cDNA cloning and characterization of the human UDP glucuronosyltransferase, UGT1A3

B. Mojarrabi, R. Butler, P. I. Mackenzie

Research output: Contribution to journalArticle

101 Citations (Scopus)

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-acetylaminofluorene and was more active towards the 6- and 12-hydroxylated metabolites of benzo[α]pyrene. RNA encoding UGT1A3 was detected in human liver and colon tissue.

Original languageEnglish
Pages (from-to)785-790
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume225
Issue number3
DOIs
Publication statusPublished - 23 Aug 1996
Externally publishedYes

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