The DOI matches its Crossref record; 35 of the 35 references it cites were found in a registry or an index.
Resistance to hepcidin is conferred by hemochromatosis-associated mutations of ferroportin
Open accessAbstract
Ferroportin (FPN) mediates iron export from cells; FPN mutations are associated with the iron overloading disorder hemochromatosis. Previously, we found that the A77D, V162del, and G490D mutations inhibited FPN activity, but that other disease-associated FPN variants retained full iron export capability. The peptide hormone hepcidin inhibits FPN as part of a homeostatic negative feedback loop. We measured surface expression and function of wild-type FPN and fully active FPN mutants in the presence of hepcidin. We found that the Y64N and C326Y mutants of FPN are completely resistant to hepcidin inhibition and that N144D and N144H are partially resistant. Hemochromatosis-associated FPN mutations, therefore, either reduce iron export ability or produce an FPN variant that is insensitive to hepcidin. The former mutation type is associated with Kupffer-cell iron deposition and normal transferrin saturation in vivo, whereas patients with the latter category of FPN mutation have high transferrin saturation and tend to deposit iron throughout the liver parenchyma. FPN-linked hemochromatosis may have a variable pathogenesis depending on the causative FPN mutant.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Deficits in hepcidin-mediated regulation of FPN, often due to hereditary hemochromatoses, lead to iron overload and widespread tissue damage affecting the liver, heart, pancreas, and joints 11-13 .”
From Structure of hepcidin-bound ferroportin reveals iron homeostatic mechanisms (2020) · cites this paper as [13]
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
“Several hereditary hemochromatosis mutations in FPN directly coordinate Co 2+ in the C domain, including C326S/F/Y 13,29-31 and H507R 32 .”
From Structure of hepcidin-bound ferroportin reveals iron homeostatic mechanisms (2020) · cites this paper as [13]
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
“Several FPN mutations decrease hepcidin binding to FPN, including N144H/D/T 34-36 , C326S/F/Y 13,29-31 , Y333H 37 , Y501C 7,38 , D504N 7,39 and H507R 32 .”
From Structure of hepcidin-bound ferroportin reveals iron homeostatic mechanisms (2020) · cites this paper as [13]
Experimental — accuracy not yet measuredIn the citing paper
“It is essential to the development of these cell types as Spic −/− mice have drastically reduced numbers of RPM and EIM which lead to reduced proerythroblast numbers in the steady state, supporting the idea that iron recycling is essential to sustain iron-sufficient erythropoiesis [58].”
From “Pumping iron”—how macrophages handle iron at the systemic, microenvironmental, and cellular levels (2017) · cites this paper as [58]
In the citing paper
“Missense mutations that affected the subcellular localization or transporter function of ferroportin (”
From Forging a field: the golden age of iron biology. (2008) · cites this paper as [159]
In the citing paper
“In contrast, missense mutations that rendered ferroportin insensitive to regulation by hepcidin (”
From Forging a field: the golden age of iron biology. (2008) · cites this paper as [159]
In the citing paper
“These issues were resolved by the discovery that there are 2 broad categories of ferroportin mutations.158,159”
From Forging a field: the golden age of iron biology. (2008) · cites this paper as [159]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
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
A novel MHC class I-like gene is mutated in patients with hereditary haemochromatosis
Feder, J. N., Gnirke, A., Thomas, W., Tsuchihashi, Z., Ruddy, D. A., Basava, A., Dormishian, F., Domingo, R., Ellis, M. C., Fullan, A., et al. (1996) · Nature Genetics · doi:10.1038/ng0896-399 · Cited by 3,664
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
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
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
Hereditary Hemochromatosis — A New Look at an Old Disease
Pietrangelo, A. (2004) · New England Journal of Medicine · doi:10.1056/nejmra031573 · Cited by 992
Autosomal-dominant hemochrom-atosis is associated with a mutation in the ferroportin (SLC11A3) gene
Montosi, G., Donovan, A., Totaro, A., Garuti, C., Pignatti, E., Cassanelli, S., Trenor, C. C., Gasparini, P., Andrews, N. C., & Pietrangelo, A. (2001) · Journal of Clinical Investigation · doi:10.1172/jci13468 · Cited by 562
Autosomal-dominant hemochrom-atosis is associated with a mutation in the ferroportin (SLC11A3) gene
Montosi, G., Donovan, A., Totaro, A., Garuti, C., Pignatti, E., Cassanelli, S., Trenor, C. C., Gasparini, P., Andrews, N. C., & Pietrangelo, A. (2001) · Journal of Clinical Investigation · doi:10.1172/jci200113468 · Cited by 557
A mutation in SLC11A3 is associated with autosomal dominant hemochromatosis
Njajou, O. T., Vaessen, N., Joosse, M., Berghuis, B., van Dongen, J. W. F., Breuning, M. H., Snijders, P. J. L. M., Rutten, W. P. F., Sandkuijl, L. A., Oostra, B. A., et al. (2001) · Nature Genetics · doi:10.1038/90038 · Cited by 492
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
Cited by
Sorted by citations
Items 101–200 of 263
Kaneko, Y., Miyajima, H., Piperno, A., Tomosugi, N., Hayashi, H., Morotomi, N., Tsuchida, K., Ikeda, T., Ishikawa, A., Ota, Y., et al. (2010) · Journal of Gastroenterology · doi:10.1007/s00535-010-0259-8 · Cited by 56
“In the less prevalent type B, the mutant gene generates proteins that show normal cell surface expression but reduced sensitivity to hepcidin [43, 44 ].”
