Molecular control of iron transport
Abstract
The iron-regulatory hormone hepcidin is a 25-amino acid peptide that is synthesized in hepatocytes. Hepcidin binds to the cellular iron export channel ferroportin and causes its internalization and degradation and thereby decreases iron efflux from iron exporting tissues into plasma. By this mechanism, hepcidin inhibits dietary iron absorption, the efflux of recycled iron from splenic and hepatic macrophages, and the release of iron from storage in hepatocytes. Hepcidin synthesis is stimulated by plasma iron and iron stores and is inhibited by erythropoietic activity, ensuring that extracellular plasma iron concentrations and iron stores remain stable and the erythropoietic demand for iron is met. During inflammation, increased hepcidin concentrations cause iron sequestration in macrophages, resulting in hypoferremia and eventually anemia of inflammation. Hepcidin deficiency plays a central role in most iron overload disorders. The role of hepcidin abnormalities in anemias that are associated with renal disease and in resistance to erythropoietic therapies remains to be elucidated.
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Elevated hepcidin leads to reduced ferroportin surface expression and hypoferremia.
“and lead to reduced ferroportin surface expression and hypoferremia”
From Regulation of erythropoiesis by hypoxia-inducible factors (2013) · cites this paper as [188]
Hepcidin suppresses intestinal iron uptake and release of iron from internal stores by facilitating the degradation and internalization of ferroportin.
“Hepcidin suppresses intestinal iron uptake and release of iron from internal stores by facilitating the degradation and internalization of the only known cellular iron exporter, ferroportin”
From Regulation of erythropoiesis by hypoxia-inducible factors (2013) · cites this paper as [188]
Hepcidin has a key role in the pathogenesis of anemia of chronic disease.
“lending support to the notion that hepcidin has a key role in the pathogenesis of anemia of chronic disease.”
From Regulation of erythropoiesis by hypoxia-inducible factors (2013) · cites this paper as [188]
Chronically elevated serum hepcidin levels are frequently associated with inflammatory states.
“Chronically elevated serum hepcidin levels are frequently associated with inflammatory states”
From Regulation of erythropoiesis by hypoxia-inducible factors (2013) · cites this paper as [188]
Interleukin-6 induces hepcidin transcription via JAK/STAT signaling.
“(interleukin-6 induces hepcidin transcription via JAK/STAT signaling)”
From Regulation of erythropoiesis by hypoxia-inducible factors (2013) · cites this paper as [188]
Cites
Hepcidin Regulates Cellular Iron Efflux by Binding to Ferroportin and Inducing Its Internalization
Nemeth, E., Tuttle, M. S., Powelson, J., Vaughn, M. B., Donovan, A., Ward, D. M., Ganz, T., & Kaplan, J. (2004) · Science · doi:10.1126/science.1104742 · Cited by 4,803 · see citing works
Self-citationNemeth, E., Rivera, S., Gabayan, V., Keller, C., Taudorf, S., Pedersen, B. K., & Ganz, T. (2004) · Journal of Clinical Investigation · doi:10.1172/jci200420945 · Cited by 2,650 · cited 9× · see citing works
“Although the acute hypoferremic response and hepcidin induction both are impaired in IL-6–deficient mice (21), chronic inflammatory stimulation elicits hepcidin even in IL-6–deficient mice (31).”
BackgroundInfluentialSelf-citationHepcidin, a urinary antimicrobial peptide synthesized in the liver
Park, C. H., Valore, E. V., Waring, A. J., & Ganz, T. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008922200 · Cited by 2,168 · see citing works
Self-citationPigeon, C., Ilyin, G., Courselaud, B., Leroyer, P., Turlin, B., Brissot, P., & Loréal, O. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008923200 · Cited by 1,697 · see citing works
Positional cloning of zebrafish ferroportin1 identifies a conserved vertebrate iron exporter
Donovan, A., Brownlie, A., Zhou, Y., Shepard, J., Pratt, S. J., Moynihan, J., Paw, B. H., Drejer, A., Barut, B., Zapata, A., et al. (2000) · Nature · doi:10.1038/35001596 · Cited by 1,667 · see citing works
McKie, A. T., Marciani, P., Rolfs, A., Brennan, K., Wehr, K., Barrow, D., Miret, S., Bomford, A., Peters, T. J., Farzaneh, F., et al. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80425-6 · Cited by 1,422 · see citing works
Hepcidin, a putative mediator of anemia of inflammation, is a type II acute-phase protein
Nemeth, E., Valore, E. V., Territo, M., Schiller, G., Lichtenstein, A., & Ganz, T. (2003) · Blood · doi:10.1182/blood-2002-10-3235 · Cited by 1,417 · see citing works
LEAP-1, a novel highly disulfide-bonded human peptide, exhibits antimicrobial activity
Krause, A., Neitz, S., Mägert, H.-J., Schulz, A., Forssmann, W.-G., Schulz-Knappe, P., & Adermann, K. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)01920-7 · Cited by 1,324 · see citing works
The iron exporter ferroportin/Slc40a1 is essential for iron homeostasis
Donovan, A., Lima, C. A., Pinkus, J. L., Pinkus, G. S., Zon, L. I., Robine, S., & Andrews, N. C. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.01.003 · Cited by 1,275 · see citing works
A Novel Mammalian Iron-regulated Protein Involved in Intracellular Iron Metabolism
Abboud, S., & Haile, D. J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000713200 · Cited by 1,267 · see citing works
Nicolas, G., Bennoun, M., Devaux, I., Beaumont, C., Grandchamp, B., Kahn, A., & Vaulont, S. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.151179498 · Cited by 1,233 · see citing works
Nicolas, G., Chauvet, C., Viatte, L., Danan, J. L., Bigard, X., Devaux, I., Beaumont, C., Kahn, A., & Vaulont, S. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0215686 · Cited by 1,214 · see citing works
Vulpe, C. D., Kuo, Y.-M., Murphy, T. L., Cowley, L., Askwith, C., Libina, N., Gitschier, J., & Anderson, G. J. (1999) · Nature Genetics · doi:10.1038/5979 · Cited by 1,084 · see citing works
Bone morphogenetic protein signaling by hemojuvelin regulates hepcidin expression
