Hepcidin Regulates Cellular Iron Efflux by Binding to Ferroportin and Inducing Its Internalization

American Association for the Advancement of Science (AAAS) - Tập 306 Số 5704 - Trang 2090-2093 - 2004
Elizabeta Nemeth1,2,3, Marie S. Tuttle1,2,3, Julie Powelson1,2,3, Michael B. Vaughn1,2,3, Adriana Donovan1,2,3, Diane M. Ward1,2,3, Tomas Ganz1,2,3, Jerry Kaplan1,2,3
1Department of Hematology, Children's Hospital, Boston, MA, USA.
2Department of Medicine, David Geffen School of Medicine, University of California, Los Angeles, CA, USA
3Department of Pathology, School of Medicine, University of Utah, Salt Lake City, UT, USA

Tóm tắt

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.

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Molecular interaction data have been deposited in the Biomolecular Interaction Network Database (BIND) with accession code 181881. We thank J. P. Kushner and J. Hoidal for their critical reading of the manuscript. This work was supported by NIH grant DK065029 and the Will Rogers Fund to T.G. and by NIH grants HL26922 and DK30534 to J.K. M.S. was supported by NIH grant T35HL007744.