cDNA cloning and characterization of the human UDP glucuronosyltransferase, UGT1A3

Biochem Biophys Res Commun. 1996 Aug 23;225(3):785-90. doi: 10.1006/bbrc.1996.1251.

Abstract

The cDNA encoding the UDP glucuronosyltransferase, UGT1A3, has been cloned and expressed in cell culture. The deduced amino acid sequence of the cDNA is 90% similar in sequence to that of a previously characterized form, UGT1A4 and to that of a third form, UGT1A5 whose function in unknown. UGT1A3, when expressed in COS cells has a relative molecular mass of 55 kDa and is active in the glucuronidation of estrone and 2-hydroxyestrone. Activity towards other polyhydroxylated estrogens including 4-hydroxyestrogen and estriol and its metabolites was not detected. UGT1A3 was also inactive towards androgens and their metabolites. The enzyme preferentially glucuronidated the N-hydroxy metabolite of 2-acetylaminofluorence and was more active towards the 6- and 12-hydroxylated metabolites of benzo[alpha]pyrene. RNA encoding UGT1A3 was detected in human liver and colon tissue.

MeSH terms

  • Animals
  • Base Sequence
  • Cell Line
  • Cloning, Molecular
  • Colon / metabolism
  • DNA Primers / genetics
  • DNA, Complementary / genetics*
  • DNA, Complementary / isolation & purification
  • Gene Expression
  • Glucuronosyltransferase / genetics*
  • Humans
  • Liver / metabolism
  • Molecular Sequence Data
  • RNA, Messenger / genetics
  • RNA, Messenger / metabolism
  • Transfection

Substances

  • DNA Primers
  • DNA, Complementary
  • RNA, Messenger
  • Glucuronosyltransferase