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Prepublished online as a Blood First Edition Paper on August 7, 2003; DOI 10.1182/blood-2003-04-1250. This Article Full Text (PDF) All Versions of this Article: 2003-04-1250v1 102/12/4191    most recent Alert me when this article is cited Alert me if a correction is posted 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 Knutson, M. D Articles by Wessling-Resnick, M. Search for Related Content PubMed PubMed Citation Articles by Knutson, M. D Articles by Wessling-Resnick, M. Social Bookmarking                   What's this? Submitted April 23, 2003 Accepted July 27, 2003 Iron loading and erythrophagocytosis increase ferroportin1 (FPN1) expression in J774 macrophages Mitchell D Knutson, Mohammad R Vafa, David J Haile, and Marianne Wessling-Resnick* Department of Nutrition, Harvard School of Public Health, Boston, MA, USA Department of Social Medicine, Rafsanjan University of Medical Sciences, Rafsanjan, Iran Department of Medicine, University of Texas Health Science Center, San Antonio, TX, USA; Audie Murphy Veterans Affairs Hospital, South Texas Veterans Health System, San Antonio, TX, USA * Corresponding author; email: wessling{at}hsph.harvard.edu. The expression of ferroportin1 (FPN1) in reticuloendothelial macrophages supports the hypothesis that this iron-export protein participates in iron recycling from senescent erythrocytes. To gain insight into FPN1s role in macrophage iron metabolism, we examined the effect of iron status and erythrophagocytosis on FPN1 expression in J774 macrophages. Northern analysis indicated that FPN1 mRNA levels decreased with iron depletion and increased upon iron loading. The iron-induced induction of FPN1 mRNA was blocked by actinomycin D, suggesting that transcriptional control was responsible for this effect. After erythrophagocytosis, FPN1 mRNA levels were also upregulated, increasing 8-fold after 4 h and returning to basal levels by 16 h. Western analysis indicated corresponding increases in FPN1 protein levels, with maximal induction after 10 h. Iron chelation suppressed FPN1 mRNA and protein induction after erythrophagocytosis, suggesting that FPN1 induction results from erythrocyte-derived iron. Comparative Northern analyses of iron-related genes after erythrophagocytosis revealed a 16-fold increase in FPN1 levels after 3 h, a 10-fold increase in heme oxygenase-1 (HO-1) after 3 h, a 2-fold increase in Nramp1 levels after 6 h, but no change in DMT1 levels. 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