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Gene Review

Ugt1a8  -  UDP glycosyltransferase 1 family,...

Rattus norvegicus

Synonyms: A3, UDP-glucuronosyltransferase 1-8, UDP-glucuronosyltransferase 1A8, UDPGT 1-8, UGT1*8, ...
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Disease relevance of Ugt1a8


High impact information on Ugt1a8

  • Neither MIP nor crystallin gene appears to be transcriptionally active in the undifferentiated epithelial cell, but transcripts from the beta-A1/A3 gene appear earlier in fiber cell differentiation than do those from the gene for MIP [2].
  • A2 mRNA was found in adult neural and muscle tissues, and A3 mRNA was found only in neural tissues and fetal heart muscle [3].
  • Evidence for genomic duplication of the glutathione transferase A3 gene in genus Rattus [4].
  • A novel adenosine receptor, the A3 receptor, has recently been cloned [5].
  • Potencies of N6,5'-disubstituted compounds in inhibition of adenylate cyclase via A3 receptors parallel their high affinity in the binding assay [5].

Biological context of Ugt1a8

  • The result suggests that both the UDPGTs are derived from a common primary-transcript and that the multiple defects of UDPGT isoenzymes observed in the homozygous Gunn rat may be produced by a single-mutated-locus after an alternative splicing of the 5' end region [6].
  • Bilirubin UDPGT activity was demonstrated by transfection of the pcDL1 vector carrying the cDNA into COS7 monkey kidney cells [6].
  • The cDNA shares an identical 913-bp sequence (corresponding to the C-terminal 247 amino acid residues) with that for rat liver 3-methylcholanthrene-inducible 4-nitrophenol UDPGT including the locus where a -1 frameshift mutation was found in the 4-nitrophenol UDPGT cDNA from the jaundiced homozygous Gunn rat [6].
  • A2, A3, B3, and B4 were identified as previously uncharacterized forms, while A4 and B4 were pseudogenes [7].
  • UGT1A8 exhibited a narrower substrate specificity that completely overlapped with UGT1A7 [8].

Anatomical context of Ugt1a8

  • We have systematically investigated the hitherto largely unexplored structure-activity relationships (SARs) for binding at A3 receptors, using 125I-N6-2-(4-aminophenyl)ethyladenosine as a radioligand and membranes from Chinese hamster ovary cells stably transfected with the rat A3-cDNA [5].
  • The agonist N6-amino[125I]iodobenzyladenosine binds with high affinity (Kd congruent to 6 nm) and specificity to recombinant A3 adenosine receptors expressed transiently in COS-1 cells or stably in CHO K1 cells [9].
  • In contrast to rat, where abundant A3 mRNA transcript is found primarily in testis, the sheep transcript is most abundant in lung, spleen, and pineal gland and is present in moderate levels in brain, kidney, and testis [9].
  • Our results indicate that compared with other vascular segments and renal tissues, A1 and A2B receptor protein and mRNA are abundantly expressed in the preglomerular microcirculation, whereas A2A and A3 receptor protein and mRNA are barely detectable or undetectable in PGMVs [10].
  • To test for the presence of functional A1 and A3 receptors, the regulation of adenylyl cyclase by adenosine analogs was examined in seminiferous tubules and spermatozoa [11].

Associations of Ugt1a8 with chemical compounds


Analytical, diagnostic and therapeutic context of Ugt1a8


  1. Genetic predisposition to stroke in spontaneously hypertensive rats. Nagaoka, A., Iwatsuka, H., Suzuoki, Z., Okamoto, K. Am. J. Physiol. (1976) [Pubmed]
  2. Expression of the gene for main intrinsic polypeptide (MIP): separate spatial distributions of MIP and beta-crystallin gene transcripts in rat lens development. Yancey, S.B., Koh, K., Chung, J., Revel, J.P. J. Cell Biol. (1988) [Pubmed]
  3. Tissue specificity, localization in brain, and cell-free translation of mRNA encoding the A3 isoform of Na+,K+-ATPase. Schneider, J.W., Mercer, R.W., Gilmore-Hebert, M., Utset, M.F., Lai, C., Greene, A., Benz, E.J. Proc. Natl. Acad. Sci. U.S.A. (1988) [Pubmed]
  4. Evidence for genomic duplication of the glutathione transferase A3 gene in genus Rattus. Fotouhi-Ardakani, N., Schecter, R.L., Batist, G. Mol. Biol. Evol. (2000) [Pubmed]
  5. A binding site model and structure-activity relationships for the rat A3 adenosine receptor. van Galen, P.J., van Bergen, A.H., Gallo-Rodriguez, C., Melman, N., Olah, M.E., IJzerman, A.P., Stiles, G.L., Jacobson, K.A. Mol. Pharmacol. (1994) [Pubmed]
  6. Isolation and sequencing of rat liver bilirubin UDP-glucuronosyltransferase cDNA: possible alternate splicing of a common primary transcript. Sato, H., Koiwai, O., Tanabe, K., Kashiwamata, S. Biochem. Biophys. Res. Commun. (1990) [Pubmed]
  7. Drug-responsive and tissue-specific alternative expression of multiple first exons in rat UDP-glucuronosyltransferase family 1 (UGT1) gene complex. Emi, Y., Ikushiro, S., Iyanagi, T. J. Biochem. (1995) [Pubmed]
  8. Analysis of substrate specificities and tissue expression of rat UDP-glucuronosyltransferases UGT1A7 and UGT1A8. Webb, L.J., Miles, K.K., Auyeung, D.J., Kessler, F.K., Ritter, J.K. Drug Metab. Dispos. (2005) [Pubmed]
  9. Molecular cloning and functional expression of a sheep A3 adenosine receptor with widespread tissue distribution. Linden, J., Taylor, H.E., Robeva, A.S., Tucker, A.L., Stehle, J.H., Rivkees, S.A., Fink, J.S., Reppert, S.M. Mol. Pharmacol. (1993) [Pubmed]
  10. Expression of adenosine receptors in the preglomerular microcirculation. Jackson, E.K., Zhu, C., Tofovic, S.P. Am. J. Physiol. Renal Physiol. (2002) [Pubmed]
  11. Localization and characterization of adenosine receptor expression in rat testis. Rivkees, S.A. Endocrinology (1994) [Pubmed]
  12. Gene expression of adenosine receptors along the nephron. Vitzthum, H., Weiss, B., Bachleitner, W., Krämer, B.K., Kurtz, A. Kidney Int. (2004) [Pubmed]
  13. Induction of UDP-glucuronosyltransferase 1A8 mRNA by 3-methylcholanthene in rat hepatoma cells. Leung, Y.K., Ho, J.W. Biochem. Pharmacol. (2002) [Pubmed]
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