Steroid UDP glucuronosyltransferases

Peter I. Mackenzie, Louise Rodbourne, Steven Stranks

    Research output: Contribution to journalArticlepeer-review

    44 Citations (Scopus)


    The glucuronidation of steroids is a major process necessary for their elimination in the bile and urine. In general, steroid glucuronides are biologically less reactive than their parent steroids. However, in some cases often associated with disease and steroid therapy, more reactive or toxic glucuronides may be formed. The concentrations of specific steroid glucuronides in the blood may also indicate hormonal imbalances and may funnction as diagnostic markers of genetic defects in steroid synthesis and metabolism. In this review, the forms of UDP glucuronosyltransferase involved in steroid glucuronidation are described in terms of their specificities, functional domains and regulation. The available evidence suggests that steroid glucuronidation is mainly carried out by members of the UGT2B subfamily which are encoded by genes containing 6 exons. Members of this subfamily exhibit a regioselectively in their glucuronidation of steroids that is mediated by domains in the amino-terminal half on the protein encoded by exons 1 and 2. Although much of this review will describe studies in the rat, preliminary evidence indicates that a similar situation may exist in humans.

    Original languageEnglish
    Pages (from-to)1099-1105
    Number of pages7
    JournalJournal of Steroid Biochemistry and Molecular Biology
    Issue number8
    Publication statusPublished - Dec 1992


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