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1. C. H. Park, E. V. Valore, A. J. Waring, and T. Ganz, “Hepcidin, a urinary antimicrobial peptide synthesized in the liver,” Journal of Biological Chemistry, vol. 276, no. 11, pp. 7806–7810, 2001. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
2. B. Gagliardo, N. Kubat, A. Faye, et al., “Pro-hepcidin is unable to degrade the iron exporter ferroportin unless maturated by a furin-dependent process,” Journal of Hepatology, vol. 50, no. 2, pp. 394–401, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
3. E. V. Valore and T. Ganz, “Posttranslational processing of hepcidin in human hepatocytes is mediated by the prohormone convertase furin,” Blood Cells, Molecules, and Diseases, vol. 40, no. 1, pp. 132–138, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
4. C. N. Roy, H. H. Mak, I. Akpan, G. Losyev, D. Zurakowski, and N. C. Andrews, “Hepcidin antimicrobial peptide transgenic mice exhibit features of the anemia of inflammation,” Blood, vol. 109, no. 9, pp. 4038–4044, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
5. A. Roettol, G. Papanikolaou, M. Politou, et al., “Mutant antimicrobial peptide hepcidin is associated with severe juvenile hemochromatosis,” Nature Genetics, vol. 33, no. 1, pp. 21–22, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
6. A. Donovan, C. A. Lima, J. L. Pinkus, et al., “The iron exporter ferroportin/Slc40a1 is essential for iron homeostasis,” Cell Metabolism, vol. 1, no. 3, pp. 191–200, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
7. S. Abboud and D. J. Haile, “A novel mammalian iron-regulated protein involved in intracellular iron metabolism,” Journal of Biological Chemistry, vol. 275, no. 26, pp. 19906–19912, 2000. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
8. A. Donovan, A. Brownlie, Y. Zhou, et al., “Positional cloning of zebrafish ferroportin1 identifies a conserved vertebrate iron exporter,” Nature, vol. 403, no. 6771, pp. 776–781, 2000. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
9. A. T. McKie, P. Marciani, A. Rolfs, et al., “A novel duodenal iron-regulated transporter, IREG1, implicated in the basolateral transfer of iron to the circulation,” Molecular Cell, vol. 5, no. 2, pp. 299–309, 2000. View at Scopus
10. E. Nemeth, M. S. Tuttle, J. Powelson, et al., “Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization,” Science, vol. 306, no. 5704, pp. 2090–2093, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
11. S. Rivera, E. Nemeth, V. Gabayan, M. A. Lopez, D. Farshidi, and T. Ganz, “Synthetic hepcidin causes rapid dose-dependent hypoferremia and is concentrated in ferroportin-containing organs,” Blood, vol. 106, no. 6, pp. 2196–2199, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
12. D.-L. Zhang, R. M. Hughes, H. Ollivierre-Wilson, M. C. Ghosh, and T. A. Rouault, “A ferroportin transcript that lacks an iron-responsive element enables duodenal and erythroid precursor cells to evade translational repression,” Cell Metabolism, vol. 9, no. 5, pp. 461–473, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
13. T. Ganz, G. Olbina, D. Girelli, E. Nemeth, and M. Westerman, “Immunoassay for human serum hepcidin,” Blood, vol. 112, no. 10, pp. 4292–4297, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
14. M. Pak, M. A. Lopez, V. Gabayan, T. Ganz, and S. Rivera, “Suppression of hepcidin during anemia requires erythropoietic activity,” Blood, vol. 108, no. 12, pp. 3730–3735, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
15. T. Ganz, “Molecular pathogenesis of anemia of chronic disease,” Pediatric Blood and Cancer, vol. 46, no. 5, pp. 554–557, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
16. Y. Xia, J. L. Babitt, Y. Sidis, R. T. Chung, and H. Y. Lin, “Hemojuvelin regulates hepcidin expression via a selective subset of BMP ligands and receptors independently of neogenin,” Blood, vol. 111, no. 10, pp. 5195–5204, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
17. B. Andriopoulos Jr., E. Corradini, Y. Xia, et al., “BMP6 is a key endogenous regulator of hepcidin expression and iron metabolism,” Nature Genetics, vol. 41, no. 4, pp. 482–487, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
18. D. Meynard, L. Kautz, V. Darnaud, F. Canonne-Hergaux, H. Coppin, and M.-P. Roth, “Lack of the bone morphogenetic protein BMP6 induces massive iron overload,” Nature Genetics, vol. 41, no. 4, pp. 478–481, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
19. J. L. Babitt, F. W. Huang, D. M. Wrighting, et al., “Bone morphogenetic protein signaling by hemojuvelin regulates hepcidin expression,” Nature Genetics, vol. 38, no. 5, pp. 531–539, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
20. L. Lin, Y. P. Goldberg, and T. Ganz, “Competitive regulation of hepcidin mRNAby soluble and cell-associated hemojuvelin,” Blood, vol. 106, no. 8, pp. 2884–2889, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