Babitt, J. L., Huang, F. W., Wrighting, D. M., Xia, Y., Sidis, Y., Samad, T. A., Campagna, J. A., Chung, R. T., Schneyer, A. L., Woolf, C. J., et al. (2006) · Nature Genetics · doi:10.1038/ng1777 · Cited by 1,026 · see citing works
Interleukin-6 induces hepcidin expression through STAT3
Wrighting, D. M., & Andrews, N. C. (2006) · Blood · doi:10.1182/blood-2006-06-027631 · Cited by 983 · see citing works
Mutations in HFE2 cause iron overload in chromosome 1q–linked juvenile hemochromatosis
Papanikolaou, G., Samuels, M. E., Ludwig, E. H., MacDonald, M. L. E., Franchini, P. L., Dubé, M.-P., Andres, L., MacFarlane, J., Sakellaropoulos, N., Politou, M., et al. (2004) · Nature Genetics · doi:10.1038/ng1274 · Cited by 974 · see citing works
Self-citationSevere iron deficiency anemia in transgenic mice expressing liver hepcidin
Nicolas, G., Bennoun, M., Porteu, A., Mativet, S., Beaumont, C., Grandchamp, B., Sirito, M., Sawadogo, M., Kahn, A., & Vaulont, S. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.072632499 · Cited by 880 · see citing works
Mutant antimicrobial peptide hepcidin is associated with severe juvenile hemochromatosis
Roetto, A., Papanikolaou, G., Politou, M., Alberti, F., Girelli, D., Christakis, J., Loukopoulos, D., & Camaschella, C. (2003) · Nature Genetics · doi:10.1038/ng1053 · Cited by 860 · see citing works
Identification of an Intestinal Heme Transporter
Shayeghi, M., Latunde-Dada, G. O., Oakhill, J. S., Laftah, A. H., Takeuchi, K., Halliday, N., Khan, Y., Warley, A., McCann, F. E., Hider, R. C., et al. (2005) · Cell · doi:10.1016/j.cell.2005.06.025 · Cited by 755 · see citing works
Weinstein, D. A., Roy, C. N., Fleming, M. D., Loda, M. F., Wolfsdorf, J. I., & Andrews, N. C. (2002) · Blood · doi:10.1182/blood-2002-04-1260 · Cited by 632 · see citing works
A role of SMAD4 in iron metabolism through the positive regulation of hepcidin expression
Wang, R.-H., Li, C., Xu, X., Zheng, Y., Xiao, C., Zerfas, P., Cooperman, S., Eckhaus, M., Rouault, T., Mishra, L., et al. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.10.010 · Cited by 614 · see citing works
Targeted gene disruption reveals an essential role for ceruloplasmin in cellular iron efflux
Harris, Z. L., Durley, A. P., Man, T. K., & Gitlin, J. D. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.19.10812 · Cited by 568 · see citing works
Time-course analysis of hepcidin, serum iron, and plasma cytokine levels in humans injected with LPS
Kemna, E., Pickkers, P., Nemeth, E., van der Hoeven, H., & Swinkels, D. (2005) · Blood · doi:10.1182/blood-2005-03-1159 · Cited by 498 · see citing works
Knutson, M. D., Oukka, M., Koss, L. M., Aydemir, F., & Wessling-Resnick, M. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0409409102 · Cited by 479 · see citing works
Suppression of hepcidin during anemia requires erythropoietic activity
Pak, M., Lopez, M. A., Gabayan, V., Ganz, T., & Rivera, S. (2006) · Blood · doi:10.1182/blood-2006-06-028787 · Cited by 472 · see citing works
Self-citationHepcidin in iron overload disorders
Papanikolaou, G., Tzilianos, M., Christakis, J. I., Bogdanos, D., Tsimirika, K., MacFarlane, J., Goldberg, Y. P., Sakellaropoulos, N., Ganz, T., & Nemeth, E. (2005) · Blood · doi:10.1182/blood-2004-12-4844 · Cited by 445 · see citing works
Hunter, H. N., Fulton, D. B., Ganz, T., & Vogel, H. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m205305200 · Cited by 400 · see citing works
Hepcidin is decreased in TFR2 hemochromatosis
Nemeth, E., Roetto, A., Garozzo, G., Ganz, T., & Camaschella, C. (2004) · Blood · doi:10.1182/blood-2004-08-3042 · Cited by 396 · see citing works
Iron, Infections, and Anemia of Inflammation
Jurado, R. L. (1997) · Clinical Infectious Diseases · doi:10.1086/515549 · Cited by 358 · see citing works
Iron Metabolism in the Reticuloendothelial System
Knutson, M. D., & Wessling‐Resnick, M. (2003) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/713609210 · Cited by 349 · see citing works
Constitutive hepcidin expression prevents iron overload in a mouse model of hemochromatosis
Nicolas, G., Viatte, L., Lou, D.-Q., Bennoun, M., Beaumont, C., Kahn, A., Andrews, N. C., & Vaulont, S. (2003) · Nature Genetics · doi:10.1038/ng1150 · Cited by 311 · see citing works
Truksa, J., Peng, H., Lee, P., & Beutler, E. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0603124103 · Cited by 309 · see citing works
Rivera, S., Nemeth, E., Gabayan, V., Lopez, M. A., Farshidi, D., & Ganz, T. (2005) · Blood · doi:10.1182/blood-2005-04-1766 · Cited by 308 · see citing works
Self-citationMuckenthaler, M. U., Roy, C. N., Custodio, Á. O., Miñana, B., DEGRAAF, J., Montross, L. K., Andrews, N. C., & Hentze, M. W. (2003) · Nature Genetics · doi:10.1038/ng1152 · Cited by 293 · see citing works
Detection of serum hepcidin in renal failure and inflammation by using ProteinChip System
Tomosugi, N., Kawabata, H., Wakatabe, R., Higuchi, M., Yamaya, H., Umehara, H., & Ishikawa, I. (2006) · Blood · doi:10.1182/blood-2005-10-4043 · Cited by 292 · see citing works
Nemeth, E., Preza, G. C., Jung, C.-L., Kaplan, J., Waring, A. J., & Ganz, T. (2006) · Blood · doi:10.1182/blood-2005-05-2049 · Cited by 273 · see citing works
Self-citationResistance to hepcidin is conferred by hemochromatosis-associated mutations of ferroportin
Drakesmith, H., Schimanski, L. M., Ormerod, E., Merryweather-Clarke, A. T., Viprakasit, V., Edwards, J. P., Sweetland, E., Bastin, J. M., Cowley, D., Chinthammitr, Y., et al. (2005) · Blood · doi:10.1182/blood-2005-02-0561 · Cited by 264 · see citing works
Hepcidin mRNA levels in mouse liver respond to inhibition of erythropoiesis
Vokurka, M., Krijt, J., Šulc, K., & Nečas, E. (2006) · Physiological Research · doi:10.33549/physiolres.930841 · Cited by 263 · see citing works
Craven, C. M., Alexander, J., Eldridge, M., Kushner, J. P., Bernstein, S., & Kaplan, J. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.10.3457 · Cited by 259 · see citing works
Kulaksiz, H., Gehrke, S. G., Janetzko, A., Rost, D., Bruckner, T., Kallinowski, B., & Stremmel, W. (2004) · Gut · doi:10.1136/gut.2003.022863 · Cited by 246 · see citing works
