Am J Physiol Cell Physiol Journal of Neurophysiology
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
QUICK SEARCH:   [advanced]


     

Am J Physiol Cell Physiol (October 24, 2001). doi:10.1152/ajpcell.00019.2001
This Article
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
282/3/C472    most recent
00019.2001v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Danzeisen, R.
Right arrow Articles by McArdle, H. J
Right arrow Search for Related Content
PubMed
Right arrow Articles by Danzeisen, R.
Right arrow Articles by McArdle, H. J

Articles in PresS, published online ahead of print October 22, 2001
Am J Physiol Cell Physiol, 10.1152/ajpcell.00019.2001
Submitted on January 16, 2001
Accepted on October 18, 2001

The placental ceruloplasmin homologue 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 Development, Growth and Function Division, The Rowett Research Institute, Aberdeen, Scotland, United Kingdom
2 Biomedical Sciences, University of Aberdeen, Aberdeen, Scotland, United Kingdom
3 Center for Research in Neuroscience, McGill University, Montreal, Quebec, Canada

* To whom correspondence should be addressed. E-mail: rd{at}rri.sari.ac.uk.

We have 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 peri-nuclear 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 both enzyme and protein levels. To identify a role for the Cu oxidase, cells were exposed to 59Fe-transferrin for 18 hours, in an environment of 20% or 5% oxygen. At 5% oxygen, 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 down-regulation of the placental Cu oxidase in BeWo cells impairs Fe release. This effect is only apparent in an environment of limited oxygen.




This article has been cited by other articles:


Home page
 IOVSHome page
K. Stasi, D. Nagel, X. Yang, L. Ren, T. Mittag, and J. Danias
Ceruloplasmin Upregulation in Retina of Murine and Human Glaucomatous Eyes
Invest. Ophthalmol. Vis. Sci., February 1, 2007; 48(2): 727 - 732.
[Abstract] [Full Text] [PDF]

Home page
 J. Nutr.Home page
C. L. Keen, M. S. Clegg, L. A. Hanna, L. Lanoue, J. M. Rogers, G. P. Daston, P. Oteiza, and J. Y. Uriu-Adams
The Plausibility of Micronutrient Deficiencies Being a Significant Contributing Factor to the Occurrence of Pregnancy Complications
J. Nutr., May 1, 2003; 133(5): 1597S - 1605.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
Visit Other APS Journals Online
Copyright © 1976 by the American Physiological Society.