21. V. Niederkofler, R. Salie, and S. Arber, “Hemojuvelin is essential for dietary iron sensing, and its mutation leads to severe iron overload,” Journal of Clinical Investigation, vol. 115, no. 8, pp. 2180–2186, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
22. L. Silvestri, A. Pagani, A. Nai, I. de Domenico, J. Kaplan, and C. Camaschella, “The serine protease matriptase-2 (TMPRSS6) inhibits hepcidin activation by cleaving membrane hemojuvelin,” Cell Metabolism, vol. 8, no. 6, pp. 502–511, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
23. A.-S. Zhang, F. Yang, K. Meyer, et al., “Neogenin-mediated hemojuvelin shedding occurs after hemojuvelin traffics to the plasma membrane,” Journal of Biological Chemistry, vol. 283, no. 25, pp. 17494–17502, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
24. L. Kautz, D. Meynard, A. Monnier, et al., “Iron regulates phosphorylation of Smad1/5/8 and gene expression of Bmp6, Smad7, Id1, and Atoh8 in the mouse liver,” Blood, vol. 112, no. 4, pp. 1503–1509, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
25. M. B. Johnson, J. Chen, N. Murchison, F. A. Green, and C. A. Enns, “Transferrin receptor 2: evidence for ligand-induced stabilization and redirection to a recycling pathway,” Molecular Biology of the Cell, vol. 18, no. 3, pp. 743–754, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
26. G. Ramey, J.-C. Deschemin, and S. Vaulont, “Cross-talk between the mitogen activated protein kinase and bone morphogenetic protein/hemojuvelin pathways is required for the induction of hepcidin by holotransferrin in primary mouse hepatocytes,” Haematologica, vol. 94, no. 6, pp. 765–772, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
27. T. Goswami and N. C. Andrews, “Hereditary hemochromatosis protein, HFE, interaction with transferrin receptor 2 suggests a molecular mechanism for mammalian iron sensing,” Journal of Biological Chemistry, vol. 281, no. 39, pp. 28494–28498, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
28. A. Piperno, D. Girelli, E. Nemeth, et al., “Blunted hepcidin response to oral iron challenge in HFE-related hemochromatosis,” Blood, vol. 110, no. 12, pp. 4096–4100, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
29. D. R. Ashby, D. P. Gale, M Busbridge, et al., “Erythropoietin administration in humans causes a marked and prolonged reduction in circulating hepcidin,” Haematologica. In press.
30. H. Huang, M. Constante, A. Layoun, and M. M. Santos, “Contribution of STAT3 and SMAD4 pathways to the regulation of hepcidin by opposing stimuli,” Blood, vol. 113, no. 15, pp. 3593–3599, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
31. M. Vokurka, J. Krijt, K. Sulc, and E. Necas, “Hepcidin mRNA levels in mouse liver respond to inhibition of erythropoiesis,” Physiological Research, vol. 55, no. 6, pp. 667–674, 2006. View at Scopus
32. T. Tanno, N. V. Bhanu, P. A. Oneal, et al., “High levels of GDF15 in thalassemia suppress expression of the iron regulatory protein hepcidin,” Nature Medicine, vol. 13, no. 9, pp. 1096–1101, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
33. T. Tanno, P. Porayette, O. Sripichai, et al., “Identification of TWSG1 as a second novel erythroid regulator of hepcidin expression in murine and human cells,” Blood, vol. 114, no. 1, pp. 181–186, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
34. C. Peyssonnaux, A. S. Zinkernagel, R. A. Schuepbach, et al., “Regulation of iron homeostasis by the hypoxia-inducible transcription factors (HIFs),” Journal of Clinical Investigation, vol. 117, no. 7, pp. 1926–1932, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
35. G. Semrin, D. S. Fishman, A. Bousvaros, et al., “Impaired intestinal iron absorption in Crohn's disease correlates with disease activity and markers of inflammation,” Inflammatory Bowel Diseases, vol. 12, no. 12, pp. 1101–1106, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
36. S. Sharma, E. Nemeth, Y.-H. Chen, et al., “Involvement of hepcidin in the anemia of multiple myeloma,” Clinical Cancer Research, vol. 14, no. 11, pp. 3262–3267, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
37. E. Nemeth, E. V. Valore, M. Territo, G. Schiller, A. Lichtenstein, and T. Ganz, “Hepcidin, a putative mediator of anemia of inflammation, is a type II acute-phase protein,” Blood, vol. 101, no. 7, pp. 2461–2463, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
38. M. V. Verga Falzacappa, M. Vujic Spasic, R. Kessler, J. Stolte, M. W. Hentze, and M. U. Muckenthaler, “STAT3 mediates hepatic hepcidin expression and its inflammatory stimulation,” Blood, vol. 109, no. 1, pp. 353–358, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
39. E. Nemeth, S. Rivera, V. Gabayan, et al., “IL-6 mediates hypoferremia of inflammation by inducing the synthesis of the iron regulatory hormone hepcidin,” Journal of Clinical Investigation, vol. 113, no. 9, pp. 1271–1276, 2004. View at Publisher · View at Google Scholar · View at Scopus
40. S. Rivera, V. Gabayan, and T. Ganz, “In chronic inflammation, there exists an IL-6 independent pathway for the induction of hepcidin,” vol. 104, no. 11, 2004, Abstract no. 3205.