Gehrke, S. G., Kulaksiz, H., Herrmann, T. R. W., Riedel, H.-D., Bents, K., Veltkamp, C., & Stremmel, W. (2003) · Blood · doi:10.1182/blood-2002-11-3610 · Cited by 244 · see citing works
The molecular basis of ferroportin-linked hemochromatosis
De Domenico, I., Ward, D. M., Nemeth, E., Vaughn, M. B., Musci, G., Ganz, T., & Kaplan, J. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0503804102 · Cited by 230 · see citing works
Self-citationIn vitro functional analysis of human ferroportin (FPN) and hemochromatosis-associated FPN mutations
Schimanski, L. M., Drakesmith, H., Merryweather-Clarke, A. T., Viprakasit, V., Edwards, J. P., Sweetland, E., Bastin, J. M., Cowley, D., Chinthammitr, Y., Robson, K. J. H., et al. (2005) · Blood · doi:10.1182/blood-2004-11-4502 · Cited by 212 · see citing works
Iron Imports. II. Iron uptake at the apical membrane in the intestine
Mackenzie, B., & Garrick, M. D. (2005) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00363.2005 · Cited by 211 · see citing works
Hepcidin excess induces the sequestration of iron and exacerbates tumor-associated anemia
Rivera, S., Liu, L., Nemeth, E., Gabayan, V., Sorensen, O. E., & Ganz, T. (2005) · Blood · doi:10.1182/blood-2004-08-3375 · Cited by 196 · see citing works
Self-citationDétivaud, L., Nemeth, E., Boudjéma, K., Turlin, B., Troadec, M., Leroyer, P., Ropert, M., Jacquelinet, S., Courselaud, B., Ganz, T., et al. (2005) · Blood · doi:10.1182/blood-2004-12-4855 · Cited by 189 · see citing works
Theurl, I., Mattle, V., Seifert, M., Mariani, M., Marth, C., & Weiss, G. (2006) · Blood · doi:10.1182/blood-2005-08-3364 · Cited by 188 · see citing works
Regulation of hepcidin and ferroportin expression by lipopolysaccharide in splenic macrophages
Liu, X.-B., Nguyen, N.-B., Marquess, K. D., Yang, F., & Haile, D. J. (2005) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2005.04.006 · Cited by 177 · see citing works
Urinary hepcidin in congenital chronic anemias
Kearney, S. L., Nemeth, E., Neufeld, E. J., Thapa, D., Ganz, T., Weinstein, D. A., & Cunningham, M. J. (2007) · Pediatric Blood & Cancer · doi:10.1002/pbc.20616 · Cited by 172 · see citing works
Self-citationSham, R. L., Phatak, P. D., West, C., Lee, P., Andrews, C., & Beutler, E. (2005) · Blood Cells, Molecules, and Diseases · doi:10.1016/j.bcmd.2004.12.002 · Cited by 146 · see citing works
Novel urine hepcidin assay by mass spectrometry
Kemna, E., Tjalsma, H., Laarakkers, C. M., Nemeth, E., Willems, H. L., & Swinkels, D. W. (2005) · Blood · doi:10.1182/blood-2005-05-1873 · Cited by 135 · see citing works
Functional consequences of ferroportin 1 mutations
Liu, X.-B., Yang, F., & Haile, D. J. (2005) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2005.04.005 · Cited by 132 · see citing works
Deregulation of proteins involved in iron metabolism in hepcidin-deficient mice
Viatte, L., Lesbordes, J.-C., Lou, D.-Q., Bennoun, M., Nicolas, G., Kahn, A., Canonne‐Hergaux, F., & Vaulont, S. (2005) · Blood · doi:10.1182/blood-2004-12-4608 · Cited by 119 · see citing works
Iron overload due to mutations in ferroportin.
Domenico, I. D., Ward, D. M., Musci, G., & Kaplan, J. (2006) · PubMed · Cited by 84 · see citing works
Viatte, L. (2005) · Blood · doi:10.1182/blood-2005-10-4071 · Cited by 80 · see citing works
Means, R. T., & Krantz, S. B. (1996) · PubMed · Cited by 54 · see citing works
Intravenous iron supplementation in the anaemia of renal and cardiac failure—a double-edged sword?
Slotki, I. N. (2005) · Nephrology Dialysis Transplantation · doi:10.1093/ndt/gfh1102 · Cited by 21 · see citing works
In Chronic Inflammation, There Exists an IL-6 Independent Pathway for the Induction of Hepcidin.
Rivera, S., Gabayan, V. R., & Ganz, T. (2004) · Blood · doi:10.1182/blood.v104.11.3205.3205 · Cited by 11 · see citing works
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Delayed Graft Function in the Kidney Transplant
Siedlecki, A. M., Irish, W. D., & Brennan, D. C. (2011) · American Journal of Transplantation · doi:10.1111/j.1600-6143.2011.03754.x · Cited by 823 · see citing works
“Collectively oxygen free radicals disrupt intracellular metabolic processes, transcellular solute gradients, and the proximal tubular cell super structure (23).”
BackgroundRegulation of erythropoiesis by hypoxia-inducible factors
Haase, V. H. (2013) · Blood Reviews · doi:10.1016/j.blre.2012.12.003 · Cited by 787 · see citing works
“Hepcidin suppresses intestinal iron uptake and release of iron from internal stores by facilitating the degradation and internalization of the only known cellular iron exporter, ferroportin, which is expressed on the surface of enterocytes, hepatocytes and macrophages.(187) In iron-deficient states (e.”
BackgroundRichardson, D. R., Lane, D. J. R., Becker, E. M., Huang, M. L.-H., Whitnall, M., Rahmanto, Y. S., Sheftel, A. D., & Ponka, P. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0912925107 · Cited by 536 · see citing works
“Hepcidin is a key regulator of systemic iron metabolism (18) and is transported in the blood bound to α2macroglobulin (18).”
BackgroundGuideline for the laboratory diagnosis of functional iron deficiency
Thomas, W., Hinchliffe, R. F., Briggs, C., Macdougall, I. C., Littlewood, T. J., & Cavill, I. (2013) · British Journal of Haematology · doi:10.1111/bjh.12311 · Cited by 405 · see citing works
“Recently, hepcidin has emerged as the master regulator of iron availability to the bone marrow (Ganz, 2007).”
BackgroundClark, S. F. (2008) · Nutrition in Clinical Practice · doi:10.1177/0884533608314536 · Cited by 380 · see citing works
Hepcidin—A Potential Novel Biomarker for Iron Status in Chronic Kidney Disease
Zaritsky, J. J., Young, B. Y., Wang, H.-J., Westerman, M. E., Olbina, G., Nemeth, E., Ganz, T., Rivera, S., Nissenson, A. R., & Salusky, I. B. (2009) · Clinical Journal of the American Society of Nephrology · doi:10.2215/cjn.05931108 · Cited by 349 · see citing works
“Hepcidin inhibits intestinal iron absorption and iron release from macrophages and hepatocytes (8).”
