Two to tango: Regulation of Mammalian iron metabolism

Hentze, Matthias W.; Muckenthaler, Martina U.; Galy, Bruno; Camaschella, Clara

doi:10.1016/j.cell.2010.06.028

Cited by 2,120Iron Metabolism and DisordersFerroptosis and cancer prognosisNeurological diseases and metabolism

Two to tango: Regulation of Mammalian iron metabolism

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Hentze, Matthias W., Muckenthaler, Martina U., Galy, Bruno, Camaschella, Clara·2010·Cell

DOI 10.1016/j.cell.2010.06.028

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Abstract

Disruptions in iron homeostasis from both iron deficiency and overload account for some of the most common human diseases. Iron metabolism is balanced by two regulatory systems, one that functions systemically and relies on the hormone hepcidin and the iron exporter ferroportin, and another that predominantly controls cellular iron metabolism through iron-regulatory proteins that bind iron-responsive elements in regulated messenger RNAs. We describe how the two distinct systems function and how they "tango" together in a coordinated manner. We also highlight some of the current questions in mammalian iron metabolism and discuss therapeutic opportunities arising from a better understanding of the underlying biological principles.

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Serum ferritin is a marker of acute and chronic inflammatory conditions and can be markedly elevated in persons with average iron storage in many medical conditions.
“It is worth noting that SF is a marker of acute and chronic inflammatory conditions that can be markedly elevated in persons with average iron storage in many different medical conditions, such as rheumatoid arthritis, systemic lupus erythematosus, chronic kidney disease, hepatitis, excessive alcohol consumption, heart failure, acute infection, intestinal disorders such as coeliac disease, obesity”
From Defining Global Thresholds for Serum Ferritin: A Challenging Mission in Establishing the Iron Deficiency Diagnosis in This Era of Striving for Health Equity (2025) · cites this paper as [11]
The section “Plasma Iron: Key to Iron Overload and Iron Deficiency Anemias” (p. 1) says inflammatory conditions, infections, cancer, and liver disorders can increase serum ferritin, even though ferritin is used to assess iron stores. It does not establish that elevations are marked in people with average iron stores, or link serum ferritin to most of the specific conditions listed in the citing sentence. (LLM, conf=0.86)
Experimental — accuracy not yet measured
Under physiological conditions iron recycling by macrophages accounts for approximately 95% of the daily needs of the metal for erythropoiesis and other physiological processes.
“Under physiological conditions iron recycling by macrophages accounts for approximately 95% of the daily needs of the metal for erythropoiesis and other physiological processes (Hentze et al., 2010; Pantopoulos et al., 2012).”
From Iron at the interface of immunity and infection (2014) · cites this paper as Hentze et al., 2010
Hepcidin expression is inhibited by iron deficiency, expansion of erythropoiesis, anemia/hypoxia, testosterone and possibly other factors.
“Hepcidin expression is inhibited by iron deficiency, expansion of erythropoiesis, anemia/hypoxia, testosterone and possibly other factors.1,47”
From Iron metabolism and iron disorders revisited in the hepcidin era (2020) · cites this paper as [1]
When intracellular iron is low, IRPs interact with conserved IREs in the UTRs of central genes accounting for iron homeostasis.
“When intracellular iron is low, IRPs interact with conserved iron-responsive elements (IREs) in the untranslated regions (UTRs) of central genes accounting for iron homeostasis [32,33].”
From Iron as a central player and promising target in cancer progression (2019) · cites this paper as [32]
The amount of the LIP is sensed by post-transcriptional mechanisms of IRP-1 and IRP-2 to fine-tune uptake, storage, and release of iron.
“The amount of the LIP is sensed by post-transcriptional mechanisms of cytosolic iron-regulated RNA binding proteins 1 and 2 (IRP-1 and IRP-2) to fine-tune uptake, storage, and release of iron.”
From Iron as a central player and promising target in cancer progression (2019) · cites this paper as [32]

Binding of IRPs to IREs in the 5'-UTR attenuates translation, whereas binding to IREs in the 3'-UTR stabilizes respective mRNAs and fosters translation.
“Binding of IRPs to IREs in the 5’-UTR attenuates translation, whereas binding to IREs in the 3’-UTR stabilizes respective mRNAs and fosters translation.”