BackgroundCallebaut, I., Joubrel, R., Pissard, S., Kannengiesser, C., Gérolami, V., Ged, C., Cadet, E., Cartault, F., Ka, C., Gourlaouen, I., et al. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu160 · Cited by 54
“Consistently with both the present observations and previous in vitro findings (18, 29, 38, 39), it has been suggested that the p.”
ResultWild-type and mutant ferroportins do not form oligomers in transfected cells
Gonçalves, A. S., Muzeau, F., Blaybel, R., Hetet, G., Driss, F., Delaby, C., Canonne‐Hergaux, F., & Beaumont, C. (2006) · Biochemical Journal · doi:10.1042/bj20051682 · Cited by 55
Superinfection in malaria: Plasmodium shows its iron will
Portugal, S., Drakesmith, H., & Mota, M. M. (2011) · EMBO Reports · doi:10.1038/embor.2011.213 · Cited by 55
“Ganz & Nemeth, 2011 ) or that confer hepcidin resistance to variants of ferroportin”
BackgroundSelf-citationStructural and functional abnormalities in iron-depleted heart
Kobak, K. A., Radwańska, M., Dzięgała, M., Kasztura, M., Josiak, K., Banasiak, W., Ponikowski, P. P., & Jankowska, E. A. (2018) · Heart Failure Reviews · doi:10.1007/s10741-018-9738-4 · Cited by 54
“Cre+ genotype), which encoded FPN completely resistant to hepcidin inhibition but with preserved iron export function [44, 45].”
BackgroundFactors influencing disease phenotype and penetrance in HFE haemochromatosis
Rochette, J., Gac, G. L., Lassoued, K., Férec, C., & Robson, K. (2010) · Human Genetics · doi:10.1007/s00439-010-0852-1 · Cited by 52
“Hepcidin (encoded by HAMP) acts by binding to and inducing the degradation of ferroportin (encoded by SLC40A1) (Nemeth et al. 2004; Drakesmith et al. 2005; Schimanski et al. 2005; De Domenico et al. 2007).”
BackgroundSelf-citationProtein degradation and iron homeostasis
Thompson, J. W., & Bruick, R. K. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.02.003 · Cited by 49
Iron storage disease in A sia‐ P acific populations: The importance of non‐ HFE mutations
McDonald, C. J., Wallace, D. F., Crawford, D. H., & Subramaniam, V. N. (2013) · Journal of Gastroenterology and Hepatology · doi:10.1111/jgh.12222 · Cited by 49
Molecular and clinical correlates in iron overload associated with mutations in ferroportin.
Domenico, I. D., Ward, D. M., Nemeth, E., Ganz, T., Corradini, E., Ferrara, F., Musci, G., Pietrangelo, A., & Kaplan, J. (2006) · PubMed · Cited by 48
Létocart, É., Gac, G. L., Majore, S., Ka, C., Radio, F. C., Gourlaouen, I., Bernardo, C. D., Férec, C., & Grammatico, P. (2009) · British Journal of Haematology · doi:10.1111/j.1365-2141.2009.07834.x · Cited by 46
“Another point of interest is that certain ferroportin mutants have been proved to show different degrees of resistance to hepcidin (Drakesmith et al, 2005; Rice et al, 2009).”
BackgroundMethodThe global burden of iron overload
Wood, M. J., Skoien, R., & Powell, L. W. (2009) · Hepatology International · doi:10.1007/s12072-009-9144-z · Cited by 45
“Type B ferroportin disease produces a disease similar to HFE hemochromatosis due to mutated ferroportin, which is resistant to the action of hepcidin [26].”