41. C. Peyssonnaux, A. S. Zinkernagel, V. Datta, X. Lauth, R. S. Johnson, and V. Nizet, “TLR4-dependent hepcidin expression by myeloid cells in response to bacterial pathogens,” Blood, vol. 107, no. 9, pp. 3727–3732, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
42. S. Sazawal, R. E. Black, M. Ramsan, et al., “Effects of routine prophylactic supplementation with iron and folic acid on admission to hospital and mortality in preschool children in a high malaria transmission setting: community-based, randomised, placebo-controlled trial,” The Lancet, vol. 367, no. 9505, pp. 133–143, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
43. M. A. Melis, M. Cau, R. Congiu, et al., “A mutation in the TMPRSS6 gene, encoding a transmembrane serine protease that suppresses hepcidin production, in familial iron deficiency anemia refractory to oral iron,” Haematologica, vol. 93, no. 10, pp. 1473–1479, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
44. K. E. Finberg, M. M. Heeney, D. R. Campagna, et al., “Mutations in TMPRSS6 cause iron-refractory iron deficiency anemia (IRIDA),” Nature Genetics, vol. 40, no. 5, pp. 569–571, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
45. J. C. Chambers, W. Zhang, Y. Li, et al., “Genome-wide association study identifies variants in TMPRSS6 associated with hemoglobin levels,” Nature Genetics, vol. 41, no. 11, pp. 1170–1172, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
46. B. Benyamin, M. A. R. Ferreira, G. Willemsen, et al., “Common variants in TMPRSS6 are associated with iron status and erythrocyte volume,” Nature Genetics, vol. 41, no. 11, pp. 1173–1175, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
47. D. A. Weinstein, C. N. Roy, M. D. Fleming, M. F. Loda, J. I. Wolfsdorf, and N. C. Andrews, “Inappropriate expression of hepcidin is associated with iron refractory anemia: implications for the anemia of chronic disease,” Blood, vol. 100, no. 10, pp. 3776–3781, 2002. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
48. A. Y. F. Chung, K. W. Leo, G. C. Wong, K. L. Chuah, J. W. Ren, and C. G. L. Lee, “Giant hepatocellular adenoma presenting with chronic iron deficiency anemia,” American Journal of Gastroenterology, vol. 101, no. 9, pp. 2160–2162, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
49. S. L. Kearney, E. Nemeth, E. J. Neufeld, et al., “Urinary hepcidin in congenital chronic anemias,” Pediatric Blood and Cancer, vol. 48, no. 1, pp. 57–63, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
50. E. Nemeth and T. Ganz, “Hepcidin and iron-loading anemias,” Haematologica, vol. 91, no. 6, pp. 727–732, 2006.
51. R. Origa, R. Galanello, T. Ganz, et al., “Liver iron concentrations and urinary hepcidin in $\beta$-thalassemia,” Haematologica, vol. 92, no. 5, pp. 583–588, 2007. View at Publisher · View at Google Scholar · View at Scopus
52. G. E. Cartwright, “The anemia of chronic disorders,” Seminars in Hematology, vol. 3, no. 4, pp. 351–375, 1966. View at Scopus
53. S. Rivera, L. Liu, E. Nemeth, V. Gabayan, O. E. Sorensen, and T. Ganz, “Hepcidin excess induces the sequestration of iron and exacerbates tumor-associated anemia,” Blood, vol. 105, no. 4, pp. 1797–1802, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
54. H. Li, M. J. Rose, L. Tran, et al., “Development of a method for the sensitive and quantitative determination of hepcidin in human serum using LC-MS/MS,” Journal of Pharmacological and Toxicological Methods, vol. 59, no. 3, pp. 171–180, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
55. E. H. J. M. Kemna, H. Tjalsma, V. N. Podust, and D. W. Swinkels, “Mass spectrometry-based hepcidin measurements in serum and urine: analytical aspects and clinical implications,” Clinical Chemistry, vol. 53, no. 4, pp. 620–628, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
56. L. M. Tussing-Humphreys, H. Liang, E. Nemeth, S. Freels, and C. A. Braunschweig, “Excess adiposity, inflammation, and iron-deficiency in female adolescents,” Journal of the American Dietetic Association, vol. 109, no. 2, pp. 297–302, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
57. L. M. Tussing-Humphreys, E. Nemeth, G. Fantuzzi, et al., “Elevated systemic hepcidin and iron depletion in obese premenopausal females,” Obesity. In press.