From Iron as a central player and promising target in cancer progression (2019) · cites this paper as [32]
LPS stimulation increased binding of IRPs to a radiolabeled IRE RNA probe, indicative of reduced cytosolic Fe availability.
“However, gel retardation assays demonstrated that LPS stimulation increased binding of iron-regulatory proteins (IRPs) to a radiolabeled iron responsive element (IRE) RNA probe (Figure 3B), indicative of reduced cytosolic Fe availability (Hentze et al., 2010).”
From Ferritin-Mediated Iron Sequestration Stabilizes Hypoxia-Inducible Factor-1α upon LPS Activation in the Presence of Ample Oxygen (2015) · cites this paper as Hentze et al., 2010
Hepcidin promotes Fpn1 internalization and degradation.
“This appears to be the result of increased expression of the master iron regulator hepcidin, which promotes Fpn1 internalization and degradation (1, 36).”
From Dopamine Is a Siderophore-Like Iron Chelator That Promotes Salmonella enterica Serovar Typhimurium Virulence in Mice (2019) · cites this paper as [1]
Iron stores, particularly ferritin-associated iron in liver and spleen, can become depleted during chronic bleeding episodes, repetitive blood donations, helminth infestations, materno-fetal transfer, or growth.
“Due to this relatively inefficient process, iron stores, particularly ferritin-associated iron in liver and spleen, can become depleted during chronic bleeding episodes, repetitive blood donations, helminth infestations, through materno-fetal transfer, or during growth [5].”
From Iron deficiency or anemia of inflammation?: Differential diagnosis and mechanisms of anemia of inflammation (2016) · cites this paper as [5]
Peripheral cellular iron uptake mainly involves endocytosis of the diferric transferrin-transferrin receptor 1 complex, and iron is then transported from endosomes into the cell cytoplasm via divalent metal ion transporter 1.
“Peripheral cellular iron uptake mainly involves endocytosis of the diferric transferrin–transferrin receptor 1 (TFR1; panel) complex; iron is then transported from the endosomes into the cell cytoplasm via the divalent metal ion transporter 1 (DMT1; panel).”
From The role of iron in brain ageing and neurodegenerative disorders (2014) · cites this paper as [2]
Iron homoeostasis is needed to maintain normal physiological brain function.
“Iron homoeostasis is needed to maintain normal physiological brain function, whereas misregulation of iron homoeostasis can cause neurotoxicity through different mechanisms.”
From The role of iron in brain ageing and neurodegenerative disorders (2014) · cites this paper as [2]
Misregulation of iron homoeostasis can cause neurotoxicity through different mechanisms.
“Iron homoeostasis is needed to maintain normal physiological brain function, whereas misregulation of iron homoeostasis can cause neurotoxicity through different mechanisms.”
From The role of iron in brain ageing and neurodegenerative disorders (2014) · cites this paper as [2]

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Altered body iron distribution and microcytosis in mice deficient in iron regulatory protein 2 (IRP2)
Galy, B., Ferring–Appel, D., Miñana, B., Bell, O., Janser, H., Muckenthaler, M. U., Schümann, K., & Hentze, M. W. (2005) · Blood · doi:10.1182/blood-2005-04-1365 · Cited by 222 · see citing works
Self-citation
Abcb10 physically interacts with mitoferrin-1 (Slc25a37) to enhance its stability and function in the erythroid mitochondria
Chen, W., Paradkar, P. N., Li, L., Pierce, E. L., Langer, N. B., Takahashi‐Makise, N., Hyde, B. B., Shirihai, O. S., Ward, D. M., Kaplan, J., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0904519106 · Cited by 220 · see citing works
TIM-2 is expressed on B cells and in liver and kidney and is a receptor for H-ferritin endocytosis
Chen, T. T., Li, L., Chung, D.-H., Allen, C. D. C., Torti, S. V., Torti, F. M., Cyster, J. G., Chen, C.-Y., Brodsky, F. M., Niemi, E. C., et al. (2005) · The Journal of Experimental Medicine · doi:10.1084/jem.20042433 · Cited by 219 · see citing works
Hepcidin Revisited, Disulfide Connectivity, Dynamics, and Structure
Jordan, J. B., Poppe, L., Haniu, M., Arvedson, T., Syed, R., Li, V., Kohno, H., Kim, H., Schnier, P. D., Harvey, T. S., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.017764 · Cited by 214 · see citing works
Elucidation of the mechanism of mitochondrial iron loading in Friedreich's ataxia by analysis of a mouse mutant