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 47
Barton, J. C., Delrio-Lafreniere, S. A., Leiendecker‐Foster, C., Li, H., Acton, R. T., Press, R. D., & Eckfeldt, J. H. (2009) · American Journal of Hematology · doi:10.1002/ajh.21524 · Cited by 45
“Heterozygosity for deleterious SLC40A1 mutations causes high-iron phenotypes in some patients without HFE C282Y homozygosity [30,31].”
BackgroundJanssen, M. C. H., & Swinkels, D. W. (2009) · Best Practice & Research Clinical Gastroenterology · doi:10.1016/j.bpg.2009.02.004 · Cited by 46
How we manage patients with hereditary haemochromatosis
Rombout‐Sestrienkova, E., van Kraaij, M. G. J., & Koek, G. H. (2016) · British Journal of Haematology · doi:10.1111/bjh.14376 · Cited by 43
Ferroportin Diseases: Functional Studies, a Link Between Genetic and Clinical Phenotype
Détivaud, L., Island, M., Jouanolle, A., Ropert, M., Bardou‐Jacquet, E., Lan, C. L., Mosser, A., Leroyer, P., Deugnier, Y., David, V., et al. (2013) · Human Mutation · doi:10.1002/humu.22396 · Cited by 47
“We used the Y64N mutant construct as a positive control for the FPN form of hepcidin resistance [Drakesmith et al., 2005].”
BackgroundMethodResultInfluentialGirelli, D., Domenico, I. D., Bozzini, C., Campostrini, N., Busti, F., Castagna, A., Soriani, N., Cremonesi, L., Ferrari, M., Colombari, R., et al. (2008) · Journal of Hepatology · doi:10.1016/j.jhep.2008.05.028 · Cited by 41
“At the opposite end of the spectrum are ‘‘gain-offunction” mutants that are properly localized on the membrane, but are resistant to hepcidin inactivation [11,15,16].”
Hamp1 but not Hamp2 regulates ferroportin in fish with two functionally distinct hepcidin types
Neves, J. V., Ramos, M. F., Moreira, A. C., Silva, T., Gomes, M. S., & Rodrigues, P. (2017) · Scientific Reports · doi:10.1038/s41598-017-14933-5 · Cited by 41
Role 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
Impaired Iron Transport Activity of Ferroportin 1 in Hereditary Iron Overload
McGregor, J., Shayeghi, M., Vulpe, C. D., Anderson, G. J., Pietrangelo, A., Simpson, R. J., & McKie, A. T. (2005) · The Journal of Membrane Biology · doi:10.1007/s00232-005-0768-1 · Cited by 39
“, C326Y, N144H) no internalization was evident, thus leading to hepcidin resistance (Drakesmith et al., 2005).”
BackgroundResultInfluentialGlobal Sequencing Approach for Characterizing the Molecular Background of Hereditary Iron Disorders
Cunat, S., Giansily‐Blaizot, M., Bismuth, M., Blanc, F., Dereure, O., Larrey, D. G., Quellec, A. L., Pouderoux, P., Rosé, C., Raingeard, I., et al. (2007) · Clinical Chemistry · doi:10.1373/clinchem.2007.090605 · Cited by 37
Kartikasari, A. E. R., Roelofs, R., Schaeps, R. M. J., Kemna, E., Peters, W. H. M., Swinkels, D. W., & Tjalsma, H. (2008) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2008.08.004 · Cited by 35
“In this experiment, we used THP1 cells, known to express ferroportin [39].”
MethodBarton, J. C., Acton, R. T., Lee, P. L., & West, C. (2007) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2007.03.008 · Cited by 34
“Taken together, these in vitro results are consistent with the present in vivo observations that suggest that SLC40A1 Q248H is associated with a mild clinical phenotype or only causes iron overload in the presence of modifying factors [44,45].”