BackgroundResultInfluentialHypoxic regulation of erythropoiesis and iron metabolism
Haase, V. H. (2010) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00174.2010 · Cited by 347 · see citing works
Anaemia in kidney disease: harnessing hypoxia responses for therapy
Koury, M. J., & Haase, V. H. (2015) · Nature Reviews Nephrology · doi:10.1038/nrneph.2015.82 · Cited by 313 · see citing works
Plasma hepcidin levels are elevated but responsive to erythropoietin therapy in renal disease
Ashby, D. R., Gale, D. P., Busbridge, M., Murphy, K. G., Duncan, N. D., Cairns, T. D. H., Taube, D. H., Bloom, S. R., Tam, F. W. K., Chapman, R., et al. (2009) · Kidney International · doi:10.1038/ki.2009.21 · Cited by 308 · see citing works
Diagnosis and management of iron deficiency anemia in patients with IBD
Stein, J. M., Hartmann, F., & Dignass, A. U. (2010) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/nrgastro.2010.151 · Cited by 304 · see citing works
Iron in innate immunity: starve the invaders
Ganz, T. (2009) · Current Opinion in Immunology · doi:10.1016/j.coi.2009.01.011 · Cited by 284 · see citing works
Self-citationIron Acquisition and Transcriptional Regulation
Kaplan, C. D., & Kaplan, J. (2009) · Chemical Reviews · doi:10.1021/cr9001676 · Cited by 275 · see citing works
Fibroblast Growth Factor 23 and Inflammation in CKD
Mendoza, J. M., Isakova, T., Ricardo, A. C., Xie, H., Navaneethan, S. D., Anderson, A. H., Bazzano, L., Xie, D., Kretzler, M., Nessel, L. C., et al. (2012) · Clinical Journal of the American Society of Nephrology · doi:10.2215/cjn.13281211 · Cited by 270 · see citing works
Sasu, B. J., Cooke, K. S., Arvedson, T. L., Plewa, C., Ellison, A. R., Sheng, J., Winters, A., Juan, T., Li, H., Begley, C. G., et al. (2010) · Blood · doi:10.1182/blood-2009-09-245977 · Cited by 251 · see citing works
Iron overload and toxicity: the hidden risk of multiple blood transfusions
Shander, A., Cappellini, M. D., & Goodnough, L. T. (2009) · Vox Sanguinis · doi:10.1111/j.1423-0410.2009.01207.x · Cited by 236 · see citing works
Molecular Mechanisms of Hepcidin Regulation: Implications for the Anemia of CKD
Babitt, J. L., & Lin, H. Y.-F. (2010) · American Journal of Kidney Diseases · doi:10.1053/j.ajkd.2009.12.030 · Cited by 236 · see citing works
“is.(15,16) A small peptide hormone of 25 amino cids, hepcidin is produced and secreted predomiantly by hepatocytes, circulates in the bloodtream, and is excreted by the kidneys.”
BackgroundRole of the hypoxia inducible factors HIF in iron metabolism
Peyssonnaux, C., Nizet, V., & Johnson, R. S. (2008) · Cell Cycle · doi:10.4161/cc.7.1.5145 · Cited by 217 · see citing works
Sierra‐Filardi, E., Vega, M. A., Sánchez‐Mateos, P., Corbí, A. L., & Puig‐Kröger, A. (2010) · Immunobiology · doi:10.1016/j.imbio.2010.05.020 · Cited by 204 · see citing works
Advances in Quantitative Hepcidin Measurements by Time-of-Flight Mass Spectrometry
Swinkels, D. W., Girelli, D., Laarakkers, C. M., Kroot, J. J., Campostrini, N., Kemna, E., & Tjalsma, H. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002706 · Cited by 202 · see citing works
“g003 especially in anemias that are associated with renal diseases where hepcidin is predicted to be an important contributor [34].”
BackgroundAshby, D. R., Gale, D. P., Busbridge, M., Murphy, K. G., Duncan, N. D., Cairns, T. D., Taube, D. H., Bloom, S. R., Tam, F. W. K., Chapman, R., et al. (2010) · Haematologica · doi:10.3324/haematol.2009.013136 · Cited by 191 · see citing works
Transferrin and ferritin response to bacterial infection: The role of the liver and brain in fish
Neves, J. V., Wilson, J. M., & Rodrigues, P. (2009) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2009.02.001 · Cited by 175 · see citing works
Ho, J., Lucy, M., Krokhin, O. V., HayGlass, K. T., PASCOE, E. A., Darroch, G., Rush, D. N., Nickerson, P. W., Rigatto, C., & Reslerova, M. (2008) · American Journal of Kidney Diseases · doi:10.1053/j.ajkd.2008.10.037 · Cited by 173 · see citing works
Nramp1 promotes efficient macrophage recycling of iron following erythrophagocytosis in vivo
Soe-Lin, S., Apte, S. S., Andriopoulos, B., Andrews, M. C., Schranzhofer, M., Kahawita, T., Garcia-Santos, D., & Ponka, P. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0900808106 · Cited by 167 · see citing works
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HIF‐prolyl hydroxylases as therapeutic targets in erythropoiesis and iron metabolism
Haase, V. H. (2017) · Hemodialysis International · doi:10.1111/hdi.12567 · Cited by 161 · see citing works
Liu, W., Zhang, S.-P., Nekhai, S., & Liu, S.-J. (2020) · Current Clinical Microbiology Reports · doi:10.1007/s40588-020-00140-w · Cited by 135 · see citing works
The genetics of essential metal homeostasis during development
Kambe, T., Weaver, B. P., & Andrews, G. K. (2008) · genesis · doi:10.1002/dvg.20382 · Cited by 136 · see citing works
“Ferroportin transporter activity is downregulated by the binding of the peptide hormone hepcidin which causes phosphorylation of ferroportin and its subsequent internalization, ubiquitination, and degradation (DeDomenico et al., 2008; Ganz, 2007).”
BackgroundZhang, Z., Zhang, F., Guo, X., An, P., Tao, Y., & Wang, F. (2012) · Hepatology · doi:10.1002/hep.25746 · Cited by 123 · see citing works
“Because both iron deficiency and iron overload are harmful to cells and tissues, iron balance is meticulously regulated to meet the body’s iron requirements and to avoid the toxicity associated with iron excess.(2,3) The liver has first-pass access to dietary nutrients and can readily take up an amount of circulating…”
BackgroundEstimating tissue iron burden: current status and future prospects
Wood, J. C. (2015) · British Journal of Haematology · doi:10.1111/bjh.13374 · Cited by 130 · see citing works
“Although a formal review of the proteins and signalling mechanisms involved in somatic iron regulation is beyond the scope of this review (for more comprehensive discussion, see Ganz, 2007), some understanding is useful to place iron monitoring in proper context.”