Huang, M. L.-H., Becker, E. M., Whitnall, M., Rahmanto, Y. S., Ponka, P., & Richardson, D. R. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0906784106 · Cited by 212 · see citing works
Combined deletion of Hfe and transferrin receptor 2 in mice leads to marked dysregulation of hepcidin and iron overload†
Wallace, D. F., Summerville, L., Crampton, E. M., Frazer, D. M., Anderson, G. J., & Subramaniam, V. N. (2009) · Hepatology · doi:10.1002/hep.23198 · Cited by 206 · see citing works
Iron regulatory proteins are essential for intestinal function and control key iron absorption molecules in the duodenum
Galy, B., Ferring-Appel, D., Kaden, S., Gröne, H.-J., & Hentze, M. W. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2007.10.006 · Cited by 195 · see citing works
Self-citation
Understanding iron homeostasis through genetic analysis of hemochromatosis and related disorders
Camaschella, C. (2005) · Blood · doi:10.1182/blood-2005-05-1857 · Cited by 194 · see citing works
Self-citation
BMP-6 Is an Autocrine Stimulator of Chondrocyte Differentiation
Grimsrud, C. D., Romano, P. R., D’Souza, M., et al. (1999) · Journal of Bone and Mineral Research · doi:10.1359/jbmr.1999.14.4.475 · Cited by 185 · 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
The molecular basis of hepcidin-resistant hereditary hemochromatosis
Fernandes, A. O., Preza, G. C., Phung, Y., Domenico, I. D., Kaplan, J., Ganz, T., & Nemeth, E. (2009) · Blood · doi:10.1182/blood-2008-03-146134 · Cited by 166 · see citing works
Contribution of STAT3 and SMAD4 pathways to the regulation of hepcidin by opposing stimuli
Huang, H., Constante, M., Layoun, A., & Santos, M. M. (2009) · Blood · doi:10.1182/blood-2008-08-173641 · Cited by 164 · see citing works
Down-regulation of Bmp/Smad signaling by Tmprss6 is required for maintenance of systemic iron homeostasis
Finberg, K. E., Whittlesey, R. L., Fleming, M. D., & Andrews, N. C. (2010) · Blood · doi:10.1182/blood-2009-05-224808 · Cited by 162 · see citing works
Bone morphogenetic protein (BMP)-responsive elements located in the proximal and distal hepcidin promoter are critical for its response to HJV/BMP/SMAD
Casanovas, G., Mleczko-Sanecka, K., Altamura, S., Hentze, M. W., & Muckenthaler, M. U. (2009) · Journal of Molecular Medicine · doi:10.1007/s00109-009-0447-2 · Cited by 161 · see citing works
Self-citation
Ca2+ channel blockers reverse iron overload by a new mechanism via divalent metal transporter-1
Ludwiczek, S., Theurl, I., Muckenthaler, M. U., Jakab, M., Mair, S. M., Theurl, M., Kiss, J., Paulmichl, M., Hentze, M. W., Ritter, M., et al. (2007) · Nature Medicine · doi:10.1038/nm1542 · Cited by 160 · see citing works
Self-citation
Molecular basis of inherited microcytic anemia due to defects in iron acquisition or heme synthesis
Iolascon, A., Falco, L. D., & Beaumont, C. (2009) · Haematologica · doi:10.3324/haematol.13619 · Cited by 153 · see citing works
Optimal sequence and structure of iron-responsive elements. Selection of RNA stem-loops with high affinity for iron regulatory factor
Henderson, B. R., Menotti, E., Bonnard, C., & Kühn, L. C. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32466-3 · Cited by 151 · see citing works
Blunted hepcidin response to oral iron challenge in HFE-related hemochromatosis
Piperno, A., Girelli, D., Nemeth, E., Trombini, P., Bozzini, C., Poggiali, E., Phung, Y., Ganz, T., & Camaschella, C. (2007) · Blood · doi:10.1182/blood-2007-06-096503 · Cited by 149 · see citing works
Self-citation
Iron regulatory proteins secure mitochondrial iron sufficiency and function
Galy, B., Ferring-Appel, D., Sauer, S. W., Kaden, S., Lyoumi, S., Puy, H., Kölker, S., Gröne, H.-J., & Hentze, M. W. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.06.007 · Cited by 147 · see citing works
Self-citation
Hepcidin-induced internalization of ferroportin requires binding and cooperative interaction with Jak2
Domenico, I. D., Lo, E., Ward, D. M., & Kaplan, J. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0900453106 · Cited by 143 · see citing works
Bone Morphogenetic Protein Signaling Is Impaired in an Hfe Knockout Mouse Model of Hemochromatosis
Corradini, E., Garuti, C., Montosi, G., Ventura, P., Andriopoulos, B., Lin, H. Y.-F., Pietrangelo, A., & Babitt, J. L. (2009) · Gastroenterology · doi:10.1053/j.gastro.2009.06.057 · Cited by 140 · see citing works
Differences in the RNA binding sites of iron regulatory proteins and potential target diversity.
