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Am J Physiol Cell Physiol 282: C472-C478, 2002. First published October 24, 2001; doi:10.1152/ajpcell.00019.2001
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Vol. 282, Issue 3, C472-C478, March 2002

Placental ceruloplasmin homolog is regulated by iron and copper and is implicated in iron metabolism

Ruth Danzeisen1, Cedric Fosset1, Zehane Chariana1, Kenneth Page2, Samuel David3, and Harry J. McArdle1

1 The Rowett Research Institute, Bucksburn, Aberdeen AB21 9SB; 2 Department of Biomedical Sciences, Institute of Medical Sciences, University of Aberdeen, Aberdeen AB25 2ZD, Scotland, United Kingdom; and 3 Center for Research in Neuroscience, The Montreal General Hospital Research Institute and McGill University, Montreal, Quebec, Canada H3G 1A4

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 to 59Fe-transferrin for 18 h in an environment of 20% O2 or 5% O2. At 5% O2, Cu-deficient cells retain significantly more 59Fe than control cells. This excess in 59Fe accumulation is caused by a significant decrease in 59Fe 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.

BeWo; hephaestin; hypoxia; placenta; human; ferroxidase


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