InfluentialHepcidin, the hormone of iron metabolism, is bound specifically to α-2-macroglobulin in blood
Pešlová, G., Petrák, J., Kuželová, K., Hrdý, I., Halada, P., Kuchel, P. W., Soe-Lin, S., Ponka, P., Šuťák, R., Becker, E., et al. (2009) · Blood · doi:10.1182/blood-2009-01-201590 · Cited by 127 · see citing works
Current approach to hemochromatosis
Brissot, P., Troadec, M., Bardou‐Jacquet, E., Lan, C. L., Jouanolle, A., Deugnier, Y., & Loréal, O. (2008) · Blood Reviews · doi:10.1016/j.blre.2008.03.001 · Cited by 129 · see citing works
Maternal serum hepcidin is low at term and independent of cord blood iron status
Rehu, M., Punnonen, K. R. A., Ostland, V. E., Heinonen, S. T., Westerman, M. E., Pulkki, K. J., & Sankilampi, U. (2010) · European Journal Of Haematology · doi:10.1111/j.1600-0609.2010.01479.x · Cited by 122 · see citing works
“Hepcidin inhibits iron efflux from the cells by degrading its exporter ferroportin, which is the sole known iron transporter in humans (7, 8).”
BackgroundAnemia After Bariatric Surgery: More Than Just Iron Deficiency
von Drygalski, A., & Andris, D. A. (2009) · Nutrition in Clinical Practice · doi:10.1177/0884533609332174 · Cited by 121 · see citing works
“The recently discovered peptide hepcidin is responsible for blocking intestinal iron absorption as well as iron release from stores during inflammation.(75) Hepcidin is up-regulated by interleukin-6, which together with other inflammatory cytokines and proteins like tumor necrosis factor-α, von Willebrand factor, C-re…”
BackgroundInhibition of fibroblast growth factor 23 (FGF23) signaling rescues renal anemia
Agoro, R., Montagna, A., Goetz, R. M., Aligbe, O., Singh, G. K., Coe, L. M., Mohammadi, M., Rivella, S., & Sitara, D. (2018) · The FASEB Journal · doi:10.1096/fj.201700667r · Cited by 117 · see citing works
“High hepcidin concentrations result in inhibition of intestinal iron absorption as well as sequestration of iron in macrophages and hepatocytes, thereby decreasing serum iron levels (38, 57).”
BackgroundErythropoietin and erythropoiesis
Fried, W. I. (2009) · Experimental Hematology · doi:10.1016/j.exphem.2009.05.010 · Cited by 115 · see citing works
“Increased hepcidin results in decreased iron absorption and decreased release of iron from the macrophages and visa versa [63].”
BackgroundTruksa, J., Lee, P. L., & Beutler, E. (2008) · Blood · doi:10.1182/blood-2008-05-160184 · Cited by 104 · see citing works
Mitochondrial Mayhem: The Mitochondrion as a Modulator of Iron Metabolism and Its Role in Disease
Huang, M. L.-H., Lane, D. J. R., & Richardson, D. R. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2011.3921 · Cited by 103 · see citing works
“However, at the systemic level, iron homeostasis is primarily regulated by the ‘‘hormone of iron metabolism,’’ hepcidin, which acts through the modulation of Fpn1 expression (52).”
Troutt, J. S., Rudling, M., Persson, L., Ståhle, L., Angelin, B., Butterfield, A. M., Schade, A. E., Cao, G., & Konrad, R. J. (2012) · Clinical Chemistry · doi:10.1373/clinchem.2012.186866 · Cited by 100 · see citing works
The Role of Fibroblast Growth Factor 23 in Inflammation and Anemia
Czaya, B. A., & Faul, C. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20174195 · Cited by 99 · see citing works
“Once digested by macrophages, iron is then recovered by the actions of heme oxygenase [270,273].”
BackgroundInfluentialIron and the liver: Update 2008
Deugnier, Y., Brissot, P., & Loréal, O. (2008) · Journal of Hepatology · doi:10.1016/j.jhep.2008.01.014 · Cited by 95 · see citing works
“iron egress from cells, especially enterocytes, macrophages and placenta cells [6–8] (Fig.”
BackgroundGender-related variations in iron metabolism and liver diseases
Harrison-Findik, D. D. (2010) · World Journal of Hepatology · doi:10.4254/wjh.v2.i8.302 · Cited by 98 · see citing works
Awan, A. A., Walther, C. P., Richardson, P., Shah, M., Winkelmayer, W. C., & Navaneethan, S. D. (2019) · Nephrology Dialysis Transplantation · doi:10.1093/ndt/gfz192 · Cited by 93 · see citing works
Grayfer, L., Hodgkinson, J. W., & Belosevic, M. (2013) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2013.08.003 · Cited by 93 · see citing works
“Aside from the above iron deprivation strategies, a major mechanism by which macrophages regulate extracellular iron concentrations centers on the hepcidin peptide hormone binding to the only known cellular iron exporter, ferroportin-1 (Ganz, 2007; Ganz and Nemeth, 2006).”
BackgroundTessitore, N., Girelli, D., Campostrini, N., Bedogna, V., Solero, G. P., Castagna, A., Melilli, E., Mantovani, W., MATTEIS, G. D., Olivieri, O., et al. (2010) · Nephrology Dialysis Transplantation · doi:10.1093/ndt/gfq321 · Cited by 89 · see citing works
“Since Hep-25 blocks iron release from the macrophages, its increase may contribute to the disordered iron homeostasis and ESA resistance in uraemia by limiting iron availability for erythropoiesis [14].”
BackgroundVaziri, N. D., & Zhou, X. (2008) · Nephrology Dialysis Transplantation · doi:10.1093/ndt/gfn601 · Cited by 85 · see citing works
Positive Iron Balance in Chronic Kidney Disease: How Much is Too Much and How to Tell?
Wish, J. B., Aronoff, G. R., Bacon, B. R., Brugnara, C., Eckardt, K., Ganz, T., Macdougall, I. C., Núñez, J. E., Perahia, A. J., & Wood, J. C. (2018) · American Journal of Nephrology · doi:10.1159/000486968 · Cited by 87 · see citing works
Coordination chemistry and biology of chelators for the treatment of iron overload disorders.
