Retinol oxidation to retinoic acid in human thyroid glandular cells

Gennaro Taibi, Concetta Nicotra, Giuseppe Carruba, Concetta M. A. Nicotra, Letizia Cocciadiferro, Giuseppe Carruba, Letizia Cocciadiferro, Maria Concetta Gueli

    Research output: Contribution to journalArticlepeer-review

    Abstract

    Retinoic acid is regarded as the retinol metabolite that controls proliferation and differentiationof epithelial cells. In the present study, we investigated the potential role of xanthinedehydrogenase (XDH) in retinoic acid biosynthesis in human thyroid glandular cells (HTGC).In particular, we observed that cellular retinoids binding proteins (CRBPs) are also implicatedin the biosynthetic pathway leading to retinoic acid formation in primary cultures of HTGC,as we have already reported for human mammary epithelial cells (HMEC). After partial proteinpurification, the enzyme responsible for retinoic acid biosynthesis was identified and quantifiedas XDH by immunoassay, by its ability to oxidize xanthine to uric acid and its sensitivity to theinhibitory effect of oxypurinol. The evidence of XDH-driven formation of retinoic acid in HTGCcultures further corroborates the potential role of XDH in retinoic acid biosynthesis in theepithelia.
    Original languageEnglish
    Pages (from-to)796-803
    Number of pages8
    JournalJournal of Enzyme Inhibition and Medicinal Chemistry
    Volume29
    Publication statusPublished - 2014

    All Science Journal Classification (ASJC) codes

    • Pharmacology
    • Drug Discovery

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