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Am J Physiol Gastrointest Liver Physiol 281: G931-G939, 2001;
0193-1857/01 $5.00
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Vol. 281, Issue 4, G931-G939, October 2001

Cloning and gastrointestinal expression of rat hephaestin: relationship to other iron transport proteins

David M. Frazer1, Christopher D. Vulpe2, Andrew T. McKie3, Sarah J. Wilkins1, Deborah Trinder4, Geoffrey J. Cleghorn5, and Gregory J. Anderson1

1 Joint Clinical Sciences Program, The Queensland Institute of Medical Research and The University of Queensland, PO Royal Brisbane Hospital and 5 Department of Pediatrics and Child Health, University of Queensland, Brisbane, Queensland 4029; and 4 Department of Medicine, The University of Western Australia, Fremantle Hospital, Fremantle, Western Australia 6160, Australia; 2 Department of Nutritional Sciences, University of California, Berkeley, California 94720; and 3 Department of Molecular Medicine, King's College, London SE59NU, United Kingdom

The membrane-bound ceruloplasmin homolog hephaestin plays a critical role in intestinal iron absorption. The aims of this study were to clone the rat hephaestin gene and to examine its expression in the gastrointestinal tract in relation to other genes encoding iron transport proteins. The rat hephaestin gene was isolated from intestinal mRNA and was found to encode a protein 96% identical to mouse hephaestin. Analysis by ribonuclease protection assay and Western blotting showed that hephaestin was expressed at high levels throughout the small intestine and colon. Immunofluorescence localized the hephaestin protein to the mature villus enterocytes with little or no expression in the crypts. Variations in iron status had a small but nonsignificant effect on hephaestin expression in the duodenum. The high sequence conservation between rat and mouse hephaestin is consistent with this protein playing a central role in intestinal iron absorption, although its precise function remains to be determined.

divalent metal transporter-1; Ireg1; absorption; intestine


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