BackgroundResultRegulation of Iron Absorption in Hemoglobinopathies
Rechavi, G., & Rivella, S. (2008) · Current Molecular Medicine · doi:10.2174/156652408786241401 · Cited by 32
Griffiths, W. J., Mayr, R., McFarlane, I., Hermann, M., Halsall, D. J., Zoller, H., & Cox, T. M. (2009) · Hepatology · doi:10.1002/hep.23377 · Cited by 33
Mutations in the HFE, TFR2, and SLC40A1 genes in patients with hemochromatosis
Rueda, A. D. C., Moreno‐Carralero, M., Cuadrado‐Grande, N., Álvarez-Sala, J. L., de Salamanca, R. E., Méndez, M., & Morán‐Jiménez, M. (2012) · Gene · doi:10.1016/j.gene.2012.07.069 · Cited by 33
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
Anderson, D. S., Heeney, M. M., Roth, U., Menzel, C., Fleming, M. D., & Steen, H. (2010) · Analytical Chemistry · doi:10.1021/ac902479p · Cited by 31
Diagnostic Evaluation of Hereditary Hemochromatosis (HFE and Non-HFE)
Bardou‐Jacquet, E., & Brissot, P. (2014) · Hematology/Oncology Clinics of North America · doi:10.1016/j.hoc.2014.04.006 · Cited by 34
Barton, J. C., Wiener, H. W., Acton, R. T., & Go, R. C. P. (2005) · BMC Hematology · doi:10.1186/1471-2326-5-5 · Cited by 31
“Hepcidin levels are significantly decreased in hemochromatosis associated with TFR2, FPN1, and HJV mutations [34-36].”
BackgroundFerroportin is a monomer in vivo in mice
Pignatti, E., Mascheroni, L., Sabelli, M., Barelli, S., Biffo, S., & Pietrangelo, A. (2005) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2005.11.001 · Cited by 32
The ferroportin Q248H mutation protects from anemia, but not malaria or bacteremia
Muriuki, J. M., Mentzer, A. J., Band, G., Gilchrist, J. J., Carstensen, T., Lule, S. A., Goheen, M. M., Joof, F., Kimita, W., Mogire, R., et al. (2019) · Science Advances · doi:10.1126/sciadv.aaw0109 · Cited by 29
“Alternately, Q248H has also been shown to impair cellular iron export [retaining only 25% of wild-type (WT) iron efflux] (5) or have no functional effect (6, 7).”
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
“mice and hepcidin resistant variants of FPN1 in humans suffer from massive iron overload, which shows the importance of functional hepcidin – FPN1 interaction [11,12].”
BackgroundFerroportin: Lack of evidence for multimers
Schimanski, L. M., Drakesmith, H., Talbott, C., Horne, K., James, J. R., Davis, S. J., Sweetland, E., Bastin, J. M., Cowley, D., & Townsend, A. (2007) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2007.09.007 · Cited by 30
Self-citationReduced 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
Zhang, W., Xu, A., Li, Y., Zhao, S., Zhou, D., Wu, L., Zhang, B., Zhao, X., Wang, Y., Wang, X., et al. (2019) · Liver International · doi:10.1111/liv.14013 · Cited by 29
Genetic hemochromatosis: Pathophysiology, diagnostic and therapeutic management
Brissot, P., Cavey, T., Ropert, M., Guggenbuhl, P., & Loréal, O. (2017) · La Presse Médicale · doi:10.1016/j.lpm.2017.05.037 · Cited by 55
“Hepcidin modulates the amount of iron release into the plasma by targeting ferroportin, the only known cellular iron exporter [12].”
BackgroundMolecular Mechanisms Regulating Hepcidin Revealed by Hepcidin Disorders
Camaschella, C., & Silvestri, L. (2011) · The Scientific World JOURNAL · doi:10.1100/tsw.2011.130 · Cited by 28
“However, few gain-of-function mutations render ferroportin resistant to the hepcidin effect[33], either because of loss of hepcidin binding or of ferroportin internalization.”
BackgroundMechanisms 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
Review article: the genetic basis of haemochromatosis
Griffiths, W. J. H. (2007) · Alimentary Pharmacology & Therapeutics · doi:10.1111/j.1365-2036.2007.03387.x · Cited by 31
20 years of Hepcidin: How far we have come
Colucci, S., Marques, O., & Altamura, S. (2021) · Seminars in Hematology · doi:10.1053/j.seminhematol.2021.05.001 · 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
“A recent study in cultured cells has provided evidence that some ferroportin1 mutations result in incorrect membrane targeting of the protein or correctly targeted protein that is defective in iron transport [ 31 ].”
