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The gene encoding the iron regulatory peptide hepcidin is regulated by anemia, hypoxia, and inflammation
Open accessAbstract
The present study was aimed at determining whether hepcidin, a recently identified peptide involved in iron metabolism, plays a role in conditions associated with both iron overload and iron deficiency.Hepcidin mRNA levels were assessed in two models of anemia, acute hemolysis provoked by phenylhydrazine and bleeding provoked by repeated phlebotomies.Hepcidin response to hypoxia was also studied, both ex vivo, in human hepatoma cells, and in vivo.Anemia and hypoxia were associated with a dramatic decrease in liver hepcidin gene expression, which may account for the increase in iron release from reticuloendothelial cells and increase in iron absorption frequently observed in these situations.A single injection of turpentine for 16 hours induced a sixfold increase in liver hepcidin mRNA levels and a twofold decrease in serum iron.The hyposideremic effect of turpentine was completely blunted in hepcidin-deficient mice, revealing hepcidin participation in anemia of inflammatory states.These modifications of hepcidin gene expression further suggest a key role for hepcidin in iron homeostasis under various pathophysiological conditions, which may support the pharmaceutical use of hepcidin agonists and antagonists in various iron homeostasis disorders.
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In the citing paper
“the turpentine-induced hypoferremia was not observed in hepcidin-deficient mice (8), demonstrating that hepcidin is required for iron sequestration during inflammatory conditions”
From IL-6 mediates hypoferremia of inflammation by inducing the synthesis of the iron regulatory hormone hepcidin (2004) · cites this paper as [8]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“hepcidin synthesis is regulated by dietary iron and iron stores, as well as by tissue oxygenation”
From IL-6 mediates hypoferremia of inflammation by inducing the synthesis of the iron regulatory hormone hepcidin (2004) · cites this paper as [8]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“decreased in mice with anemia caused by bleeding or hemolysis or in mice with hypoxemia due to decreased ambient oxygen”
From IL-6 mediates hypoferremia of inflammation by inducing the synthesis of the iron regulatory hormone hepcidin (2004) · cites this paper as [8]
The cited source says what the claim attributes to it.
In the citing paper
“injections of turpentine increased hepcidin mRNA”
From IL-6 mediates hypoferremia of inflammation by inducing the synthesis of the iron regulatory hormone hepcidin (2004) · cites this paper as [8]
The cited source says what the claim attributes to it.
In the citing paper
“decreased serum iron”
From IL-6 mediates hypoferremia of inflammation by inducing the synthesis of the iron regulatory hormone hepcidin (2004) · cites this paper as [8]
In the citing paper
“Infection and inflammation induce hepcidin production, driving a decrease in plasma iron concentrations by inhibiting the absorption of iron and promoting the sequestration of iron in macrophages.”
From Iron homeostasis in host defence and inflammation (2015) · cites this paper as [26]
In the citing paper
“The increase in hepcidin secretion in response to infectious or inflammatory stimuli is responsible for the characteristic hypoferraemia of inflammation26,27, which develops within a few hours of a systemic infection or following injection of microbial components or certain cytokines.”
From Iron homeostasis in host defence and inflammation (2015) · cites this paper as [26]
In the citing paper
“Strikingly, anaemia and anoxia both suppress hepcidin production [245,339,340] (Fig 3), such that just while superoxide production is being enhanced by the anoxia there is more iron being absorbed from the intestine and effluxed into the circulation.”
In the citing paper
“A common mechanism of hypoferremia of inflammation is a cytokine-driven increase in hepcidin [15] that downregulates ferroportin and thereby decreases iron flow into extracellular fluid from all its sources.”
From Iron and infection (2018) · cites this paper as [15]
In the citing paper
“Thus, under the influence of increased concentrations of hepcidin, recycled iron is retained in macrophages of the liver and the spleen, and iron absorption is decreased.”
From Iron and infection (2018) · cites this paper as [15]
In the citing paper
“Conversely, hepcidin expression is inhibited by hypoxia and erythropoiesis [11,12].”