Bernhardt, P. (2007) · Dalton Transactions · doi:10.1039/b708133b · Cited by 79 · see citing works
Altered Iron Metabolism Is Part of the Choroid Plexus Response to Peripheral Inflammation
Marques, F., Falcão, A. M., Sousa, J. C., Coppola, G., Geschwind, D. H., Sousa, N., Correia‐Neves, M., & Palha, J. A. (2009) · Endocrinology · doi:10.1210/en.2008-1610 · Cited by 84 · see citing works
Pharmacokinetics of Anti-hepcidin Monoclonal Antibody Ab 12B9m and Hepcidin in Cynomolgus Monkeys
Xiao, J. J., Krzyżański, W., Wang, Y., Li, H., Rose, M. J., Ma, M., Wu, Y., Hinkle, B., & Ruixo, J. J. P. (2010) · The AAPS Journal · doi:10.1208/s12248-010-9222-0 · Cited by 80 · see citing works
“Hepcidin, a hormone peptide of 25 amino acids synthesized by the liver, binds to ferroportin, causes ferroportin internalization and degradation, and thereby blocks the iron export (5,6).”
Backgroundvon Drygalski, A., Andris, D. A., Nuttleman, P. R., Jackson, S., Klein, J. P., & Wallace, J. R. (2010) · Surgery for Obesity and Related Diseases · doi:10.1016/j.soard.2010.04.008 · Cited by 80 · see citing works
Pishchany, G., Dickey, S. E., & Skaar, E. P. (2009) · Infection and Immunity · doi:10.1128/iai.01531-08 · Cited by 77 · see citing works
“This idea is supported by the fact that the liver is the major storage site for iron in vertebrates (17, 18).”
BackgroundHutchinson, C. (2016) · European Journal of Nutrition · doi:10.1007/s00394-016-1155-7 · Cited by 76 · see citing works
“IL-6 has been shown to play a primary role in the production and release of hepcidin [77–79], which is predominantly produced by the liver, but also by other organs including adipose tissue [80, 81].”
BackgroundUremic Toxins Affect Erythropoiesis during the Course of Chronic Kidney Disease: A Review
Hamza, E., Metzinger, L., & Meuth, V. M. (2020) · Cells · doi:10.3390/cells9092039 · Cited by 77 · see citing works
Solstad, T., LARSEN, A., Seppola, M., & JORGENSEN, T. (2008) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2008.05.013 · Cited by 77 · see citing works
Uehata, T., Tomosugi, N., Shoji, T., Sakaguchi, Y., Suzuki, A., Kaneko, T., Okada, N., Yamamoto, R., Nagasawa, Y., Kato, K., et al. (2011) · Nephrology Dialysis Transplantation · doi:10.1093/ndt/gfr431 · Cited by 75 · see citing works
Iron, oxidative stress and the example of solar ultraviolet a radiation.
Aroun, A., Zhong, J. L., Tyrrell, R. M., & Pourzand, C. (2012) · Photochemical & Photobiological Sciences · doi:10.1039/c1pp05204g · Cited by 74 · see citing works
Akizawa, T., Nangaku, M., Yamaguchi, T., Arai, M., Koretomo, R., Matsui, A., & Hirakata, H. (2019) · American Journal of Nephrology · doi:10.1159/000496929 · Cited by 74 · see citing works
Shander, A., & Sazama, K. J. (2010) · Transfusion · doi:10.1111/j.1537-2995.2009.02551.x · Cited by 74 · see citing works
“The peptide hormone hepcidin inhibits the ferroportin-mediated release of ferric iron from enterocytes by binding to ferroportin and inducing its lysosomal degradation.(4,11) In contrast to the expression of DMT1, which increases in states of iron deficiency and decreases in iron overload, expression of hepcidin decre…”
BackgroundSham, R. L., Phatak, P. D., Nemeth, E., & Ganz, T. (2009) · Blood · doi:10.1182/blood-2009-04-216226 · Cited by 74 · see citing works
Iron-Deficiency Anemia in CKD: A Narrative Review for the Kidney Care Team
Hain, D. J., Bednarski, D., Cahill, M. L., Dix, A., Foote, B. S., Haras, M. S., Pace, R. C., & Gutiérrez, O. M. (2023) · Kidney Medicine · doi:10.1016/j.xkme.2023.100677 · Cited by 89 · see citing works
“phagocytosis, ultimately recycling their iron content, which is used either for the production of new RBCs or stored for future use.(6,20,23) The recycling of RBCs in the spleen and liver provides most of the body’s iron (2025 mg/d),whereas dietary absorption provides only 12 mg/d of iron.”
BackgroundMethodHepcidin induces HIV-1 transcription inhibited by ferroportin
Xu, M., Kashanchi, F., Foster, A., Rotimi, J., Turner, W., Gordeuk, V. R., & Nekhai, S. A. (2010) · Retrovirology · doi:10.1186/1742-4690-7-104 · Cited by 70 · see citing works
“Hepcidin binds to ferroportin, and this leads to ferroportin internalization and degradation by lysosomes [1].”
Diehm, N., Benenati, J. F., Becker, G. J., Quesada, R., Tsoukas, A. I., Katzen, B. T., & Kovacs, M. E. (2007) · Journal of Vascular Surgery · doi:10.1016/j.jvs.2007.06.027 · Cited by 67 · see citing works
“In inflammatory states, increased hepcidin concentrations cause iron sequestration in macrophages, resulting in hypoferremia and anemia.(21,23,29,47) Furthermore, proinflammatory cytokines induce hypoferremia by modulating macrophage iron metabolism via induction of ferritin biosynthesis.”
BackgroundSmith, K. D. (2007) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2007.07.003 · Cited by 67 · see citing works
“Prokaryotes and eukaryotes have evolved a multitude of exquisite biological systems to acquire, transport and store this molecule (Ganz, 2007; Wandersman & Delepelaire, 2004).”
BackgroundWagner, M., Alam, A., Zimmermann, J., Rauh, K., Batzner, A., Raff, U., Wanner, C., & Schramm, L. (2011) · Clinical Journal of the American Society of Nephrology · doi:10.2215/cjn.00380111 · Cited by 64 · see citing works
“We could not separate iron deficiency from iron dysregulation under the influence of inflammation, because we did not have measurements of soluble transferrin receptor (11) or hepcidin (10).”
BackgroundIron transport & homeostasis mechanisms: their role in health & disease.
Nadadur, S. S., Srirama, K., & Mudipalli, A. (2008) · PubMed · Cited by 64 · see citing works
Ward, D. G., Roberts, K., Stonelake, P. S., Goon, P. K. Y., Zampronio, C. G., Martin, A., Johnson, P. J., Iqbal, T. H., & Tselepis, C. (2008) · Proteome Science · doi:10.1186/1477-5956-6-28 · Cited by 62 · see citing works
“Background Hepcidin, a 25-residue peptide hormone, is a key regulator of iron homeostasis [1-3].”