BackgroundA novel mutation in ferroportin implicated in iron overload
Wallace, D. F., Dixon, J. L., Ramm, G. A., Anderson, G. J., Powell, L. W., & Subramaniam, V. N. (2007) · Journal of Hepatology · doi:10.1016/j.jhep.2007.01.033 · Cited by 27
Clinicopathological study of Japanese patients with genetic iron overload syndromes
Hattori, A., Miyajima, H., Tomosugi, N., Tatsumi, Y., Hayashi, H., & Wakusawa, S. (2012) · Pathology International · doi:10.1111/j.1440-1827.2012.02848.x · Cited by 27
Bach, V., Remacha, A. F., Altés, A., Barceló, M. J., Molina, M. A., & Baiget, M. (2005) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2005.09.001 · Cited by 27
Ferroportin and Erythroid Cells: An Update
Cianetti, L., Gabbianelli, M., & Sposi, N. M. (2010) · Advances in Hematology · doi:10.1155/2010/404173 · Cited by 28
Ka, C., Guellec, J., Pepermans, X., Kannengiesser, C., Ged, C., Wuyts, W. A., Cassiman, D. M., de Lédinghen, V., Varet, B. R., de Kerguenec, C., et al. (2018) · Haematologica · doi:10.3324/haematol.2018.189845 · Cited by 25
Speletas, M. G., Kioumi, A., Loules, G., Hytiroglou, P., Tsitouridis, J., Christakis, J. I., & Germenis, A. E. (2007) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2007.09.011 · Cited by 25
“However, these Fpn mutants are resistant to regulation by the hepcidin, an antimicrobial protein, which induces internalization and degradation of wt-Fpn but not of these Fpn mutants, yielding a phenotype similar to classical hemochromatosis, with inappropriately high duodenal absorption of iron, increased transferrin…”
BackgroundZebrafish as a model for defining the functional impact of mammalian ferroportin mutations
Domenico, I. D., Vaughn, M. B., Yoon, D., Kushner, J. P., Ward, D. M., & Kaplan, J. (2007) · Blood · doi:10.1182/blood-2007-07-100248 · Cited by 25
Vaulont, S. (2005) · Journal of Clinical Investigation · doi:10.1172/jci25642 · Cited by 26
Impact of D181V and A69T on the function of ferroportin as an iron export pump and hepcidin receptor
Praschberger, R., Schranz, M., Griffiths, W. J., Baumgartner, N., Hermann, M., Lomas, D. J., Pietrangelo, A., Cox, T. M., Vogel, W., & Zoller, H. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2014.05.011 · Cited by 26
Molecular Mechanisms of Intestinal Iron Transport
Collins, J. F., & Anderson, G. J. (2012) · Elsevier eBooks · doi:10.1016/b978-0-12-382026-6.00071-3 · Cited by 22
Liu, B., Jia, R., Huang, B., & Lei, J. (2017) · Marine and Freshwater Behaviour and Physiology · doi:10.1080/10236244.2017.1360726 · Cited by 21
“The increase of hepcidin can suppress erythropoiesis by iron starvation leading to anemia during inflammation (Drakesmith et al. 2005).”
BackgroundWallace, D. F., McDonald, C. J., Ostini, L., Iser, D. M., Tuckfield, A., & Subramaniam, V. N. (2017) · American Journal of Hematology · doi:10.1002/ajh.24844 · Cited by 21
A novel ferroportin mutation in a Canadian family with autosomal dominant hemochromatosis
Morris, T. J., Litvinova, M. M., Ralston, D., Mattman, A., Holmes, D. T., & Lockitch, G. (2005) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2005.07.007 · Cited by 22
McDonald, C. J., Wallace, D. F., Ostini, L., Bell, S., Demediuk, B., & Subramaniam, V. N. (2010) · Journal of Hepatology · doi:10.1016/j.jhep.2010.07.048 · Cited by 20
Lee, P. L., Gelbart, T., West, C., & Barton, J. C. (2007) · Acta Haematologica · doi:10.1159/000112830 · Cited by 22
“Hemochromatosis phenotypes of persons with SLC40A1 mutations vary depending on the mutation. Those that encode ferroportin that cannot be internalized after hepcidin binding are associated with iron deposition in hepatocytes and elevated transferrin saturation [”
BackgroundWallace, D. F., & Subramaniam, V. N. (2011) · Humana Press eBooks · doi:10.1007/978-1-60327-485-2_20 · Cited by 18
Uguen, K., Ka, C., Collod‐Béroud, G., Tertre, M. L., Guellec, J., Férec, C., Béroud, C., Callebaut, I., & Gac, G. L. (2023) · Human Mutation · doi:10.1155/2023/5162256 · Cited by 21
“The study of few other families [16] and the achievement of in vitro assays [17, 18] then revealed the existence of two functional categories of SLC40A1 gene mutations underlying two distinct clinical entities.”