From Hepcidin and Host Defense against Infectious Diseases (2015) · cites this paper as [11]
In the citing paper
“In addition, the amount of hepcidin mRNA in liver cells is decreased in response to hypoxia and ineffective erythropoiesis (overlapping with the response to iron deficiency) 99,105 and induced in response to treatment with lipopolysaccharide or by inflammation of other etiologies.92,99”
From Forging a field: the golden age of iron biology. (2008) · cites this paper as [99]
In the citing paper
“Initially, murine hepcidin mRNA was shown to be elevated in response to iron overload 92 and decreased in response to iron deficiency.99,100”
From Forging a field: the golden age of iron biology. (2008) · cites this paper as [99]
In the citing paper
“Experimental studies in cultured cells, in animal models and in human subjects have established that hepcidin production is O2-sensitive and involves the HIF pathway.”
From Regulation of erythropoiesis by hypoxia-inducible factors (2013) · cites this paper as [192]
In the citing paper
“A study that examined postmortem unfixed frozen brain sections from elderly normal or PD-affected individuals showed that individual neurons from brains of individuals with PD had significantly elevated iron concentrations (220).”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [220]
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Citations
Cites
Hepcidin, 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
Pigeon, 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
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
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
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
Self-citationRegulators of iron balance in humans [see comments]
Finch, C. (1994) · Blood · doi:10.1182/blood.v84.6.1697.1697 · Cited by 455
Milanini, J., Viñals, F., Pouysségur, J., & Pagès, G. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.29.18165 · Cited by 315
Iron metabolism in the erythrophagocytosing Kupffer cell
Kondo, H. G., Saito, K., Grasso, J. P., & Aisen, P. (1988) · Hepatology · doi:10.1002/hep.1840080108 · Cited by 125
Kelley‐Loughnane, N., Sabla, G. E., Ley, C. A., Aronow, B. J., & Bezerra, J. A. (2002) · Hepatology · doi:10.1053/jhep.2002.31351 · Cited by 77
Raja, K. B., Simpson, R. J., Pippard, M. J., & Peters, T. J. (1988) · British Journal of Haematology · doi:10.1111/j.1365-2141.1988.tb04217.x · Cited by 72
Flagged first, then by citations
Research works printed but not linked: 3
- Raja, 1990, Int J Exp Pathol, 71, 785
- Mazure, 2002, Cancer Res, 62, 1158
- Torrance, 1980, Meth Hematol, 1, 90
Cited by
Sorted by citations
Items 601–700 of 1,019
Association of Serum Hepcidin Levels with Aerobic and Resistance Exercise: A Systematic Review
Larsuphrom, P., & Latunde-Dada, G. O. (2021) · Nutrients · doi:10.3390/nu13020393 · Cited by 37
Exogenous BMP7 corrects plasma iron overload and bone loss in Bmp6-/- mice
Pauk, M., Grgurević, L., Brkljačić, J. M., Kufner, V., Bordukalo-Nikšić, T., Grabušić, K., Razdorov, G., Rogić, D., Žuvić, M., Oppermann, H., et al. (2014) · International Orthopaedics · doi:10.1007/s00264-014-2550-4 · Cited by 33
Truksa, J., Lee, P. L., & Beutler, E. (2007) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2007.06.014 · Cited by 33
Kayali, Z., Ranguelov, R. D., Mitros, F. A., SHUFELT, C. L., Elmi, F., Rayhill, S. C., Schmidt, W. N., & Brown, K. E. (2005) · Liver International · doi:10.1111/j.1478-3231.2005.01022.x · Cited by 33
The inhibitory effect of environmental ammonia on Danio rerio LPS induced acute phase response
Gonçalves, A. F., Páscoa, I., Neves, J. V., Coimbra, J., Vijayan, M. M., Rodrigues, P., & Wilson, J. M. (2011) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2011.04.008 · Cited by 33
BMPER Protein Is a Negative Regulator of Hepcidin and Is Up-regulated in Hypotransferrinemic Mice
Patel, N., Masaratana, P., Díaz‐Castro, J., Latunde-Dada, G. O., Qureshi, A., Lockyer, P. P., Jacob, M., Arno, M. J., Matak, P., Mitry, R. R., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.310789 · Cited by 33
Liver iron modulates hepcidin expression during chronically elevated erythropoiesis in mice
Díaz, V., Gammella, E., Recalcati, S., Santambrogio, P., Naldi, A. M., Vogel, J., Gassmann, M., & Cairo, G. (2013) · Hepatology · doi:10.1002/hep.26550 · Cited by 33
Exogenous iron increases hemoglobin in β–thalassemic mice
Ginzburg, Y. Z., Rybicki, A. C., Suzuka, S. M., Hall, C. B., Breuer, W. V., Cabantchik, Z. I., Bouhassira, E. E., Fabry, M. E., & Nagel, R. L. (2008) · Experimental Hematology · doi:10.1016/j.exphem.2008.10.004 · Cited by 33
Tubular reabsorption and local production of urine hepcidin-25
Peters, H. P. E., Laarakkers, C. M., Pickkers, P., Masereeuw, R., Boerman, O. C., Eek, A., Cornelissen, E. A. M., Swinkels, D. W., & Wetzels, J. F. M. (2013) · BMC Nephrology · doi:10.1186/1471-2369-14-70 · Cited by 32
Iron and oxygen sensing: a tale of 2 interacting elements?
