| Literature DB >> 8829220 |
A Many1, A Westerhausen-Larson, A Kanbour-Shakir, J M Roberts.
Abstract
Xanthine dehydrogenase/oxidase (XDH, EC 1.1.1.204, XO, EC 1.2.3.2) produces uric acid, and in the oxidase form also generates the free radical superoxide. Previous reports failed to demonstrate XDH/XO activity in human placenta. Our objective was to determine evidence of XDH/XO in human placenta. We developed a cDNA probe for human XDH/XO and used it to detect mRNA by Northern hybridization. Immunohistochemical localization of the enzyme in placental tissue was performed using a specific antibody for XDH/XO and ABC-peroxidase. Enzyme activity assay was determined by the conversion of [14C] xanthine to [14C] uric acid. mRNA was detected in all placental samples (n = 4). Villous and non-villous trophoblast cells expressed immunohistochemical staining for XOD (n = 4). Enzyme activity was detected in all placentae (n = 6). Despite previous reports, we found mRNA, XDH/XO protein and enzyme activity in human placenta localized to trophoblast cells. Enzyme activity was much lower than in liver. Several conditions in the maternal-fetal unit could potentially increase XDH/XO activity and conversion of the enzyme to its oxidase form.Entities:
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Year: 1996 PMID: 8829220 DOI: 10.1016/s0143-4004(96)90061-2
Source DB: PubMed Journal: Placenta ISSN: 0143-4004 Impact factor: 3.481