Han, L., Liu, Y., Lü, M., Wang, H., & Tang, F. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.11.022 · Cited by 17
Stasiak, I. M., Smith, D. A., Ganz, T., Crawshaw, G. J., Hammermueller, J., Bienzle, D., & Lillie, B. N. (2018) · Journal of Comparative Physiology B · doi:10.1007/s00360-018-1155-4 · Cited by 17
Zimmermann, M. B., Harrington, M., Villalpando, S., & Hurrell, R. F. (2009) · American Journal of Clinical Nutrition · doi:10.3945/ajcn.2009.28800 · Cited by 17
Effect of SNPs on iron metabolism
Fairweather‐Tait, S. J., Harvey, L. J., Heath, A. M., & Roe, M. A. (2007) · Genes & Nutrition · doi:10.1007/s12263-007-0007-8 · Cited by 16
“A77D, V162del, G490D) and others (Y64N, C326Y) that are associated with resistance to hepcidin [8].”
BackgroundViveiros, A., Panzer, M., Baumgartner, N., Schaefer, B., Finkenstedt, A., Henninger, B., Theurl, I., Nachbaur, K., Weiß, G., Haubner, R., et al. (2020) · Liver International · doi:10.1111/liv.14539 · Cited by 17
The Molecular Circuitry Regulating the Switch between Iron Deficiency and Overload in Mice
Mok, H., Mlodnicka, A., Hentze, M. W., Muckenthaler, M. U., & Schumacher, A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m509857200 · Cited by 16
Importance of Iron Absorption in Human Health: An Overview
Dixit, S. P., Logesh, R., Palaniswamy, D. S., & Mohankumar, S. K. (2020) · Current Nutrition & Food Science · doi:10.2174/1573401316999200801021752 · Cited by 18
Obesity and iron deficiency in chronic kidney disease: the putative role of hepcidin
Sarafidis, P. A., Rumjon, A., MacLaughlin, H. L., & Macdougall, I. C. (2011) · Nephrology Dialysis Transplantation · doi:10.1093/ndt/gfr686 · Cited by 15
“In reticuloendothelial macrophages, hepcidin was previously shown to bind to the cellular iron export channel ferroportin, inducing its internalization and subsequent degradation [8, 9].”
BackgroundIron chelation with deferasirox in a patient with de-novo ferroportin mutation
Ünal, Ş., Piperno, A., & Gümrük, F. (2015) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2015.01.002 · Cited by 15
Chen, S. ‐., Yang, L. ‐., Chong, Y., Jie, Y., Wu, Y., Yang, J., Lin, G., & Li, X. (2015) · Internal Medicine Journal · doi:10.1111/imj.12764 · Cited by 14
A novel mutation in the SLC40A1 gene associated with reduced iron export in vitro
Moreno‐Carralero, M., Muñoz‐Muñoz, J., Cuadrado‐Grande, N., López‐Rodríguez, R., Hernández‐Alfaro, M. J., del‐Castillo‐Rueda, A., de Salamanca, R. E., Méndez, M., & Morán‐Jiménez, M. (2014) · American Journal of Hematology · doi:10.1002/ajh.23714 · Cited by 14
“Mutations in SLC40A1 gene have different effects on FPN1 protein function: they impair iron trafficking and the hepcidin binding site, and are responsible for variable phenotype presentations [2–4].”
BackgroundInfluentialHepcidin and the anemia of chronic disease.
Haurani, F. I. (2006) · PubMed · Cited by 14
Kasvosve, I., Debebe, Z., Nekhai, S. A., & Gordeuk, V. R. (2010) · Clinica Chimica Acta · doi:10.1016/j.cca.2010.04.031 · Cited by 12
“Other studies indicated that the Q248H allele retains the ability to export iron and respond to hepcidin when expressed in HEK 293T cells [12,13].”
Clark, R. J., Preza, G. C., Tan, C. C., van Dijk, J. W. A., Fung, E., Nemeth, E., Ganz, T., & Craik, D. J. (2013) · Biopolymers · doi:10.1002/bip.22350 · Cited by 12
Yamashita, T., Morotomi, N., Sohda, T., Hayashi, H., Yoshida, N., Ochi, K., Ohkura, I., Karita, M., Fujiwara, H., Yamashita, H., et al. (2014) · Clinical Journal of Gastroenterology · doi:10.1007/s12328-014-0487-1 · Cited by 13
“resistant or completely insensitive to the regulation of hepcidin; certain FP mutations have been shown to exhibit loss-of-function and gain-of-function dichotomy [8, 9].”
