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Gene Review

UGT2B10  -  UDP glucuronosyltransferase 2 family,...

Homo sapiens

Synonyms: UDP-glucuronosyltransferase 2B10, UDPGT 2B10
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Disease relevance of UGT2B10

  • In liver microsomes from four patients (A, B, C, and D) with Crigler-Najjar syndrome type I (CN type I), UDPGT activity towards bilirubin was undetectable (A, B, C, and D) and activity towards phenolic compounds and 5-hydroxytryptamine either reduced (A and B) or normal (C and D) [1].
  • Concurrent with this decrease in T4 was an increase in TSH levels, an increase in thyroid and liver weights, a three- to sixfold increase in hepatic T4-uridine diphosphate glucuronosyl transferase (UDPGT) activity, and increases in thyroid follicular cell hypertrophy and hyperplasia [2].

High impact information on UGT2B10

  • These findings suggest considerable heterogeneity with regard to the expression of UDPGT isoenzymes among CN type I patients [1].
  • Biochanin A significantly decreased the testosterone-stimulated release of PSA, presumably because biochanin A increased UDPGT and increased the intracellular glucuronidation of testosterone [3].
  • The steroid form of the UDPGT transcript was expressed in LNCaP cells and was enhanced in biochanin A-treated LNCaP cells [3].
  • EGF treatment resulted in a decreased UGT2B17 expression, whereas UGT2B10 and -B11 mRNA remained at their basal levels [4].
  • The significance of a possible induction of UDPGT in human foetal liver cells by HgCl2 is discussed [5].

Chemical compound and disease context of UGT2B10

  • Crigler-Najjar syndrome type 1 (CN type 1) is an autosomal recessive disorder characterized by nonhemolytic jaundice resulting from mutations to the gene encoding bilirubin-UDP-glucuronosyltransferase (UDPGT) [6].

Biological context of UGT2B10

  • Two new UDP-glucuronosyltransferase cDNAs, designated UGT2B10 and UGT2B11, encoding 528 amino acid proteins were isolated from a human liver cDNA library [7].
  • The glucuronidation of 3'-azido-3'-deoxythymidine (AZT) by human liver microsomes and human hepatocytes in culture has been studied in vitro to determine the UDP-glucuronosyltransferase (UDPGT) form conceivably involved in the AZT biotransformation process [8].
  • The differential expression of UDPGT in the four tissues clearly demonstrated for the first time that multiple isoforms with differing substrate specificities were present in fish [9].
  • In comparison with the amino acid sequences of seven species of glucosyltransferases and six species of galactosyltransferases, glutamine and histidine are highly conserved as the last amino acid residue of a glycosyltransferase-specific conserved region (UDPGT) in glucosyltransferases and galactosyltransferases, respectively [10].
  • In embryonic and early fetal development of the metanephric kidney, UDPGT is located primarily in derivatives of the ureteric bud such as the ureter, pelvis, calyces and collecting ducts [11].

Anatomical context of UGT2B10

  • Increased thyroid T4 elimination, primarily via increased hepatic conjugation by T4-UDPGT, resulting in decreased serum T4, appeared to be responsible for the increased TSH levels [2].
  • The results indicate that the 55-kDa polypeptide was the major polyaromatic hydrocarbon-inducible UDPGT isoenzyme in hepatic and renal microsomes [9].

Associations of UGT2B10 with chemical compounds

  • Among these UGTs, UGT2B7 is specific for estriol and 3,4-catechol estrogens, UGT2B15 glucuronidates 17beta-hydroxy-C19 steroids while UGT2B10 has as yet an undescribed activity [12].
  • Using a cell-free assay with testosterone as substrate, we showed that LNCaP had UDP-glucuronosyltransferase (UDPGT) activity [3].
  • Kinetic studies of the glucuronidation reaction with harmol and 1-naphthol showed that Hg2+ ions seemed to induce the expression of a high-affinity form of UDPGT, which was absent from the normal controls [5].
  • The dramatic increase in specific activity in UDPGT was accompanied by a parallel increase in Vmax. measured with harmol and UDP-glucuronic acid [5].
  • The enzymatic glucuronidation of 3'-azido-3'-deoxythymidine (AZT) catalyzed by human liver microsomal UDP-glucuronosyltransferase (EC, UDPGT) was inhibited by a number of nucleoside analogs [13].