Butt, J., Kim, H. Y., Basilion, J. P., Cohen, S., Iwaï, K., Philpott, C. C., Altschul, S. F., Klausner, R. D., & Rouault, T. A. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.9.4345 · Cited by 139 · see citing works
Neogenin inhibits HJV secretion and regulates BMP-induced hepcidin expression and iron homeostasis
Lee, D., Zhou, L.-J., Zhou, Z., Xie, J., Jung, J.-U., Liu, Y., Xi, C.-X., Mei, L., & Xiong, W. (2010) · Blood · doi:10.1182/blood-2009-11-251199 · Cited by 139 · see citing works
Macrophages function as a ferritin iron source for cultured human erythroid precursors
Leimberg, M. J., Prus, E., Konijn, A. M., & Fibach, E. (2007) · Journal of Cellular Biochemistry · doi:10.1002/jcb.21499 · Cited by 137 · see citing works
Activation of iron regulatory protein-1 by oxidative stress in vitro
Pantopoulos, K., & Hentze, M. W. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.18.10559 · Cited by 129 · see citing works
Self-citation
Hepcidin, 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
Iron Regulatory Proteins: From Molecular Mechanisms to Drug Development
Recalcati, S., Minotti, G., & Cairo, G. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2983 · Cited by 123 · see citing works
Complete loss of iron regulatory proteins 1 and 2 prevents viability of murine zygotes beyond the blastocyst stage of embryonic development
Smith, S., Ghosh, M. C., Ollivierre, H., Tong, W. H., & Rouault, T. A. (2006) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2005.12.006 · Cited by 123 · see citing works
SMAD7 controls iron metabolism as a potent inhibitor of hepcidin expression
Mleczko‐Sanecka, K., Casanovas, G., Ragab, A., Breitkopf, K., Müller, A., Boutros, M., Dooley, S., Hentze, M. W., & Muckenthaler, M. U. (2009) · Blood · doi:10.1182/blood-2009-09-238105 · Cited by 120 · see citing works
Self-citation
BMP/Smad signaling is not enhanced in Hfe-deficient mice despite increased Bmp6 expression
Kautz, L., Meynard, D., Besson‐Fournier, C., Darnaud, V., Saati, T. A., Coppin, H., & Roth, M. (2009) · Blood · doi:10.1182/blood-2009-02-206771 · Cited by 110 · see citing works
ER Stress-Inducible Factor CHOP Affects the Expression of Hepcidin by Modulating C/EBPalpha Activity
Oliveira, S. J., Pinto, J. P., Picarote, G., Costa, V. M., Carvalho, F. D., Rangel, M., de Sousa, M. A. B., & de Almeida, S. F. (2009) · PLoS ONE · doi:10.1371/journal.pone.0006618 · Cited by 101 · see citing works
The role of Dcytb in iron metabolism: an update
McKie, A. T. (2008) · Biochemical Society Transactions · doi:10.1042/bst0361239 · Cited by 101 · see citing works
A mutation in Sec15l1 causes anemia in hemoglobin deficit (hbd) mice
Lim, J. E., Jin, O., Bennett, C. M., Morgan, K. J., Wang, F., Trenor, C. C., Fleming, M. D., & Andrews, N. C. (2005) · Nature Genetics · doi:10.1038/ng1659 · Cited by 97 · see citing works
Hepcidin, a key regulator of iron metabolism, is transcriptionally activated by p53
Weizer‐Stern, O., Adamsky, K., Margalit, O., Ashur‐Fabian, O., Givol, D., Amariglio, N., & Rechavi, G. (2007) · British Journal of Haematology · doi:10.1111/j.1365-2141.2007.06638.x · Cited by 94 · see citing works
Alterations of systemic and muscle iron metabolism in human subjects treated with low-dose recombinant erythropoietin
Robach, P., Recalcati, S., Girelli, D., Gelfi, C., Aachmann‐Andersen, N. J., Thomsen, J. J., Norgaard, A. M., Alberghini, A., Campostrini, N., Castagna, A., et al. (2009) · Blood · doi:10.1182/blood-2008-09-178095 · Cited by 86 · see citing works