BackgroundTFR2-Related Hereditary Hemochromatosis
Gobbi, M. D., & Roetto, A. (2011) · Institutional Research Information System University of Turin (University of Turin) · Cited by 12
Molecular basis of hereditary iron homeostasis defects
Horváthová, M., Ponka, P., & Divoký, V. (2010) · Hematology · doi:10.1179/102453310x12583347009810 · Cited by 12
Gordeuk, V. R., Diaz, S. F., Onojobi, G. O., Kasvosve, I., Debebe, Z., Edossa, A., Pantin, J. M., Xiong, S., Nekhai, S. A., Nouraie, M. S., et al. (2008) · Alcoholism Clinical and Experimental Research · doi:10.1111/j.1530-0277.2008.00782.x · Cited by 10
“Other studies indicated that the Q248H allele retains the ability to export iron and respond to hepcidin when expressed in HEK 293T cells (Drakesmith et al., 2005; Schimanski et al., 2005).”
BackgroundPREVALENCE OF HFE MUTATIONS IN CALIFORNIA NEWBORNS
Hoppe, C. C., Watson, R. M., Long, C. M., Lorey, F., Lara, R., Klitz, W., Styles, L. A., & Vichinsky, E. P. (2006) · Pediatric Hematology and Oncology · doi:10.1080/08880010600751918 · Cited by 12
In vivo role(s) of the iron regulatory proteins (IRP) 1 and 2 in aseptic local inflammation
Viatte, L., Gröne, H.-J., Hentze, M. W., & Galy, B. (2009) · Journal of Molecular Medicine · doi:10.1007/s00109-009-0494-8 · Cited by 11
Uguen, K., Tertre, M. L., Tchernitchko, D., Elbahnsi, A., Maestri, S., Gourlaouen, I., Férec, C., Ka, C., Callebaut, I., & Gac, G. L. (2024) · Human Genetics and Genomics Advances · doi:10.1016/j.xhgg.2024.100335 · Cited by 12
Molecular diagnosis of genetic iron-overload disorders
Brissot, P., Bardou‐Jacquet, E., Troadec, M., Mosser, A., Island, M., Détivaud, L., Loréal, O., & Jouanolle, A. (2010) · Expert Review of Molecular Diagnostics · doi:10.1586/erm.10.55 · Cited by 10
The Crosstalk between Micro RNA and Iron Homeostasis
Li, Z. S. Y. (2013) · International Journal of Genomic Medicine · doi:10.4172/2332-0672.1000112 · Cited by 10
Srai, S. K., & Sharp, P. (2011) · Humana Press eBooks · doi:10.1007/978-1-60327-485-2_1 · Cited by 11
A simple clinical score to promote and enhance ferroportin disease screening
Landemaine, A., Hamdi‐Rozé, H., Cunat, S., Loustaud-Ratti, V., Causse, X., Ahmed, S. N. S., Drénou, B., Bureau, C., Pelletier, G., de Kerguenec, C., et al. (2021) · Journal of Hepatology · doi:10.1016/j.jhep.2021.10.022 · Cited by 10
Tertre, M. L., Ka, C., Raud, L., Berlivet, I., Gourlaouen, I., Richard, G., Uguen, K., Chen, J., Férec, C., Fichou, Y., et al. (2020) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2020.102527 · Cited by 13
Paying the Iron Price: Liver Iron Homeostasis and Metabolic Disease
Ameka, M., & Hasty, A. H. (2022) · Comprehensive physiology · doi:10.1002/cphy.c210039 · Cited by 17
“However, more refined studies in both cell types reveal discreet and salient differences in their ability and capacity to handle iron and lipids and glucose in different contexts (59, 180).”
Iron chelators reverse organ damage in type 4B hereditary hemochromatosis
Wu, L., Song, Z., Li, Q., Mou, L.-J., Yu, Y., Shen, S., & Song, X. (2021) · Medicine · doi:10.1097/md.0000000000025258 · Cited by 7
Hayashi, H., Yano, M., Urawa, N., Mizutani, A., Hamaoka, S., Araki, J., Kojima, Y., Naito, Y., Kato, A., Tatsumi, Y., et al. (2018) · Internal Medicine · doi:10.2169/internalmedicine.0481-17 · Cited by 7
“The altered FPN molecules may therefore resist hepcidin to various degrees due to their vessel-side expression (8).”
BackgroundIron Matryoshka—Haemochromatosis nested in Ferroportin Disease?