Analytical, diagnostic and therapeutic context of UGT2B10

  • To investigate this possibility directly, UDPGT was extracted from human liver and kidney tissue and its activity was characterized using MPA as a substrate in vitro, assessing the conversion of MPA to MPAG using analysis by high-performance liquid chromatography [14].
  • With further UDPGT purification (approximately 200-fold) from kidney extracts using a combination of ammonium sulfate precipitation, followed by anion exchange, hydroxyapatite, and size exclusion chromatography, the enzyme was more than 80% pure when assessed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis [14].


  1. Immunochemical analysis of uridine diphosphate-glucuronosyltransferase in four patients with the Crigler-Najjar syndrome type I. van Es, H.H., Goldhoorn, B.G., Paul-Abrahamse, M., Elferink, R.P., Jansen, P.L. J. Clin. Invest. (1990) [Pubmed]
  2. Mechanism of thiazopyr-induced effects on thyroid hormone homeostasis in male Sprague-Dawley rats. Hotz, K.J., Wilson, A.G., Thake, D.C., Roloff, M.V., Capen, C.C., Kronenberg, J.M., Brewster, D.W. Toxicol. Appl. Pharmacol. (1997) [Pubmed]
  3. Increased UDP-glucuronosyltransferase activity and decreased prostate specific antigen production by biochanin A in prostate cancer cells. Sun, X.Y., Plouzek, C.A., Henry, J.P., Wang, T.T., Phang, J.M. Cancer Res. (1998) [Pubmed]
  4. Isoform-Specific Regulation of Uridine Diphosphate-Glucuronosyltransferase 2B Enzymes in the Human Prostate: Differential Consequences for Androgen and Bioactive Lipid Inactivation. Chouinard, S., Pelletier, G., B??langer, A., Barbier, O. Endocrinology (2006) [Pubmed]
  5. Expression of a high-affinity form of UDP-glucuronosyltransferase in human foetal liver cells in culture on exposure to mercuric chloride. Tan, T.M., Wong, K.P., Sit, K.H. Biochem. J. (1991) [Pubmed]
  6. Gene therapy with bilirubin-UDP-glucuronosyltransferase in the Gunn rat model of Crigler-Najjar syndrome type 1. Li, Q., Murphree, S.S., Willer, S.S., Bolli, R., French, B.A. Hum. Gene Ther. (1998) [Pubmed]
  7. cDNA cloning and expression of two new members of the human liver UDP-glucuronosyltransferase 2B subfamily. Jin, C.J., Miners, J.O., Lillywhite, K.J., Mackenzie, P.I. Biochem. Biophys. Res. Commun. (1993) [Pubmed]
  8. In vitro glucuronidation of 3'-azido-3'-deoxythymidine by human liver. Role of UDP-glucuronosyltransferase 2 form. Rajaonarison, J.F., Lacarelle, B., De Sousa, G., Catalin, J., Rahmani, R. Drug Metab. Dispos. (1991) [Pubmed]
  9. Differential expression and induction of UDP-glucuronosyltransferase isoforms in hepatic and extrahepatic tissues of a fish, Pleuronectes platessa: immunochemical and functional characterization. Clarke, D.J., Burchell, B., George, S.G. Toxicol. Appl. Pharmacol. (1992) [Pubmed]
  10. Alteration of sugar donor specificities of plant glycosyltransferases by a single point mutation. Kubo, A., Arai, Y., Nagashima, S., Yoshikawa, T. Arch. Biochem. Biophys. (2004) [Pubmed]
  11. Differential localisation of UDP-glucuronosyltransferase in kidney during human embryonic and fetal development. Hume, R., Coughtrie, M.W., Burchell, B. Arch. Toxicol. (1995) [Pubmed]
  12. Expression of transcripts encoding steroid UDP-glucuronosyltransferases in human prostate hyperplastic tissue and the LNCaP cell line. Bélanger, G., Beaulieu, M., Marcotte, B., Lévesque, E., Guillemette, C., Hum, D.W., Bélanger, A. Mol. Cell. Endocrinol. (1995) [Pubmed]
  13. Glucuronidation of 3'-azido-3'-deoxythymidine catalyzed by human liver UDP-glucuronosyltransferase. Significance of nucleoside hydrophobicity and inhibition by xenobiotics. Resetar, A., Minick, D., Spector, T. Biochem. Pharmacol. (1991) [Pubmed]
  14. Evidence that tacrolimus augments the bioavailability of mycophenolate mofetil through the inhibition of mycophenolic acid glucuronidation. Zucker, K., Tsaroucha, A., Olson, L., Esquenazi, V., Tzakis, A., Miller, J. Therapeutic drug monitoring. (1999) [Pubmed]
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