Hepatocyte-targeted HFE and TFR2 control hepcidin expression in mice
Gao, J., Chen, J., Domenico, I. D., Koeller, D. M., Harding, C. O., Fleming, R. E., Koeberl, D. D., & Enns, C. A. (2010) · Blood · doi:10.1182/blood-2009-09-245209 · Cited by 79 · see citing works
Molecular and pathological basis of aceruloplasminemia
Kono, S., & Miyajima, H. (2006) · Biological Research · doi:10.4067/s0716-97602006000100003 · Cited by 79 · see citing works
Oxidative stress and cell death in cells expressing L-ferritin variants causing neuroferritinopathy
Cozzi, A., Rovelli, E., Frizzale, G., Campanella, A., Amendola, M., Arosio, P., & Levi, S. (2009) · Neurobiology of Disease · doi:10.1016/j.nbd.2009.09.009 · Cited by 78 · see citing works
Multiple determinants within iron-responsive elements dictate iron regulatory protein binding and regulatory hierarchy
Goforth, J. B., Anderson, S. A., Nizzi, C. P., & Eisenstein, R. S. (2010) · RNA · doi:10.1261/rna.1857210 · Cited by 71 · see citing works
Voltage-gated Calcium Channels Provide an Alternate Route for Iron Uptake in Neuronal Cell Cultures
Gaasch, J. A., Geldenhuys, W. J., Lockman, P. R., Allen, D. D., & der Schyf, C. J. V. (2007) · Neurochemical Research · doi:10.1007/s11064-007-9313-1 · Cited by 65 · see citing works
Transferrin-a modulates hepcidin expression in zebrafish embryos
Fraenkel, P. G., Gibert, Y., Holzheimer, J., Lattanzi, V. J., Burnett, S. F., Dooley, K. A., Wingert, R. A., & Zon, L. I. (2008) · Blood · doi:10.1182/blood-2008-06-165340 · Cited by 64 · see citing works
Suppression of the hepcidin‐encoding gene Hamp permits iron overload in mice lacking both hemojuvelin and matriptase‐2/TMPRSS6
Truksa, J., Gelbart, T., Peng, H., Beutler, E., Beutler, B., & Lee, P. L. (2009) · British Journal of Haematology · doi:10.1111/j.1365-2141.2009.07873.x · Cited by 63 · see citing works
The power plant of the cell is also a smithy: The emerging role of mitochondria in cellular iron homeostasis
Sheftel, A. D., & Lill, R. (2008) · Annals of Medicine · doi:10.1080/07853890802322229 · Cited by 48 · see citing works
Human heme oxygenase‐1 deficiency: A lesson on serendipity in the discovery of the novel disease
Koizumi, S. (2007) · Pediatrics International · doi:10.1111/j.1442-200x.2007.02353.x · Cited by 41 · see citing works
Microelectronic DNA chip for hereditary hyperferritinemia cataract syndrome, a model for large-scale analysis of disorders of iron metabolism
Ferrari, F., Foglieni, B., Arosio, P., Camaschella, C., Daraio, F., Levi, S., García‐Erce, J. A., Beaumont, C., Cazzola, M., Ferrari, M., et al. (2006) · Human Mutation · doi:10.1002/humu.20294 · Cited by 39 · see citing works
Self-citation
Hepcidin Activation During Inflammation: Make It STAT
Fleming, R. E. (2007) · Gastroenterology · doi:10.1053/j.gastro.2006.11.049 · Cited by 36 · see citing works
Genes determining blood cell traits
Andrews, N. C. (2009) · Nature Genetics · doi:10.1038/ng1109-1161 · Cited by 33 · see citing works
The distal location of the iron responsive region of the hepcidin promoter
Truksa, J., Lee, P. L., Peng, H., Flanagan, J. M., & Beutler, E. (2007) · Blood · doi:10.1182/blood-2007-05-091108 · Cited by 29 · see citing works

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ROS Are Good
Mittler, R. (2017) · Trends in Plant Science · doi:10.1016/j.tplants.2016.08.002 · Cited by 3,499 · see citing works
Insights into RNA Biology from an Atlas of Mammalian mRNA-Binding Proteins
