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Hepcidin Regulates Cellular Iron Efflux by Binding to Ferroportin and Inducing Its Internalization
Elizabeta Nemeth,1
Marie S. Tuttle,2
Julie Powelson,2
Michael B. Vaughn,2
Adriana Donovan,3
Diane McVey Ward,2
Tomas Ganz,1*
Jerry Kaplan2*
Abstract:
Hepcidin is a peptide hormone secreted by the liver in responseto iron loading and inflammation. Decreased hepcidin leads totissue iron overload, whereas hepcidin overproduction leadsto hypoferremia and the anemia of inflammation. Ferroportinis an iron exporter present on the surface of absorptive enterocytes,macrophages, hepatocytes, and placental cells. Here we reportthat hepcidin bound to ferroportin in tissue culture cells.After binding, ferroportin was internalized and degraded, leadingto decreased export of cellular iron. The posttranslationalregulation of ferroportin by hepcidin may thus complete a homeostaticloop: Iron regulates the secretion of hepcidin, which in turncontrols the concentration of ferroportin on the cell surface.
1 Department of Medicine, David Geffen School of Medicine, University of California, Los Angeles, CA, USA. 2 Department of Pathology, School of Medicine, University of Utah, Salt Lake City, UT, USA. 3 Department of Hematology, Children's Hospital, Boston, MA, USA.
* To whom correspondence should be addressed. E-mail: TGanz{at}mednet.ucla.edu (T.G.); jerry.kaplan{at}path.utah.edu (J.K.)
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