BackgroundTherapeutic targeting of the HIF oxygen-sensing pathway: Lessons learned from clinical studies
Haase, V. H. (2017) · Experimental Cell Research · doi:10.1016/j.yexcr.2017.05.004 · Cited by 64 · see citing works
Sofroniadou, S., & Goldsmith, D. (2011) · Drug Safety · doi:10.2165/11585040-000000000-00000 · Cited by 60 · see citing works
A dual-monoclonal sandwich ELISA specific for hepcidin-25
Butterfield, A. M., Luan, P., Witcher, D. R., Manetta, J., Murphy, A. T., Wroblewski, V. J., & Konrad, R. J. (2010) · Clinical Chemistry · doi:10.1373/clinchem.2010.151522 · Cited by 59 · see citing works
The ins and outs of mitochondrial iron-loading: the metabolic defect in Friedreich’s ataxia
Richardson, D. R., Huang, M. L. H., Whitnall, M., Becker, E., Ponka, P., & Rahmanto, Y. S. (2009) · Journal of Molecular Medicine · doi:10.1007/s00109-009-0565-x · Cited by 59 · see citing works
“Since Fpn1 is downregulated by decreased cytosolic iron [32], this again supports the idea that the cardiomyocyte was responding to cytosolic iron-deficiency.”
BackgroundInfluentialFrataxin and the molecular mechanism of mitochondrial iron-loading in Friedreich's ataxia
Chiang, S., Kovačević, Ž., Sahni, S., Lane, D. J. R., Merlot, A. M., Kalinowski, D. S., Huang, M. L. H., & Richardson, D. R. (2016) · Clinical Science · doi:10.1042/cs20160072 · Cited by 58 · see citing works
Iron homeostasis and anemia markers in early breast cancer
Lamy, P., Durigova, A., & Jacot, W. (2014) · Clinica Chimica Acta · doi:10.1016/j.cca.2014.04.011 · Cited by 57 · see citing works
Structure–activity relationship of human liver-expressed antimicrobial peptide 2
Hocquellet, A., Odaert, B., Cabanne, C., Noubhani, A., Dieryck, W., Joucla, G., Sénéchal, C. L., Milenkov, M., Chaignepain, S., Schmitter, J., et al. (2009) · Peptides · doi:10.1016/j.peptides.2009.10.006 · Cited by 56 · see citing works
Ferristatin II Promotes Degradation of Transferrin Receptor-1 In Vitro and In Vivo
Byrne, S. L., Buckett, P. D., Kim, J., Luo, F., Sanford, J. C., Chen, J., Enns, C. A., & Wessling‐Resnick, M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0070199 · Cited by 54 · see citing works
“Hepcidin interacts with the iron exporter ferroportin to induce its lysosomal degradation, thereby blocking dietary absorption [35] and release of iron stores [69].”
Protein moonlighting in iron metabolism: glyceraldehyde-3-phosphate dehydrogenase (GAPDH)
Boradia, V. M., Raje, M., & Raje, C. I. (2014) · Biochemical Society Transactions · doi:10.1042/bst20140220 · Cited by 53 · see citing works
Hepcidin and inflammatory bowel disease: dual role in host defence and iron homoeostasis
Arnold, J., Sangwaiya, A., Bhatkal, B., Geoghegan, F., & Busbridge, M. (2009) · European Journal of Gastroenterology & Hepatology · doi:10.1097/meg.0b013e32830e2885 · Cited by 54 · see citing works
Vilela, E. M., Bastos, J. A., Fernandes, N. M. D. S., Ferreira, A. P., Chaoubah, A., & Bastos, M. G. (2011) · Clinics · doi:10.1590/s1807-59322011000400022 · Cited by 54 · see citing works
“The target for serum hepcidin is the iron exporter ferroportin 1, which is found in the plasma membranes of most body cells and is found at high concentrations in duodenal enterocytes, macrophages, and hepatocytes.(3,8) The gene that encodes hepcidin is regulated by iron load, anemia, and, in particular, chronic infla…”
BackgroundThe Role of Iron in Alcohol-Mediated Hepatocarcinogenesis
Mueller, S., & Rausch, V. (2014) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-09614-8_6 · Cited by 51 · see citing works
[Iron deficiency and overload. Implications in oxidative stress and cardiovascular health].
Toxqui, L., Piero, A. D., Courtois, V., Bastida, S., Sánchez-Muniz, F. J., & Vaquero, M. P. (2010) · PubMed · doi:10.3305/nh.2010.25.3.4583 · Cited by 50 · see citing works
Not all DMT1 mutations lead to iron overload
Blanco, E., Kannengiesser, C., Grandchamp, B., Tasso, M., & Beaumont, C. (2009) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2009.05.003 · Cited by 48 · see citing works
Sundramoorthy, A. K., Premkumar, B. S., & Gunasekaran, S. (2015) · ACS Sensors · doi:10.1021/acssensors.5b00172 · Cited by 49 · see citing works
Moonlighting cell surface GAPDH recruits Apo Transferrin to effect iron egress from mammalian cells
Sheokand, N., Malhotra, H., Kumar, S., Tillu, V. A., Chauhan, A. S., Raje, C. I., & Raje, M. (2014) · Journal of Cell Science · doi:10.1242/jcs.154005 · Cited by 47 · see citing works
Kakhlon, O., Breuer, W. V., Münnich, A., & Cabantchik, Z. I. (2010) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/y09-128 · Cited by 48 · see citing works
Haase‐Fielitz, A., Mertens, P. R., Plaß, M., Kuppe, H., Hetzer, R., Westerman, M. E., Ostland, V. E., Prowle, J. R., Bellomo, R., & Haase, M. (2011) · Critical Care · doi:10.1186/cc10339 · Cited by 46 · see citing works
“The hepcidin gene is regulated by iron loading, hypoxia or inflammation [10-12], and its protein is produced by liver and kidney cells [13].”
BackgroundNon-HFE hemochromatosis: Pathophysiological and diagnostic aspects
Bardou‐Jacquet, E., Ali, Z. B., Beaumont-Epinette, M.-P., Loréal, O., Jouanolle, A., & Brissot, P. (2013) · Clinics and Research in Hepatology and Gastroenterology · doi:10.1016/j.clinre.2013.11.003 · Cited by 45 · see citing works
Serum hepcidin but not prohepcidin may be an effective marker for anemia of inflammation (AI)
Sasu, B. J., Li, H., Rose, M. J., Arvedson, T. L., Doellgast, G., & Molineux, G. (2010) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2010.07.013 · Cited by 43 · see citing works
Jiang, X., Gao, M., Chen, Y., Liu, J. L., Qi, S., Ma, J., Zhang, Z., & Xu, Y. H. (2016) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2016.02.005 · Cited by 43 · see citing works
Gu, L., Fu, R., Chen, P., Du, N., Chen, S., Mao, D., Chen, B., Mao, F., Khadaroo, P. A., & Jin, Q. (2020) · Obesity Surgery · doi:10.1007/s11695-020-04488-2 · Cited by 44 · see citing works
A fluorescent probe for the Fe3+ ion pool in endoplasmic reticulum in liver cells
Lee, M. H., Lee, H.-Y., Chang, M. J., Kim, H. S., Kang, C., & Kim, J. S. (2016) · Dyes and Pigments · doi:10.1016/j.dyepig.2016.03.032 · Cited by 42 · see citing works
Iron Deficiency, Zinc, Magnesium, Vitamin Deficiencies in Crohn's Disease: Substitute or Not?
