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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.
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“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]
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Regulation of Hepcidin by Erythropoiesis: The Story So Far
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“Most forms of genetic hemochromatosis are caused by mutations in genes (HFE, HFE2, TFR2) that regulate hepcidin synthesis, resulting in an inability to produce sufficient hepcidin to achieve iron homeostasis and prevent iron overload, or more rarely by mutations in ferroportin that confer resistance to inhibition by h…”
BackgroundSelf-citationWallace, D. F., Harris, J. M., & Subramaniam, V. N. (2009) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00621.2008 · Cited by 84
Chung, B., Chaston, T. B., Marks, J., Srai, S. K., & Sharp, P. (2009) · Journal of Nutrition · doi:10.3945/jn.108.102905 · Cited by 78
New insights into the regulation of iron homeostasis
Deicher, R., & Hörl, W. H. (2006) · European Journal of Clinical Investigation · doi:10.1111/j.1365-2362.2006.01633.x · Cited by 80
The overlapping of local iron overload and HFE mutation in venous leg ulcer pathogenesis
Zamboni, P., Izzo, M., Tognazzo, S., Carandina, S., De Palma, M., Catozzi, L., Caggiati, A., Scapoli, G., & Gemmati, D. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.01.026 · Cited by 76
Sham, R. L., Phatak, P. D., Nemeth, E., & Ganz, T. (2009) · Blood · doi:10.1182/blood-2009-04-216226 · Cited by 74
Hepcidin and Ferroportin: The New Players in Iron Metabolism
De Domenico, I., Ward, D., & Kaplan, J. (2011) · Seminars in Liver Disease · doi:10.1055/s-0031-1286058 · Cited by 71
“The high levels of FPN result from decreased FPN degradation in response to the hormone hepcidin.(7,16,21) Hepcidin resistance leads to continued iron export through FPN independent of hepcidin levels.”
Hepcidin: Homeostasis and Diseases Related to Iron Metabolism
Reichert, C. O., da Cunha, J., Levy, D., Maselli, L. M. F., Bydlowski, S. P., & Spada, C. (2017) · Acta Haematologica · doi:10.1159/000471838 · Cited by 77
Evidence for the multimeric structure of ferroportin.
De Domenico, I., Ward, D. M., Musci, G., & Kaplan, J. (2007) · Blood · doi:10.1182/blood-2006-06-032516 · Cited by 72
Genetic and clinical heterogeneity of ferroportin disease
Cemonesi, L., Forni, G. L., Soriani, N., Lamagna, M., Fermo, I., Daraio, F., Gallì, A., Pietra, D., Malcovati, L., Ferrari, M., et al. (2005) · British Journal of Haematology · doi:10.1111/j.1365-2141.2005.05815.x · Cited by 74
“Recent studies have clarified the molecular basis of this phenotypic heterogeneity (De Domenico et al, 2005; Drakesmith et al, 2005; Schimanski et al, 2005).”
BackgroundHepcidin 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
Armitage, A. E., & Moretti, D. (2019) · Pharmaceuticals · doi:10.3390/ph12020059 · Cited by 76
“Likewise, patients with “gain-of-function” ferroportin mutations (rendering ferroportin hepcidin-resistant) develop iron overload [43,44].”
BackgroundIron homeostasis: new players, newer insights
Edison, E. S., Bajel, A. R., & Chandy, M. (2008) · European Journal Of Haematology · doi:10.1111/j.1600-0609.2008.01143.x · Cited by 71
“FPN mutants may reach the membrane but are resistant to the action of hepcidin, resulting in hepcidin resistance, and a HH like phenotype (107).”
BackgroundNairz, M., Schroll, A., Haschka, D., Dichtl, S., Sonnweber, T., Theurl, I., Theurl, M., Lindner, E., Demetz, E., Aßhoff, M., et al. (2015) · European Journal of Immunology · doi:10.1002/eji.201545569 · Cited by 67
Pathophysiology of Hereditary Hemochromatosis
Fleming, R. E., Britton, R. S., Waheed, A., Sly, W. S., & Bacon, B. R. (2005) · Seminars in Liver Disease · doi:10.1055/s-2005-923313 · Cited by 68
Mayr, R., Griffiths, W. J. H., Hermann, M., McFarlane, I., Halsall, D. J., Finkenstedt, A., Douds, A., Davies, S. E., Janecke, A. R., Vogel, W., et al. (2011) · Gastroenterology · doi:10.1053/j.gastro.2011.02.064 · Cited by 64
Hepcidin: an important new regulator of iron homeostasis
Hugman, A. (2006) · Clinical & Laboratory Haematology · doi:10.1111/j.1365-2257.2006.00768.x · Cited by 62
“The phenotype varies depending on the type of FPN mutant and its susceptibility to inhibition by hepcidin (Drakesmith et al., 2005).”