Simpson, R. J., & McKie, A. T. (2014) · Metallomics · doi:10.1039/c4mt00225c · Cited by 32
Sun, C., Wu, Q., Gao, S., Ma, Z., Liu, Y., Zhang, J., & Zhao, Y. (2019) · Journal of Diabetes Investigation · doi:10.1111/jdi.13170 · Cited by 33
Du, F., Qian, Z., Gong, Q., Zhu, Z. J., Lü, L., & Ke, Y. (2012) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2011.12.002 · Cited by 33
Low Serum Hepcidin in Patients with Autoimmune Liver Diseases
Lyberopoulou, A., Chachami, G., Gatselis, N., Kyratzopoulou, E., Saitis, A., Gabeta, S., Eliades, P., Paraskeva, E., Zachou, K., Koukoulis, G. Κ., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0135486 · Cited by 35
Understanding the Intricacies of Iron Overload Associated with β-Thalassemia: A Comprehensive Review
Basu, S., Rahaman, M., Dolai, T. K., Shukla, P. C., & Chakravorty, N. (2023) · Thalassemia Reports · doi:10.3390/thalassrep13030017 · Cited by 37
A critical role for murine transferrin receptor 2 in erythropoiesis during iron restriction
Wallace, D. F., Secondes, E. S., Rishi, G., Ostini, L., McDonald, C. J., Lane, S., Vu, T., Hooper, J. D., Velasco, G., Ramsay, A. J., et al. (2014) · British Journal of Haematology · doi:10.1111/bjh.13225 · Cited by 31
Gutschow, P., Schmidt, P. J., Han, H., Ostland, V., Bartnikas, T. B., Pettiglio, M. A., Herrera, C., Butler, J. S., Nemeth, E., Ganz, T., et al. (2014) · Haematologica · doi:10.3324/haematol.2014.116723 · Cited by 31
Davis, M. R., Shawron, K., Rendina-Ruedy, E., Peterson, S., Lucas, E. A., Smith, B. J., & Clarke, S. L. (2011) · Journal of Nutrition · doi:10.3945/jn.111.144105 · Cited by 30
Chen, Y., Xu, W., Yang, H. J., Shao, M., Xu, S., Deng, J., Gao, X., Liu, H., Shuai, Z., Xu, S., et al. (2020) · Immunological Investigations · doi:10.1080/08820139.2020.1742731 · Cited by 32
Effect of ferroportin polymorphism on iron homeostasis and infection
Kasvosve, I. (2012) · Clinica Chimica Acta · doi:10.1016/j.cca.2012.11.013 · Cited by 34
Koliaraki, V., Marinou, M., Samiotaki, M. K., Panayotou, G., Pantopoulos, K., & Mamalaki, A. (2008) · Biochimie · doi:10.1016/j.biochi.2008.01.012 · Cited by 30
The relationship between systemic iron homeostasis and erythropoiesis
Rishi, G., & Subramaniam, V. N. (2017) · Bioscience Reports · doi:10.1042/bsr20170195 · Cited by 35
Does Hypoxia Cause Carcinogenic Iron Accumulation in Alcoholic Liver Disease (ALD)?
da Silva, I. S., Rausch, V., Seitz, H. K., & Mueller, S. (2017) · Cancers · doi:10.3390/cancers9110145 · Cited by 31
Serum pro-hepcidin: measuring active hepcidin or a non-functional precursor?