Castello, A., Fischer, B., Eichelbaum, K., Horos, R., Beckmann, B. M., Strein, C., Davey, N. E., Humphreys, D. T., Preiss, T., Steinmetz, L. M., et al. (2012) · Cell · doi:10.1016/j.cell.2012.04.031 · Cited by 2,132 · see citing works
Self-citation
The role of iron in brain ageing and neurodegenerative disorders
Ward, R. J., Zucca, F. A., Duyn, J. H., Crichton, R. R., & Zecca, L. (2014) · The Lancet Neurology · doi:10.1016/s1474-4422(14)70117-6 · Cited by 1,819 · see citing works
Fueling Immunity: Insights into Metabolism and Lymphocyte Function
Pearce, E. L., Poffenberger, M. C., Chang, C.-H., & Jones, R. G. (2013) · Science · doi:10.1126/science.1242454 · Cited by 1,363 · see citing works
Hepcidin and iron homeostasis
Ganz, T., & Nemeth, E. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.01.014 · Cited by 1,282 · see citing works
Systemic Iron Homeostasis
Ganz, T. (2013) · Physiological Reviews · doi:10.1152/physrev.00008.2013 · Cited by 1,122 · see citing works
Regulation of cellular iron metabolism
Wang, J., & Pantopoulos, K. (2011) · Biochemical Journal · doi:10.1042/bj20101825 · Cited by 986 · see citing works
Iron metabolism and iron disorders revisited in the hepcidin era
Camaschella, C., Nai, A., & Silvestri, L. (2020) · Haematologica · doi:10.3324/haematol.2019.232124 · Cited by 734 · see citing works
“Binding to its ubiquitous receptor TFR1, transferrin delivers iron to cells through the wellknown endosomal cycle.(1) This function is crucial not only for erythropoiesis, but also for muscle(4) and for B- and Tlymphocytes, as highlighted by a TFR1 homozygous mutation that causes combined immunodeficiency with only mi…”
Self-citation
Iron Homeostasis and Ferroptosis in Human Diseases: Mechanisms and Therapeutic Prospects
Ru, Q., Li, Y., Chen, L., Wu, Y., Min, J., & Wang, F. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-01969-z · Cited by 724 · see citing works
HSPB1 as a novel regulator of ferroptotic cancer cell death
Sun, X., Ou, Z., Xie, M., Kang, R., Fan, Y., Niu, X., Wang, H., Cao, L., & Tang, D. (2015) · Oncogene · doi:10.1038/onc.2015.32 · Cited by 666 · see citing works
Interactions of iron, dopamine and neuromelanin pathways in brain aging and Parkinson's disease
Zucca, F. A., Segura-Aguilar, J., Ferrari, E., Muñoz, P., Paris, I., Sulzer, D., Sarna, T., Casella, L., & Zecca, L. (2017) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2015.09.012 · Cited by 659 · see citing works
Mechanisms of mammalian iron homeostasis
Pantopoulos, K., Porwal, S. K., Tartakoff, A., & Devireddy, L. (2012) · Biochemistry · doi:10.1021/bi300752r · Cited by 598 · see citing works
Iron and diabetes risk
Simcox, J. A., & McClain, D. A. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.02.007 · Cited by 545 · see citing works
Regulation of iron transport and the role of transferrin
Gkouvatsos, K., Papanikolaou, G., & Pantopoulos, K. (2012) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2011.10.013 · Cited by 518 · see citing works
Iron metabolism in the CNS: implications for neurodegenerative diseases
Rouault, T. A. (2013) · Nature Reviews Neuroscience · doi:10.1038/nrn3453 · Cited by 496 · see citing works
On-demand erythrocyte disposal and iron recycling requires transient macrophages in the liver
Theurl, I., Hilgendorf, I., Nairz, M., Tymoszuk, P., Haschka, D., Asshoff, M., He, S., Gerhardt, L. M. S., Holderried, T. A. W., Seifert, M., et al. (2016) · Nature Medicine · doi:10.1038/nm.4146 · Cited by 412 · see citing works