Viveiros, A., Schaefer, B., Tilg, H., & Zoller, H. (2019) · Liver International · doi:10.1111/liv.14061 · Cited by 7
Андреева, Т. В., Дмитриевна, С. А., Gusev, F. E., Malyarchuk, A. B., Доценко, Г. С., Dudko, N. A., Plotnikova, M. Y., Станиславовна, К. С., Manakhov, A. D., Ustkachkintseva, T. V., et al. (2025) · Science Advances · doi:10.1126/sciadv.ads8179 · Cited by 8
Tertre, M. L., Elbahnsi, A., Ka, C., Callebaut, I., & Gac, G. L. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22126412 · Cited by 6
“The results presented in Figure 1; Figure 2 suggest that the Asp325-Arg40 inter-lobe interaction could be a key in the dynamics of the human FPN1 extracellular gate and in the stability of the iron exporter at the cell surface, whereas the Asp325-Cys326 interaction is also very important from a functional point of vie…”
BackgroundResultWolff, F., Bailly, B., Gulbis, B., & COTTON, F. J. (2013) · Clinica Chimica Acta · doi:10.1016/j.cca.2013.12.024 · Cited by 6
Sarıkaya, B., Dursun, A. D., DEVEDEN, E. Y. T., & Pınar, L. (2017) · TURKISH JOURNAL OF MEDICAL SCIENCES · doi:10.3906/sag-1703-73 · Cited by 6
“Severe exercise yields an increase in cytokine production, especially that of IL-6, which is the predominate mediator of the iron regulatory hormone hepcidin (6).”
BackgroundGenetic biases related to chronic venous ulceration
Stana, J., Maver, U., & Potočnik, U. (2019) · Journal of Wound Care · doi:10.12968/jowc.2019.28.2.59 · Cited by 7
Clinical management of hemochromatosis: current perspectives
Brissot, P., Cavey, T., Ropert, M., Guggenbuhl, P., & Loréal, O. (2017) · International Journal of Clinical Transfusion Medicine · doi:10.2147/ijctm.s105214 · Cited by 6
“Then, a hepcidin resistance state develops 13 whose consequences are similar to those following true plasma hepcidin deficiency (type 4B HC).”
Kondo, S., Ferdousi, F., Zhao, J., Suidasari, S., Yokozawa, M., Yamauchi, K., Tominaga, K., & Isoda, H. (2023) · Nutrients · doi:10.3390/nu15194095 · Cited by 6
“Additionally, changes in plasma iron and renal Hif1a between 17 and 24 days may have been negative feedback of HAMP and HIF degradation under normoxia to maintain homeostasis in the blood environment [33,34].”
BackgroundHepcidin: looking back at two decades of progress
Ganz, T. (2022) · Nature Cardiovascular Research · doi:10.1038/s44161-022-00034-8 · Cited by 5
Liver Disease in Iron Overload
Guindi, M. M. (2018) · Elsevier eBooks · doi:10.1016/b978-0-323-42873-6.00011-1 · Cited by 4
Tertre, M. L., Ka, C., Guellec, J., Gourlaouen, I., Férec, C., Callebaut, I., & Gac, G. L. (2017) · Transfusion Clinique et Biologique · doi:10.1016/j.tracli.2017.07.002 · Cited by 5
Metadata
- Authors
- 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., Robson, K. J. H., & Townsend, A. R. M.
- Affiliations
- Siriraj Hospital (TH)
- From the Weatherall Institute of Molecular Medicine, Oxford, United Kingdom; Medical Research Council Molecular Haematology Unit, Weatherall Institute of Molecular Medicine, Oxford, United Kingdom; Department of Paediatrics, Faculty of Medicine, Siriraj Hospital, Mahidol University, Bangkok, Thailand; and Department of Internal Medicine, Faculty of Medicine, Siriraj Hospital, Mahidol University, Bangkok, Thailand.
- ORCID
- Venue
- Blood
- Publisher
- American Society of Hematology
- Published
- 2005-08-01
- Volume
- 106
- Issue
- 3
- Pages
- 1092-1097
- ISSN
- 0006-4971 (ISSN-L)
- 1528-0020
- OpenAlex
- W2131823953
- Cited by
- 264
- References
- 34
- Citations by year
- 2026: 1 · 2025: 3 · 2024: 3 · 2023: 4 · 2022: 6 · 2021: 6 · 2020: 9 · 2019: 9 · 2018: 13 · 2017: 14 · 2016: 11 · 2015: 9 · 2014: 10 · 2013: 14 · 2012: 11
- FWCI
- 15.95
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Blood (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Wellcome Trust
- Topics
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Life Sciences › Neuroscience › Neurology › Neurological diseases and metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Ferroptosis and cancer prognosis
- Keywords
- ferroportin, hepcidin, hemochromatosis, iron export, iron overload, transferrin saturation, Kupffer cells, liver iron deposition, iron homeostasis
- MeSH terms
- Ferroportin, Cell Line, Drug Resistance, Gene Expression Regulation, Hemochromatosis, Humans, Iron, Iron Radioisotopes, Transferrin, Mutation, Missense, 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 ›
Are you an author, or do you see a problem with this page? Request a review