Brookes, M., Sharma, N. K., Tselepis, C., & Iqbal, T. H. (2004) · Gut · doi:10.1136/gut.2004.047639 · Cited by 31
Deciphering the role of hepcidin in iron metabolism and anemia management
Kesharwani, P., Dash, D., & Koiri, R. K. (2025) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2025.127591 · Cited by 33
Morbidities in non‐transfusion‐dependent thalassemia
Saliba, A. N., & Taher, A. T. (2016) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.13083 · Cited by 30
Dahlquist, D. T., Stellingwerff, T., Dieter, B. P., McKenzie, D. C., & Koehle, M. S. (2017) · Applied Physiology, Nutrition, and Metabolism · doi:10.1139/apnm-2017-0207 · Cited by 31
Samba-Mondonga, M., Constante, M., Fragoso, G., Calvé, A., & Santos, M. M. (2019) · PLoS ONE · doi:10.1371/journal.pone.0208677 · Cited by 30
Impact of bacterial infections on erythropoiesis
de Souza, L. V., Hoffmann, A., & Weiß, G. (2020) · Expert Review of Anti-infective Therapy · doi:10.1080/14787210.2021.1841636 · Cited by 30
α‐1 Antitrypsin binds preprohepcidin intracellularly and prohepcidin in the serum
Pandur, E., Nagy, J., Poór, V. S., Sarnyai, Á., Huszár, A., Miseta, A., & Sipos, K. (2009) · FEBS Journal · doi:10.1111/j.1742-4658.2009.06937.x · Cited by 29
Langdon, J. M., Barkataki, S., Berger, A. E., Cheadle, C., Xue, Q., Sung, V., & Roy, C. N. (2014) · American Journal of Hematology · doi:10.1002/ajh.23856 · Cited by 30
Hepcidin, an antimicrobial peptide is downregulated in ceruloplasmin-deficient mice
Guo, P., Cui, R., Chang, Y., Wu, W., Qian, Z., Yoshida, K., Qiao, Y.-T., Takeda, S., & Duan, X. (2008) · Peptides · doi:10.1016/j.peptides.2008.09.017 · Cited by 30
Lipopolysaccharide infusion up-regulates hepcidin mRNA expression in equine liver
Oliveira-Filho, J. P., Badial, P. R., Cunha, P. H., Peiró, J. R., Araújo, J. P., Divers, T. J., Winand, N. J., & Borges, A. S. (2011) · Innate Immunity · doi:10.1177/1753425911420181 · Cited by 29
Study of Serum Hepcidin in Hereditary Hemolytic Anemias
El-Beshlawy, A. M., Alaraby, I., Kader, M. S. E. M. A., Ahmed, D. H., & Abdelrahman, H. E. M. (2012) · Hemoglobin · doi:10.3109/03630269.2012.721151 · Cited by 31
Krieg, L., Milstein, O., Krebs, P., Xia, Y., Beutler, B., & Du, X. (2011) · Blood · doi:10.1182/blood-2011-04-350082 · Cited by 30
Reduced sensitivity of the ferroportin Q248H mutant to physiological concentrations of hepcidin
Nekhai, S. A., Xu, M., Foster, A., Kasvosve, I., Diaz, S. F., Machado, R. F., Castro, O. L., Kato, G. J., Taylor, J. G., & Gordeuk, V. R. (2012) · Haematologica · doi:10.3324/haematol.2012.066530 · Cited by 32
Govus, A. D., Abbiss, C. R., Garvican‐Lewis, L. A., Swinkels, D. W., Laarakkers, C. M., Gore, C. J., & Peeling, P. (2014) · European Journal of Applied Physiology · doi:10.1007/s00421-014-2938-2 · Cited by 30
Attenuation of acute and chronic liver injury in rats by iron-deficient diet
Otogawa, K., Ogawa, T., Shiga, R., Nakatani, K., Ikeda, K., Nakajima, Y., & Kawada, N. (2007) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00735.2007 · Cited by 30
Inherited iron loading: genetic testing in diagnosis and management
