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Prepublished online as a Blood First Edition Paper on November 14, 2002; DOI 10.1182/blood-2002-10-3235. This Article Full Text Full Text (PDF) All Versions of this Article: 2002-10-3235v1 101/7/2461    most recent Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Nemeth, E. Articles by Ganz, T. Search for Related Content PubMed PubMed Citation Articles by Nemeth, E. Articles by Ganz, T. Related Collections Red Cells Plenary Papers Gene Expression Brief Reports Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  Blood, 1 April 2003, Vol. 101, No. 7, pp. 2461-2463 PLENARY PAPERS Brief report Hepcidin, a putative mediator of anemia of inflammation, is a type II acute-phase protein Elizabeta Nemeth, Erika V. Valore, Mary Territo, Gary Schiller, Alan Lichtenstein, and Tomas Ganz From the Departments of Medicine and Pathology, David Geffen School of Medicine, and the West Los Angeles Veterans Administration Hospital, University of California, Los Angeles (UCLA), Los Angeles, CA. Hepcidin is a liver-made peptide proposed to be a central regulator of intestinal iron absorption and iron recycling by macrophages. In animal models, hepcidin is induced by inflammation and iron loading, but its regulation in humans has not been studied. We report that urinary excretion of hepcidin was greatly increased in patients with iron overload, infections, or inflammatory diseases. Hepcidin excretion correlated well with serum ferritin levels, which are regulated by similar pathologic stimuli. In vitro iron loading of primary human hepatocytes, however, unexpectedly down-regulated hepcidin mRNA, suggesting that in vivo regulation of hepcidin expression by iron stores involves complex indirect effects. Hepcidin mRNA was dramatically induced by interleukin-6 (IL-6) in vitro, but not by IL-1 or tumor necrosis factor  (TNF-), demonstrating that human hepcidin is a type II acute-phase reactant. The linkage of hepcidin induction to inflammation in humans supports its proposed role as a key mediator of anemia of inflammation. © 2003 by The American Society of Hematology.   CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: S. A. Browne and D. 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