Retinol oxidation to retinoic acid in human thyroid glandular cells

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

Risultato della ricerca: Article

Abstract

Retinoic acid is regarded as the retinol metabolite that controls proliferation and differentiation of epithelial cells. In the present study, we investigated the potential role of xanthine dehydrogenase (XDH) in retinoic acid biosynthesis in human thyroid glandular cells (HTGC). In particular, we observed that cellular retinoids binding proteins (CRBPs) are also implicated in 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 protein purification, the enzyme responsible for retinoic acid biosynthesis was identified and quantified as XDH by immunoassay, by its ability to oxidize xanthine to uric acid and its sensitivity to the inhibitory effect of oxypurinol. The evidence of XDH-driven formation of retinoic acid in HTGC cultures further corroborates the potential role of XDH in retinoic acid biosynthesis in the epithelia.
Lingua originaleEnglish
pagine (da-a)796-803
Numero di pagine8
RivistaJournal of Enzyme Inhibition and Medicinal Chemistry
Volume29
Stato di pubblicazionePublished - 2014

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Tretinoin
Vitamin A
Thyroid Gland
Oxypurinol
Epithelial Cells
Retinol-Binding Proteins
Xanthine
Biosynthetic Pathways
Uric Acid
Immunoassay
Breast
Enzymes

All Science Journal Classification (ASJC) codes

  • Drug Discovery
  • Medicine(all)
  • Pharmacology

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title = "Retinol oxidation to retinoic acid in human thyroid glandular cells",
abstract = "Retinoic acid is regarded as the retinol metabolite that controls proliferation and differentiation of epithelial cells. In the present study, we investigated the potential role of xanthine dehydrogenase (XDH) in retinoic acid biosynthesis in human thyroid glandular cells (HTGC). In particular, we observed that cellular retinoids binding proteins (CRBPs) are also implicated in 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 protein purification, the enzyme responsible for retinoic acid biosynthesis was identified and quantified as XDH by immunoassay, by its ability to oxidize xanthine to uric acid and its sensitivity to the inhibitory effect of oxypurinol. The evidence of XDH-driven formation of retinoic acid in HTGC cultures further corroborates the potential role of XDH in retinoic acid biosynthesis in the epithelia.",
author = "Gueli, {Maria Concetta} and Concetta Nicotra and Gennaro Taibi and Letizia Cocciadiferro and Giuseppe Carruba and Nicotra, {Concetta M. A.} and Letizia Cocciadiferro and Giuseppe Carruba",
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TY - JOUR

T1 - Retinol oxidation to retinoic acid in human thyroid glandular cells

AU - Gueli, Maria Concetta

AU - Nicotra, Concetta

AU - Taibi, Gennaro

AU - Cocciadiferro, Letizia

AU - Carruba, Giuseppe

AU - Nicotra, Concetta M. A.

AU - Cocciadiferro, Letizia

AU - Carruba, Giuseppe

PY - 2014

Y1 - 2014

N2 - Retinoic acid is regarded as the retinol metabolite that controls proliferation and differentiation of epithelial cells. In the present study, we investigated the potential role of xanthine dehydrogenase (XDH) in retinoic acid biosynthesis in human thyroid glandular cells (HTGC). In particular, we observed that cellular retinoids binding proteins (CRBPs) are also implicated in 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 protein purification, the enzyme responsible for retinoic acid biosynthesis was identified and quantified as XDH by immunoassay, by its ability to oxidize xanthine to uric acid and its sensitivity to the inhibitory effect of oxypurinol. The evidence of XDH-driven formation of retinoic acid in HTGC cultures further corroborates the potential role of XDH in retinoic acid biosynthesis in the epithelia.

AB - Retinoic acid is regarded as the retinol metabolite that controls proliferation and differentiation of epithelial cells. In the present study, we investigated the potential role of xanthine dehydrogenase (XDH) in retinoic acid biosynthesis in human thyroid glandular cells (HTGC). In particular, we observed that cellular retinoids binding proteins (CRBPs) are also implicated in 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 protein purification, the enzyme responsible for retinoic acid biosynthesis was identified and quantified as XDH by immunoassay, by its ability to oxidize xanthine to uric acid and its sensitivity to the inhibitory effect of oxypurinol. The evidence of XDH-driven formation of retinoic acid in HTGC cultures further corroborates the potential role of XDH in retinoic acid biosynthesis in the epithelia.

UR - http://hdl.handle.net/10447/104434

M3 - Article

VL - 29

SP - 796

EP - 803

JO - Journal of Enzyme Inhibition and Medicinal Chemistry

JF - Journal of Enzyme Inhibition and Medicinal Chemistry

SN - 1475-6366

ER -