Worwood, M. (2004) · Blood Reviews · doi:10.1016/j.blre.2004.03.003 · Cited by 32
Iron Fortification: Its Efficacy and Safety in Relation to Infections
Hurrell, R. F. (2007) · Food and Nutrition Bulletin · doi:10.1177/15648265070284s411 · Cited by 30
Blunted hepcidin response to inflammation in the absence of Hfe and transferrin receptor 2
Wallace, D. F., McDonald, C. J., Ostini, L., & Subramaniam, V. N. (2011) · Blood · doi:10.1182/blood-2010-08-303859 · Cited by 29
Advantages and disadvantages of the animal models v. in vitro studies in iron metabolism: a review
García, Y., & Díaz‐Castro, J. (2013) · animal · doi:10.1017/s1751731113001134 · Cited by 31
Wang, M., Tang, W., Xin, H., & Zhu, Y. Z. (2016) · PLoS ONE · doi:10.1371/journal.pone.0163289 · Cited by 29
Mechanisms and Regulation of Intestinal Iron Transport
Collins, J. F., Flores, S. R., Wang, X., & Anderson, G. J. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-809954-4.00060-8 · Cited by 30
Increased DMT1 and FPN1 expression with enhanced iron absorption in ulcerative colitis human colon
Minor, E. A., Kupec, J. T., Nickerson, A. J., Narayanan, K., & Rajendran, V. M. (2019) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00128.2019 · Cited by 29
Evliyaoğlu, E., Kilercioğlu, S., Yılmaz, H. A., Turchini, G. M., Paolucci, M., Clark, T. D., Demirkale, İ., & Eroldoğan, O. T. (2022) · Aquaculture · doi:10.1016/j.aquaculture.2021.737884 · Cited by 30
Novel insights into alcoholic liver disease: Iron overload, iron sensing and hemolysis
Mueller, S., Chen, C., Mueller, J. H., & Wang, S. (2022) · Journal of Translational Internal Medicine · doi:10.2478/jtim-2021-0056 · Cited by 30
Hortová-Kohoutková, M., Skotáková, M., Onyango, I. G., Slezáková, M., Panovský, R., Opatřil, L., Slanina, P., Zuani, M. D., Mrkva, O., Andrejčinová, I., et al. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1110540 · Cited by 28
Severe microcytic anemia but increased erythropoiesis in mice lacking Hfe or Tfr2 and Tmprss6
Lee, P. L., Hsu, M., Welser-Alves, J. V., & Peng, H. (2012) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2011.12.005 · Cited by 31
Recombinant human hepcidin expressed in Escherichia coli isolates as an iron containing protein
Gerardi, G., Biasiotto, G., Santambrogio, P., Zanella, I., Ingrassia, R., Corrado, M., Cavadini, P., Derosas, M., Levi, S., & Arosio, P. (2005) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2005.06.002 · Cited by 29
Iron Metabolism Dysregulation and Cognitive Dysfunction in Pediatric Obesity: Is There a Connection?
Grandone, A., Marzuillo, P., Perrone, L., & Giudice, E. D. (2015) · Nutrients · doi:10.3390/nu7115458 · Cited by 29
(2012) · doi:10.5772/31289 · Cited by 29
Tandara, L., Grubišić, T. Ž., Gudelj, I., Jurišić, Z., Tandara, M., Gugo, K., Mladinov, S., & Salamunić, I. (2015) · Clinical Biochemistry · doi:10.1016/j.clinbiochem.2015.07.010 · Cited by 30
Understanding and exploiting hepcidin as an indicator of anemia due to chronic kidney disease
Larson, D. S., & Coyne, D. W. (2013) · Kidney Research and Clinical Practice · doi:10.1016/j.krcp.2013.01.001 · Cited by 27
