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UGT2B@  -  UDP glucuronosyltransferase 2 family,...

Homo sapiens

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High impact information on UGT2B@

  • Thus, tissue-specific and interindividual polymorphic regulation of UGT1A and UGT2B genes in small intestine is identified and implicated as molecular biological determinant contributing to interindividual prehepatic drug and xenobiotic metabolism in humans [1].
  • To isolate cDNA clones encoding novel UGT2B enzymes, human prostate and LNCaP cell cDNA libraries were screened using a pool of steroid-specific UGT2B cDNA probes [2].
  • The tissue distribution and cellular localization of the UGT2B transcripts and proteins in humans clearly indicate that these enzymes are synthesized in androgen-sensitive tissues [3].
  • To determine whether this putative Pbx site contributes to the regulation of UGT2B expression, we chose the UGT2B17 gene and investigated the capacity of its Pbx site to bind specific transcription factors and alter promoter activity [4].
  • In some of these UGT2B genes, a putative pre-B cell homeobox (Pbx) transcription factor binding site is found directly adjacent to the functional HNF1 site [4].

Biological context of UGT2B@


Anatomical context of UGT2B@


Associations of UGT2B@ with chemical compounds

  • In summary, our data showed that several members of UGT1A and UGT2B families are capable of converting LA and AA metabolites into glucuronide derivatives, which is considered an irreversible step to inactivation and elimination of endogenous substances from the body [12].
  • Treatment of stable cells with actinomycin D reveals that UGT2B transcripts are stable for 12 h, except for the UGT2B4 transcript, which was decreased by 50% after the 12-h incubation period [8].
  • Cycloheximide treatment of stably transfected HK293 cells demonstrated that the UGT2B17 protein is more labile than the other enzymes; the protein levels decrease after 1 h of treatment, whereas other UGT2B proteins were stable for at least 12 h [8].
  • The findings of this study clearly show that UGT2B specifically utilizes UDP-glucose but not UDP-glucuronic acid as a sugar donor for the conjugation of AS-3201 in human liver microsomes [9].
  • Measurement of aldosterone glucuronidation and normalization with the UGT2B protein contents in monkey tissues demonstrate that liver and kidney glucuronidate this hormone with a similar velocity [11].

Other interactions of UGT2B@

  • Localization of a bile acid UDP-glucuronosyltransferase gene (UGT2B) to chromosome 4 using the polymerase chain reaction [13].
  • UGT2B7 was the only product of the UGT2 gene family examined and it metabolized all the aromatic amines at similar low relative levels compared with a preferred substrate, 4-OH-estrone [14].
  • The deduced amino acid sequences of UGTs 2B10 and 2B11 share > 76% sequence similarity with other known human liver UGT2B subfamily isoforms and < 48% sequence similarity with UGT1 family proteins [15].
  • Treatment with both DHT (0.5 nM) and EGF (10 ng/ml) caused a greater decrease of DHT glucuronidation and UGT2B messenger RNA levels than when the cells were treated with either compound alone [16].
  • The gastrointestinal tract, contains several UDP-glucuronosyltransferases (UGTs) of the UGT1A and UGT2B subfamilies [17].

