Placental ceruloplasmin homolog is regulated by iron and copper and is implicated in iron metabolism
| Autor: | Zehane Chariana, Samuel David, Ruth Danzeisen, Harry J. McArdle, Kenneth Robert Page, Cedric Fosset |
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| Rok vydání: | 2002 |
| Předmět: |
Hephaestin
Physiology Iron Placenta Deferoxamine Phenylenediamines Cell Fractionation Iron Chelating Agents Heterocyclic Compounds Pregnancy Tumor Cells Cultured medicine Animals Humans Metallothionein Choriocarcinoma Aceruloplasminemia chemistry.chemical_classification Oxidase test biology Ceruloplasmin Sarcosine Cell Biology medicine.disease Oxygen medicine.anatomical_structure chemistry Biochemistry Transferrin Cell culture Uterine Neoplasms biology.protein Female Oxidoreductases Copper |
| Zdroj: | American Journal of Physiology-Cell Physiology. 282:C472-C478 |
| ISSN: | 1522-1563 0363-6143 |
| Popis: | We previously reported an endogenous, membrane-bound Cu oxidase with homology to ceruloplasmin in BeWo cells, a placental choriocarcinoma cell line. In this previous study, ceruloplasmin immunoreactivity was localized to the perinuclear region and non-brush-border membranes. Here, we show that azide-sensitive oxidase activity is enriched in the same fractions, correlating subcellular localization of enzyme activity with ceruloplasmin immunoreactivity. Expression of the placental Cu oxidase is inversely proportional to Fe status and directly proportional to Cu status at enzyme and protein levels. To identify a role for the Cu oxidase, cells were exposed to59Fe-transferrin for 18 h in an environment of 20% O2or 5% O2. At 5% O2, Cu-deficient cells retain significantly more59Fe than control cells. This excess in59Fe accumulation is caused by a significant decrease in59Fe release. These results indicate that downregulation of the placental Cu oxidase in BeWo cells impairs Fe release. This effect is only apparent in an environment of limited O2. |
| Databáze: | OpenAIRE |
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