Wallace, D. F., & Subramaniam, V. N. (2015) · International Immunology · doi:10.1093/intimm/dxu144 · Cited by 28
(Z)-ligustilide increases ferroportin1 expression and ferritin content in ischemic SH-SY5Y cells
Zhang, Y., Li, F.-M., Guo, Y., Jiang, L., Ma, J., Ke, Y., & Qian, Z. (2016) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2016.10.029 · Cited by 28
AMPK Serves as a Therapeutic Target Against Anemia of Inflammation
Wang, M., Xin, H., Tang, W., Li, Y., Zhang, Z., Fan, L., Miao, L., Tan, B., Wang, X., & Zhu, Y. Z. (2016) · Antioxidants and Redox Signaling · doi:10.1089/ars.2016.6846 · Cited by 28
Strategies to Interfere with Tumor Metabolism through the Interplay of Innate and Adaptive Immunity
Mora, J., Mertens, C., Meier, J. K., Fuhrmann, D. C., Brüne, B., & Jung, M. (2019) · Cells · doi:10.3390/cells8050445 · Cited by 27
Immunolocalization of Ferroportin in Healthy and Anemic Mice
D’Anna, M. C., Veuthey, T., & Roque, M. E. (2008) · Journal of Histochemistry & Cytochemistry · doi:10.1369/jhc.2008.951616 · Cited by 27
Effect of penicillamine and zinc on iron metabolism in Wilson's disease
Medici, V., Leo, V. D., Lamboglia, F., Bowlus, C. L., Tseng, S.-C., Renata D'Incà, Irato, P., Burra, P., Martines, D., & Sturniolo, G. C. (2007) · Scandinavian Journal of Gastroenterology · doi:10.1080/00365520701514495 · Cited by 28
Pyruvate kinase deficiency associated with severe liver dysfunction in the newborn
Raphaël, M. F., van Wijk, R., Schweizer, J. J., Meeteren, N. S.-V., Kindermann, A., van Solinge, W. W., & Smiers, F. J. W. (2007) · American Journal of Hematology · doi:10.1002/ajh.20942 · Cited by 28
Live high, train low – influence on resting and post‐exercise hepcidin levels
Govus, A. D., Peeling, P., Abbiss, C. R., Lawler, N. G., Swinkels, D. W., Laarakkers, C. M., Thompson, K., Peiffer, J. J., Gore, C. J., & Garvican‐Lewis, L. A. (2016) · Scandinavian Journal of Medicine and Science in Sports · doi:10.1111/sms.12685 · Cited by 28
Małyszko, J. S., Małyszko, J. S., Pawlak, K., & Myśliwiec, M. (2006) · Transplantation Proceedings · doi:10.1016/j.transproceed.2006.08.137 · Cited by 28
Recent advances in intestinal iron transport
Anderson, G. J., & Frazer, D. M. (2005) · Current Gastroenterology Reports · doi:10.1007/s11894-005-0005-1 · Cited by 31
Hepcidin and Hfe in iron overload in β‐thalassemia
Gardenghi, S., Ramos, P., Follenzi, A., Rao, N., Rachmilewitz, E. A., Giardina, P. J., Grady, R. W., & Rivella, S. (2010) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2010.05595.x · Cited by 27
Wang, B., Yin, Q., Han, Y., Wu, M., Li, Z., Tu, Y., Zhou, L., Wei, Q., Liu, H., Tang, R., et al. (2020) · Renal Failure · doi:10.1080/0886022x.2020.1811121 · Cited by 26
Protein Antioxidants in Thalassemia
Awadallah, S. M. (2013) · Advances in clinical chemistry · doi:10.1016/b978-0-12-407681-5.00003-9 · Cited by 27
Foka, P., Dimitriadis, A., Kyratzopoulou, E., Giannimaras, D. A., Sarno, S., Simos, G., Georgopoulou, U., & Mamalaki, A. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1621-4 · Cited by 27
Is mesalazine really safe for use in breastfeeding mothers?
