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Originally published in Science Express on 28 October 2004
Science 17 December 2004:
Vol. 306. no. 5704, pp. 2090 - 2093
DOI: 10.1126/science.1104742
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Reports

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*

Hepcidin is a peptide hormone secreted by the liver in response to iron loading and inflammation. Decreased hepcidin leads to tissue iron overload, whereas hepcidin overproduction leads to hypoferremia and the anemia of inflammation. Ferroportin is an iron exporter present on the surface of absorptive enterocytes, macrophages, hepatocytes, and placental cells. Here we report that hepcidin bound to ferroportin in tissue culture cells. After binding, ferroportin was internalized and degraded, leading to decreased export of cellular iron. The posttranslational regulation of ferroportin by hepcidin may thus complete a homeostatic loop: Iron regulates the secretion of hepcidin, which in turn controls 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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Science. ISSN 0036-8075 (print), 1095-9203 (online)