is an early event in human liver and biliary cancer. Strassburg, C.P., Manns, M.P., Tukey, R.H. Cancer Res. (1997) [Pubmed]
  9. Tissue-specific, inducible, and hormonal control of the human UDP-glucuronosyltransferase-1 (UGT1) locus. Chen, S., Beaton, D., Nguyen, N., Senekeo-Effenberger, K., Brace-Sinnokrak, E., Argikar, U., Remmel, R.P., Trottier, J., Barbier, O., Ritter, J.K., Tukey, R.H. J. Biol. Chem. (2005) [Pubmed]
  10. Gastrointestinally distributed UDP-glucuronosyltransferase 1A10, which metabolizes estrogens and nonsteroidal anti-inflammatory drugs, depends upon phosphorylation. Basu, N.K., Kubota, S., Meselhy, M.R., Ciotti, M., Chowdhury, B., Hartori, M., Owens, I.S. J. Biol. Chem. (2004) [Pubmed]
  11. Troglitazone glucuronidation in human liver and intestine microsomes: high catalytic activity of UGT1A8 and UGT1A10. Watanabe, Y., Nakajima, M., Yokoi, T. Drug Metab. Dispos. (2002) [Pubmed]
  12. Polymorphism of UDP-glucuronosyltransferase and drug metabolism. Maruo, Y., Iwai, M., Mori, A., Sato, H., Takeuchi, Y. Curr. Drug Metab. (2005) [Pubmed]
  13. Polymorphic gene regulation and interindividual variation of UDP-glucuronosyltransferase activity in human small intestine. Strassburg, C.P., Kneip, S., Topp, J., Obermayer-Straub, P., Barut, A., Tukey, R.H., Manns, M.P. J. Biol. Chem. (2000) [Pubmed]
  14. The human UDP glucuronosyltransferase, UGT1A10, glucuronidates mycophenolic acid. Mojarrabi, B., Mackenzie, P.I. Biochem. Biophys. Res. Commun. (1997) [Pubmed]
  15. Amino acid residue ILE211 is essential for the enzymatic activity of human UDP-glucuronosyltransferase 1A10 (UGT1A10). Martineau, I., Tchernof, A., Bélanger, A. Drug Metab. Dispos. (2004) [Pubmed]
  16. Expression of the UDP-glucuronosyltransferase 1A locus in human colon. Identification and characterization of the novel extrahepatic UGT1A8. Strassburg, C.P., Manns, M.P., Tukey, R.H. J. Biol. Chem. (1998) [Pubmed]
  17. Differential expression of the UGT1A locus in human liver, biliary, and gastric tissue: identification of UGT1A7 and UGT1A10 transcripts in extrahepatic tissue. Strassburg, C.P., Oldhafer, K., Manns, M.P., Tukey, R.H. Mol. Pharmacol. (1997) [Pubmed]
  18. Evaluation of 5-hydroxytryptophol and other endogenous serotonin (5-hydroxytryptamine) analogs as substrates for UDP-glucuronosyltransferase 1A6. Krishnaswamy, S., Hao, Q., Von Moltke, L.L., Greenblatt, D.J., Court, M.H. Drug Metab. Dispos. (2004) [Pubmed]
  19. Phenylalanine 90 and 93 are localized within the phenol binding site of human UDP-glucuronosyltransferase 1A10 as determined by photoaffinity labeling, mass spectrometry, and site-directed mutagenesis. Xiong, Y., Bernardi, D., Bratton, S., Ward, M.D., Battaglia, E., Finel, M., Drake, R.R., Radominska-Pandya, A. Biochemistry (2006) [Pubmed]
  20. Studies on the substrate specificity of human intestinal UDP- lucuronosyltransferases 1A8 and 1A10. Cheng, Z., Radominska-Pandya, A., Tephly, T.R. Drug Metab. Dispos. (1999) [Pubmed]
  21. Species- and disposition model-dependent metabolism of raloxifene in gut and liver: role of UGT1A10. Jeong, E.J., Liu, Y., Lin, H., Hu, M. Drug Metab. Dispos. (2005) [Pubmed]
  22. Functional characterization of wild-type and variant (T202I and M59I) human UDP-glucuronosyltransferase 1A10. Jinno, H., Saeki, M., Tanaka-Kagawa, T., Hanioka, N., Saito, Y., Ozawa, S., Ando, M., Shirao, K., Minami, H., Ohtsu, A., Yoshida, T., Saijo, N., Sawada, J. Drug Metab. Dispos. (2003) [Pubmed]
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