Silverman, D. A., Ford, J., Shaw, I., & Probert, C. S. (2004) · Gut · doi:10.1136/gut.2004.048058 · Cited by 27
Type of Renal Replacement Therapy and Residual Renal Function May Affect Prohepcidin and Hepcidin
Małyszko, J., Małyszko, J. S., Koźmiński, P., & Myśliwiec, M. (2009) · Renal Failure · doi:10.3109/08860220903216071 · Cited by 28
Gastrins, iron homeostasis and colorectal cancer
Kovac, S., Anderson, G. J., & Baldwin, G. S. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.02.007 · Cited by 28
Liver-gut axis in the regulation of iron homeostasis
Darshan, D. (2007) · World Journal of Gastroenterology · doi:10.3748/wjg.v13.i35.4737 · Cited by 31
Transferrin receptor 2 is crucial for iron sensing in human hepatocytes
Rapisarda, C., Puppi, J., Hughes, R. D., Dhawan, A. K., Farnaud, S., Evans, R. W., & Sharp, P. (2010) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00157.2010 · Cited by 28
New strategies to target iron metabolism for the treatment of beta thalassemia
Oikonomidou, P. R., Casu, C., & Rivella, S. (2016) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.13018 · Cited by 27
Serum Hepcidin as a Diagnostic Marker of Severe Iron Overload in Beta-thalassemia Major
Kaddah, A. M., Abdel-Salam, A., Farhan, M. S., & Ragab, R. (2017) · The Indian Journal of Pediatrics · doi:10.1007/s12098-017-2375-4 · Cited by 29
Leitch, H. A., Buckstein, R. J., Zhu, N. Y., Nevill, T. J., Yee, K. W. L., Leber, B. F., Keating, M., St‐Hilaire, È., Kumar, R., Delage, R., et al. (2018) · Leukemia Research · doi:10.1016/j.leukres.2018.09.005 · Cited by 27
The Functional Versatility of Transferrin Receptor 2 and Its Therapeutic Value
Roetto, A., Mezzanotte, M., & Pellegrino, R. M. (2018) · Pharmaceuticals · doi:10.3390/ph11040115 · Cited by 27
Long, A., Garver, K. A., & Jones, S. R. M. (2019) · Journal of Fish Diseases · doi:10.1111/jfd.12989 · Cited by 27
Mild copper deficiency alters gene expression of proteins involved in iron metabolism
Auclair, S., Feillet‐Coudray, C., Coudray, C., Schneider, S., Muckenthaler, M. U., & Mazur, A. (2006) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2005.11.003 · Cited by 28
Przybylowski, P., Malyszko, J. S., Macdougall, I. C., & Malyszko, J. (2013) · Transplantation Proceedings · doi:10.1016/j.transproceed.2012.02.040 · Cited by 26
Peters, H. P. E., Rumjon, A., Bansal, S. S., Laarakkers, C. M., van den Brand, J. A. J. G., Sarafidis, P. A., Musto, R., Małyszko, J., Swinkels, D. W., Wetzels, J. F. M., et al. (2012) · Nephrology Dialysis Transplantation · doi:10.1093/ndt/gfs164 · Cited by 26
Iron Supplementation during Three Consecutive Days of Endurance Training Augmented Hepcidin Levels
Ishibashi, A., Maeda, N., Kamei, A., & Goto, K. (2017) · Nutrients · doi:10.3390/nu9080820 · Cited by 26
A Novel Approach for Iron Deficiency Anaemia with Liposomal Iron: Concept to Clinic
Maladkar, M. N., Sankar, S., & Yadav, A. (2020) · Journal of Biosciences and Medicines · doi:10.4236/jbm.2020.89003 · Cited by 30
Han, Y., Huang, W., Meng, H., Zhan, Y., & Hou, J. (2021) · Journal of Periodontal Research · doi:10.1111/jre.12865 · Cited by 27
BMP5 contributes to hepcidin regulation and systemic iron homeostasis in mice
Xiao, X., Xu, Y., Moschetta, G. A., Yu, Y., Fisher, A. L., Alfaro-Magallanes, V. M., McMillen, S. A., Phillips, S., Wang, C., Christian, J. L., et al. (2023) · Blood · doi:10.1182/blood.2022019195 · Cited by 25
Heritage, M. L., Murphy, T. L., Bridle, K. R., Anderson, G. J., Crawford, D. H., & Fletcher, L. M. (2009) · Alcoholism Clinical and Experimental Research · doi:10.1111/j.1530-0277.2009.00969.x · Cited by 27
Venn-Watson, S. K., Smith, C. R., & Jensen, E. D. (2008) · Journal of Wildlife Diseases · doi:10.7589/0090-3558-44.2.318 · Cited by 26
Variant Creutzfeldt-Jakob disease: update
Bramble, M. G., & Ironside, J. W. (2004) · Gut · doi:10.1136/gut.2004.048231 · Cited by 26