58. B. J. Sasu, M. Hainu, T. C. Boone, et al., “Hepcidin, hepcidin antagonists and methods of use,” US patent no. US2008213277, Amgen Inc.Thousand Oaks, Calif, USA, September 2008.
59. B. Young and J. Zaritsky, “Hepcidin for clinicians,” Clinical Journal of the American Society of Nephrology, vol. 4, no. 8, pp. 1384–1387, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
60. J. Zaritsky, B. Young, H. J. Wang, et al., “Hepcidin—a potential novel biomarker for iron status in chronic kidney disease,” Clinical Journal of the American Society of Nephrology, vol. 4, no. 6, pp. 1051–1056, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
61. D. R. Ashby, D. P. Gale, M. Busbridge, et al., “Plasma hepcidin levels are elevated but responsive to erythropoietin therapy in renal disease,” Kidney International, vol. 75, no. 9, pp. 976–981, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
62. J. W. Adamson, “Hyporesponsiveness to erythropoiesis stimulating agents in chronic kidney disease: the many faces of inflammation,” Advances in Chronic Kidney Disease, vol. 16, no. 2, pp. 76–82, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
63. J. Elliott, D. Mishler, and R. Agarwal, “Hyporesponsiveness to erythropoietin: causes and management,” Advances in Chronic Kidney Disease, vol. 16, no. 2, pp. 94–100, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
64. M. Busbridge, C. Griffiths, D. R. Ashby, et al., “Development of a novel immunoassay for the iron regulatory peptide hepcidin,” British Journal of Biomedical Science, vol. 66, no. 3, pp. 150–157, 2009.
65. A. Castagna, N. Campostrini, F. Zaninotto, and D. Girelli, “Hepcidin assay in serum by SELDI-TOF-MS and other approaches,” Journal of Proteomics. In press. View at Publisher · View at Google Scholar · View at PubMed
66. S. S. Bansal, J. M. Halket, J. Fusova, et al., “Quantification of hepcidin using matrix-assisted laser desorption/ ionization time-of-flight mass spectrometry,” Rapid Communications in Mass Spectrometry, vol. 23, no. 11, pp. 1531–1542, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
67. J. J. C. Kroot, J. C. M. Hendriks, C. M. M. Laarakkers, et al., “(Pre)analytical imprecision, between-subject variability, and daily variations in serum and urine hepcidin: implications for clinical studies,” Analytical Biochemistry, vol. 389, no. 2, pp. 124–129, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
68. M. F. Young, R. P. Glahn, M. Ariza-Nieto, et al., “Serum hepcidin is significantly associated with iron absorption from food and supplemental sources in healthy young women,” American Journal of Clinical Nutrition, vol. 89, no. 2, pp. 533–538, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
69. M. Ruivard, F. Laine, T. Ganz, et al., “Iron absorption in dysmetabolic iron overload syndrome is decreased and correlates with increased plasma hepcidin,” Journal of Hepatology, vol. 50, no. 6, pp. 1219–1225, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
70. P. B. Yu, C. C. Hong, C. Sachidanandan, et al., “Dorsomorphin inhibits BMP signals required for embryogenesis and iron metabolism,” Nature Chemical Biology, vol. 4, no. 1, pp. 33–41, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
71. J. L. Babitt, F. W. Huang, Y. Xia, Y. Sidis, N. C. Andrews, and H. Y. Lin, “Modulation of bone morphogenetic protein signaling in vivo regulates systemic iron balance,” Journal of Clinical Investigation, vol. 117, no. 7, pp. 1933–1939, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
72. N. Nishimoto, Y. Kanakura, K. Aozasa, et al., “Humanized anti-interleukin-6 receptor antibody treatment of multicentric Castleman disease,” Blood, vol. 106, no. 8, pp. 2627–2632, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
73. H. Kawabata, N. Tomosugi, J. Kanda, Y. Tanaka, K. Yoshizaki, and T. Uchiyama, “Anti-interleukin 6 receptor antibody tocilizumab reduces the level of serum hepcidin in patients with multicentric Castleman's disease,” Haematologica, vol. 92, no. 6, pp. 857–858, 2007. View at Publisher · View at Google Scholar · View at Scopus
74. S. Klaus, M. Arend, P. Fourney, et al., “Induction of erythropoiesis and iron utilization by the HIF prolyl hydroxylase inhibitor FG-4592,” Journal of the American Society of Nephrology, vol. 16, p. 49A, 2005.