Analytical, diagnostic and therapeutic context of UGT2B@


  1. 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]
  2. Isolation and characterization of a novel cDNA encoding a human UDP-glucuronosyltransferase active on C19 steroids. Beaulieu, M., Lévesque, E., Hum, D.W., Bélanger, A. J. Biol. Chem. (1996) [Pubmed]
  3. Inactivation of androgens by UDP-glucuronosyltransferase enzymes in humans. Bélanger, A., Pelletier, G., Labrie, F., Barbier, O., Chouinard, S. Trends Endocrinol. Metab. (2003) [Pubmed]
  4. The homeodomain Pbx2-Prep1 complex modulates hepatocyte nuclear factor 1alpha-mediated activation of the UDP-glucuronosyltransferase 2B17 gene. Gregory, P.A., Mackenzie, P.I. Mol. Pharmacol. (2002) [Pubmed]
  5. Isolation of a human YAC contig encompassing a cluster of UGT2 genes and its regional localization to chromosome 4q13. Monaghan, G., Clarke, D.J., Povey, S., See, C.G., Boxer, M., Burchell, B. Genomics (1994) [Pubmed]
  6. Characterization and substrate specificity of UGT2B4 (E458): a UDP-glucuronosyltransferase encoded by a polymorphic gene. Lévesque, E., Beaulieu, M., Hum, D.W., Bélanger, A. Pharmacogenetics (1999) [Pubmed]
  7. Genomic organization of the UGT2b gene cluster on human chromosome 4q13. Riedy, M., Wang, J.Y., Miller, A.P., Buckler, A., Hall, J., Guida, M. Pharmacogenetics (2000) [Pubmed]
  8. Relative enzymatic activity, protein stability, and tissue distribution of human steroid-metabolizing UGT2B subfamily members. Turgeon, D., Carrier, J.S., Lévesque, E., Hum, D.W., Bélanger, A. Endocrinology (2001) [Pubmed]
  9. Uridine diphosphate sugar-selective conjugation of an aldose reductase inhibitor (AS-3201) by UDP-glucuronosyltransferase 2B subfamily in human liver microsomes. Toide, K., Terauchi, Y., Fujii, T., Yamazaki, H., Kamataki, T. Biochem. Pharmacol. (2004) [Pubmed]
  10. Glucuronidation of estrogens and retinoic acid and expression of UDP-glucuronosyltransferase 2B7 in human intestinal mucosa. Czernik, P.J., Little, J.M., Barone, G.W., Raufman, J.P., Radominska-Pandya, A. Drug Metab. Dispos. (2000) [Pubmed]
  11. Human uridine diphosphate-glucuronosyltransferase UGT2B7 conjugates mineralocorticoid and glucocorticoid metabolites. Girard, C., Barbier, O., Veilleux, G., El-Alfy, M., Bélanger, A. Endocrinology (2003) [Pubmed]
  12. Glucuronidation of arachidonic and linoleic acid metabolites by human UDP-glucuronosyltransferases. Turgeon, D., Chouinard, S., Belanger, P., Picard, S., Labbe, J.F., Borgeat, P., Belanger, A. J. Lipid Res. (2003) [Pubmed]
  13. Localization of a bile acid UDP-glucuronosyltransferase gene (UGT2B) to chromosome 4 using the polymerase chain reaction. Monaghan, G., Povey, S., Burchell, B., Boxer, M. Genomics (1992) [Pubmed]
  14. Glucuronidation of benzidine and its metabolites by cDNA-expressed human UDP-glucuronosyltransferases and pH stability of glucuronides. Ciotti, M., Lakshmi, V.M., Basu, N., Davis, B.B., Owens, I.S., Zenser, T.V. Carcinogenesis (1999) [Pubmed]
  15. 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]
  16. Differential regulation of two uridine diphospho-glucuronosyltransferases, UGT2B15 and UGT2B17, in human prostate LNCaP cells. Guillemette, C., Lévesque, E., Beaulieu, M., Turgeon, D., Hum, D.W., Bélanger, A. Endocrinology (1997) [Pubmed]
  17. The caudal-related homeodomain protein Cdx2 and hepatocyte nuclear factor 1alpha cooperatively regulate the UDP-glucuronosyltransferase 2B7 gene promoter. Gregory, P.A., Gardner-Stephen, D.A., Rogers, A., Michael, M.Z., Mackenzie, P.I. Pharmacogenet. Genomics (2006) [Pubmed]
  18. Isolation and characterization of a simian UDP-glucuronosyltransferase UGT2B18 active on 3-hydroxyandrogens. Beaulieu, M., Lévesque, E., Barbier, O., Turgeon, D., Bélanger, G., Hum, D.W., Bélanger, A. J. Mol. Biol. (1998) [Pubmed]
  19. UDP-glucuronosyltransferase activity, expression and cellular localization in human placenta at term. Collier, A.C., Ganley, N.A., Tingle, M.D., Blumenstein, M., Marvin, K.W., Paxton, J.W., Mitchell, M.D., Keelan, J.A. Biochem. Pharmacol. (2002) [Pubmed]
  20. Cellular localization of uridine diphosphoglucuronosyltransferase 2B enzymes in the human prostate by in situ hybridization and immunohistochemistry. Barbier, O., Lapointe, H., El Alfy, M., Hum, D.W., Bélanger, A. J. Clin. Endocrinol. Metab. (2000) [Pubmed]
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