Pellegrino, R. M., Boda, E., Montarolo, F., Boero, M., Mezzanotte, M., Saglio, G. N., Buffo, A., & Roetto, A. (2016) · Scientific Reports · doi:10.1038/srep30725 · Cited by 26
Dzikaite, V., Holmström, P., Stål, P., Eckes, K., Hagen, K., Eggertsen, G., Gåfvels, M., Melefors, Ö., & Hultcrantz, R. (2006) · Journal of Hepatology · doi:10.1016/j.jhep.2005.07.028 · Cited by 26
A novel monoclonal antibody immunoassay for the detection of human serum hepcidin
Schwarz, P., Strnad, P., von Figura, G., Janetzko, A., Krayenbühl, P. A., Adler, G., & Kulaksiz, H. (2010) · Journal of Gastroenterology · doi:10.1007/s00535-010-0344-z · Cited by 25
Circulating factors are involved in hypoxia-induced hepcidin suppression
Ravasi, G., Pelucchi, S., Greni, F., Mariani, R., Giuliano, A., Parati, G., Silvestri, L., & Piperno, A. (2014) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2014.06.006 · Cited by 25
Neves, J. V., Caldas, C., Ramos, M. F., & Rodrigues, P. (2016) · PLoS ONE · doi:10.1371/journal.pone.0153940 · Cited by 25
Angmo, S., Tripathi, N., Abbat, S., Sharma, S., Singh, S. S., Halder, A., Yadav, K., Shukla, G., Sandhir, R., Rishi, V., et al. (2017) · Scientific Reports · doi:10.1038/srep40097 · Cited by 26
Alamo, I. G., Kannan, K. B., Bible, L. E., Loftus, T. J., Ramos, H., Efron, P. A., & Mohr, A. M. (2017) · The Journal of Trauma: Injury, Infection, and Critical Care · doi:10.1097/ta.0000000000001374 · Cited by 25
Nakai, T., Iwamura, Y., Kato, K., Hirano, I., Matsumoto, Y., Tomioka, Y., Yamamoto, M. P., & Suzuki, N. (2023) · Blood Advances · doi:10.1182/bloodadvances.2023009798 · Cited by 25
Red cell distribution width and survival in patients hospitalized on a medical ICU
Fujita, B., Franz, M., Figulla, H., Pfeifer, R., Kabisch, B., Fritzenwanger, M., & Jung, C. (2015) · Clinical Biochemistry · doi:10.1016/j.clinbiochem.2015.07.011 · Cited by 25
Jenkitkasemwong, S., Broderius, M. A., Nam, H., Prohaska, J. R., & Knutson, M. D. (2010) · Journal of Nutrition · doi:10.3945/jn.109.117077 · Cited by 24
Małyszko, J., Małyszko, J. S., & Myśliwiec, M. (2009) · Renal Failure · doi:10.1080/08860220903082606 · Cited by 25
The prevalence and etiology of anemia among HIV-infected children in India
Shet, A., Arumugam, K., Rajagopalan, N., Dinakar, C., Krishnamurthy, S., Mehta, S., & Shet, A. S. (2011) · European Journal of Pediatrics · doi:10.1007/s00431-011-1599-y · Cited by 27
Robach, P., Recalcati, S., Girelli, D., Campostrini, N., Kempf, T., Wollert, K. C., Corbella, M., Santambrogio, P., Perbellini, L., Brasse‐Lagnel, C., et al. (2013) · European Journal Of Haematology · doi:10.1111/ejh.12122 · Cited by 25
Metadata
- Authors
- Nicolas, G., Chauvet, C., Viatte, L., Danan, J. L., Bigard, X., Devaux, I., Beaumont, C., Kahn, A., & Vaulont, S.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- Service de Santé des Armées (FR)
- Inserm (FR)
- Corresponding author
- Vaulont, Sophie
- Venue
- Journal of Clinical Investigation
- Published
- 2002-10-01
- Volume
- 110
- Issue
- 7
- Pages
- 1037-1044
- ISSN
- 0021-9738 (ISSN-L)
- OpenAlex
- W4243766541
- Cited by
- 1,214
- References
- 14
- Citations by year
- 2026: 11 · 2025: 23 · 2024: 16 · 2023: 36 · 2022: 33 · 2021: 35 · 2020: 63 · 2019: 52 · 2018: 53 · 2017: 55 · 2016: 44 · 2015: 45 · 2014: 71 · 2013: 58 · 2012: 61
- FWCI
- 20.80
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Clinical Investigation (publishedVersion)
- Funders
- Institut National de la Santé et de la Recherche Médicale
- Fondation pour la Recherche Médicale
- Topics
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Health Sciences › Medicine › Hematology › Erythropoietin and Anemia Treatment
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Ferroptosis and cancer prognosis
- Keywords
- hepcidin, iron homeostasis, anemia, hypoxia, inflammation, iron deficiency, iron overload, phlebotomy, turpentine, hepatoma cells, serum iron, reticuloendothelial cells
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