BackgroundThe molecular basis of iron overload disorders and iron-linked anemias
Kaplan, J., Ward, D. M., & Domenico, I. D. (2011) · International Journal of Hematology · doi:10.1007/s12185-010-0760-0 · Cited by 62
Gac, G. L., Ka, C., Joubrel, R., Gourlaouen, I., Lehn, P., Mornon, J., Férec, C., & Callebaut, I. (2013) · Human Mutation · doi:10.1002/humu.22369 · Cited by 67
“…to that of the p.Asn144His mutation, which, in contrast to the p.Cys326Tyr mutation, is known to cause resistance to hepcidin in a manner that does not directly depend on the binding of the liver peptide to ferroportin [De Domenico et al., 2005; Drakesmith et al., 2005; Fernandes et al., 2009].”
BackgroundInfluentialSex and Acquired Cofactors Determine Phenotypes of Ferroportin Disease
Lan, C. L., Mosser, A., Ropert, M., Détivaud, L., Loustaud-Ratti, V., Vital-Durand, D., Roget, L. D.-P., Bardou‐Jacquet, E., Turlin, B., David, V., et al. (2011) · Gastroenterology · doi:10.1053/j.gastro.2010.12.049 · Cited by 66
Primary iron overload with inappropriate hepcidin expression in V162del ferroportin disease†
Zoller, H., McFarlane, I., Theurl, I., Stadlmann, S., Nemeth, E., Oxley, D., Ganz, T., Halsall, D. J., Cox, T. M., & Vogel, W. (2005) · Hepatology · doi:10.1002/hep.20775 · Cited by 62
Towards explaining "unexplained hyperferritinemia"
Camaschella, C., & Poggiali, E. (2009) · Haematologica · doi:10.3324/haematol.2008.005405 · Cited by 61
“The true ferroportin disease (hemochromatosis type 4a in Table 1) is due to mutant proteins that are not correctly targeted to the cell surface and is characterized by macrophage iron accumulation, low/normal transferrin saturation and iron-restricted erythropoiesis.(6) A second form (hemochromatosis type 4b), due to…”
BackgroundInteractions Between Ferroportin and Hephaestin in Rat Enterocytes Are Reduced After Iron Ingestion
Yeh, K., YEH, M. K. Y., & Glass, J. (2011) · Gastroenterology · doi:10.1053/j.gastro.2011.03.059 · Cited by 57
Magnetic resonance imaging to identify classic and nonclassic forms of ferroportin disease
Pietrangelo, A., Corradini, E., Ferrara, F., Vegetti, A., Jong, G. D., Abbati, G. L., Arcuri, P. P., Martinelli, S., & Cerofolini, E. (2006) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2006.08.007 · Cited by 61
Human macrophage ferroportin biology and the basis for the ferroportin disease
Sabelli, M., Montosi, G., Garuti, C., Caleffi, A., Oliveto, S., Biffo, S., & Pietrangelo, A. (2016) · Hepatology · doi:10.1002/hep.29007 · Cited by 60
“A number of in vitro studies, mostly using overexpressed exogenous wild-type (WT) and mutant FPN1 in a variety of cell lines, have investigated FPN1 biology and function and have provided valuable information on the effect of different FPN1 mutants on protein traffic and iron transfer capability.((3,5-7,9,12,20-26)) I…”
BackgroundVlasveld, L. T., Janssen, R., Bardou-Jacquet, E., Venselaar, H., Hamdi-Roze, H., Drakesmith, H., & Swinkels, D. W. (2019) · Pharmaceuticals · doi:10.3390/ph12030132 · Cited by 57
“The membrane expression of variant ferroportin proteins was determined by surface biotinylation and Western blotting [8,39], immunofluorescence [6,31–33,40,42,46,55–57,65,87] and confocal microscopy [11,34,41,83], or flow cytometry [31,35,41,42,56].”
BackgroundMethodResultInfluentialSelf-citationDNA-array of gene variants in venous leg ulcers: Detection of prognostic indicators
Gemmati, D., Federici, F., Catozzi, L., Gianesini, S., Tacconi, G., Scapoli, G. L., & Zamboni, P. (2009) · Journal of Vascular Surgery · doi:10.1016/j.jvs.2009.07.103 · Cited by 57
Chapter 6 Iron Homeostasis and Erythropoiesis
Wrighting, D. M., & Andrews, N. C. (2008) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/s0070-2153(07)00006-3 · Cited by 59
Pietrangelo, A. (2006) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.26.061505.111226 · Cited by 57
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
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