Kruis, W., & Nguyen, G. (2016) · Digestive Diseases · doi:10.1159/000443012 · Cited by 42 · see citing works
Troutt, J. S., Butterfield, A. M., & Konrad, R. J. (2013) · Journal of Clinical Laboratory Analysis · doi:10.1002/jcla.21634 · Cited by 41 · see citing works
“The 25-amino acid active form of hepcidin (hepcidin-25) is the master hormone regulating iron homeostasis in humans (1, 2) Hepcidin-25 is synthesized and secreted by the liver and controls dietary iron absorption and release of hepatic and macrophage iron stores by binding directly to the iron transport protein ferrop…”
BackgroundAnemia and anemia correction: surrogate markers or causes of morbidity in chronic kidney disease?
Vaziri, N. D. (2008) · Nature Reviews Nephrology · doi:10.1038/ncpneph0847 · Cited by 41 · see citing works
“As mentioned above, there are several mechanisms by which oxidative stress and inflammation cause anemia in patients with CKD”
BackgroundWagner, M., Ashby, D. R., Kurtz, C. B., Alam, A., Busbridge, M., Raff, U., Zimmermann, J., Heuschmann, P. U., Wanner, C., & Schramm, L. (2015) · PLoS ONE · doi:10.1371/journal.pone.0123072 · Cited by 40 · see citing works
“Hepcidin is the key-hormone of iron metabolism in ACD [14] and inflammatory processes are not only a cause, but also a symptom of iron dysregulation [30–32].”
BackgroundInfluentialRole of Cellular Iron and Oxygen in the Regulation of HIV-1 Infection
Nekhai, S. A., Kumari, N., & Dhawan, S. (2013) · Future Virology · doi:10.2217/fvl.13.6 · Cited by 40 · see citing works
Cytochrome P450 1B1: A Key Regulator of Ocular Iron Homeostasis and Oxidative Stress
Song, Y., Annalora, A. J., Marcus, C. B., Jefcoate, C. R. E., Sorenson, C. M., & Sheibani, N. (2022) · Cells · doi:10.3390/cells11192930 · Cited by 42 · see citing works
“Ferroportin is the only known cellular iron efflux transporter in vertebrates, and it is typically expressed in iron-exporting cells, including enterocytes, macrophages, and hepatocytes [59].”
BackgroundA review of select minerals influencing the haematopoietic process
de Oliveira, D. C., Nogueira‐Pedro, A., Santos, E. W., Hastreiter, A. A., da Silva, G. B., Borelli, P., & Fock, R. A. (2018) · Nutrition Research Reviews · doi:10.1017/s0954422418000112 · Cited by 38 · see citing works
“playing high uptake rates for the non-transferrin-bound Fe present when the Fe exceeds the Fe total binding capacity of transferrin((20,21)) (Fig.”
BackgroundValerio, L. G. (2007) · Toxicology Mechanisms and Methods · doi:10.1080/15376510701556690 · Cited by 37 · see citing works
“In human diseases of iron overload, hepcidin thus far appears to be the etiologic factor in most forms of hemochromatosis (Nemeth and Ganz 2006; Ganz 2007), either through mutations in the gene itself or due to mutations in other molecular factors influencing the synthesis of the hormone.”
BackgroundHepcidin in Trauma: Linking Injury, Inflammation, and Anemia
Sihler, K. C., Raghavendran, K., Westerman, M. E., Ye, W., & Napolitano, L. M. (2010) · The Journal of Trauma: Injury, Infection, and Critical Care · doi:10.1097/ta.0b013e3181f066d5 · Cited by 37 · see citing works
Valenzuela‐Muñoz, V., Valenzuela‐Miranda, D., Gonçalves, A. T., Novoa, B., Figueras, A. J., & Gallardo‐Escárate, C. (2020) · Aquaculture · doi:10.1016/j.aquaculture.2020.735058 · Cited by 36 · see citing works
Vitamin C Affects the Expression of Hepcidin and Erythropoietin Receptor in HepG2 Cells
Chiu, P., Ko, S., & Chang, C. (2012) · Journal of Renal Nutrition · doi:10.1053/j.jrn.2011.09.007 · Cited by 34 · see citing works
“Inversely, an iron-rich environment, presence of inflammation, or renal failure will act as an ‘‘iron signal’’ to augment expression of hepcidin.(4,6) Larger EPO doses and parenteral vitamin C have been used to improve renal anemia in uremic patients.”
Background
- Authors
- Ganz, T.
- Affiliations
- University of California, Los Angeles (US)
- Corresponding author
- Ganz, Tomas
- ORCID
- Ganz, Tomas
- Venue
- Journal of the American Society of Nephrology
- Published
- 2007-02
- Volume
- 18
- Issue
- 2
- Pages
- 394-400
- ISSN
- 1046-6673 (ISSN-L)
- OpenAlex
- W2120359196
- Cited by
- 353
- References
- 58
- Citations by year
- 2026: 1 · 2025: 4 · 2024: 8 · 2023: 9 · 2022: 15 · 2021: 30 · 2020: 13 · 2019: 17 · 2018: 17 · 2017: 12 · 2016: 19 · 2015: 22 · 2014: 17 · 2013: 22 · 2012: 18
- FWCI
- 23.00
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of the American Society of Nephrology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Heart, Lung, and Blood Institute (R01HL046809, HL46809)
- Topics
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Health Sciences › Medicine › Hematology › Erythropoietin and Anemia Treatment
- Health Sciences › Medicine › Pulmonary and Respiratory Medicine › Ferroptosis and cancer prognosis
- Keywords
- hepcidin, iron transport, ferroportin, iron homeostasis, dietary iron absorption, iron storage, erythropoiesis, inflammation, anemia of chronic disease, iron overload, anemia of chronic kidney disease
- MeSH terms
- Ferroportin, Anemia, Biological Transport, Bone and Bones, Homeostasis, Humans, Inflammation, Intestinal Absorption, Iron, Kidney Diseases, Kinetics, Liver, Iron Overload, Antimicrobial Cationic Peptides, Cation Transport Proteins, Hepcidins
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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