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Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization.
Science. 2004 Dec 17; 306(5704):2090-3.Sci

Abstract

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.

Authors+Show Affiliations

Department of Medicine, David Geffen School of Medicine, University of California, Los Angeles, CA, USA.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

15514116

Citation

Nemeth, Elizabeta, et al. "Hepcidin Regulates Cellular Iron Efflux By Binding to Ferroportin and Inducing Its Internalization." Science (New York, N.Y.), vol. 306, no. 5704, 2004, pp. 2090-3.
Nemeth E, Tuttle MS, Powelson J, et al. Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization. Science. 2004;306(5704):2090-3.
Nemeth, E., Tuttle, M. S., Powelson, J., Vaughn, M. B., Donovan, A., Ward, D. M., Ganz, T., & Kaplan, J. (2004). Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization. Science (New York, N.Y.), 306(5704), 2090-3.
Nemeth E, et al. Hepcidin Regulates Cellular Iron Efflux By Binding to Ferroportin and Inducing Its Internalization. Science. 2004 Dec 17;306(5704):2090-3. PubMed PMID: 15514116.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization. AU - Nemeth,Elizabeta, AU - Tuttle,Marie S, AU - Powelson,Julie, AU - Vaughn,Michael B, AU - Donovan,Adriana, AU - Ward,Diane McVey, AU - Ganz,Tomas, AU - Kaplan,Jerry, Y1 - 2004/10/28/ PY - 2004/10/30/pubmed PY - 2005/1/15/medline PY - 2004/10/30/entrez SP - 2090 EP - 3 JF - Science (New York, N.Y.) JO - Science VL - 306 IS - 5704 N2 - 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. SN - 1095-9203 UR - https://www.unboundmedicine.com/medline/citation/15514116/Hepcidin_regulates_cellular_iron_efflux_by_binding_to_ferroportin_and_inducing_its_internalization_ L2 - https:///www.science.org/doi/10.1126/science.1104742?url_ver=Z39.88-2003&rfr_id=ori:rid:crossref.org&rfr_dat=cr_pub=pubmed DB - PRIME DP - Unbound Medicine ER -