Targeting cancer vulnerabilities with high-dose vitamin C
Ngo, B., Van Riper, J. M., Cantley, L. C., & Yun, J. (2019) · Nature Reviews Cancer · doi:10.1038/s41568-019-0135-7 · Cited by 423 · see citing works
Hepcidin in the diagnosis of iron disorders
Girelli, D., Nemeth, E., & Swinkels, D. W. (2016) · Blood · doi:10.1182/blood-2015-12-639112 · Cited by 417 · see citing works
The complex interplay of iron metabolism, reactive oxygen species, and reactive nitrogen species: insights into the potential of various iron therapies to induce oxidative and nitrosative stress
Koskenkorva-Frank, T. S., Weiss, G., Koppenol, W. H., & Burckhardt, S. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.09.001 · Cited by 406 · see citing works
Iron deficiency and heart failure: diagnostic dilemmas and therapeutic perspectives
Jankowska, E. A., von Haehling, S., Anker, S. D., Macdougall, I. C., & Ponikowski, P. (2013) · European Heart Journal · doi:10.1093/eurheartj/ehs224 · Cited by 399 · see citing works
Cellular iron uptake, trafficking and metabolism: Key molecules and mechanisms and their roles in disease
Lane, D. J. R., Merlot, A. M., Huang, M. L.-H., Bae, D.-H., Jansson, P. J., Sahni, S., Kalinowski, D. S., & Richardson, D. R. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2015.01.021 · Cited by 399 · see citing works
Nutrient acquisition strategies of mammalian cells
Palm, W., & Thompson, C. B. (2017) · Nature · doi:10.1038/nature22379 · Cited by 388 · see citing works
Hepatic acute phase proteins – Regulation by IL-6- and IL-1-type cytokines involving STAT3 and its crosstalk with NF-κB-dependent signaling
Bode, J. G., Albrecht, U., Häussinger, D., Heinrich, P. C., & Schaper, F. (2012) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2011.09.008 · Cited by 379 · see citing works
An essential role for functional lysosomes in ferroptosis of cancer cells
Torii, S., Shintoku, R., Kubota, C., Yaegashi, M., Torii, R., Sasaki, M., Suzuki, T., Mori, M., Yoshimoto, Y., Takeuchi, T., et al. (2016) · Biochemical Journal · doi:10.1042/bj20150658 · Cited by 349 · see citing works
Iron at the interface of immunity and infection
Nairz, M., Haschka, D., Demetz, E., & Weiss, G. (2014) · Frontiers in Pharmacology · doi:10.3389/fphar.2014.00152 · Cited by 325 · see citing works
“Under physiological conditions iron recycling by macrophages accounts for approximately 95% of the daily needs of the metal for erythropoiesis and other physiological processes (Hentze et al., 2010; Pantopoulos et al., 2012).”
Background
Obesity as an emerging risk factor for iron deficiency
Aigner, E., Feldman, A., & Datz, C. (2014) · Nutrients · doi:10.3390/nu6093587 · Cited by 328 · see citing works
Gut Microbiota and Iron: The Crucial Actors in Health and Disease
Yilmaz, B., & Li, H. (2018) · Pharmaceuticals · doi:10.3390/ph11040098 · Cited by 317 · see citing works
Shared and distinct mechanisms of iron acquisition by bacterial and fungal pathogens of humans
Caza, M., & Kronstad, J. W. (2013) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2013.00080 · Cited by 306 · see citing works
Serum hepcidin: reference ranges and biochemical correlates in the general population
Galesloot, T. E., Vermeulen, S. H., Geurts-Moespot, A. J., Klaver, S. M., Kroot, J. J., van Tienoven, D., Wetzels, J. F. M., Kiemeney, L. A. L. M., Sweep, F. C., den Heijer, M., et al. (2011) · Blood · doi:10.1182/blood-2011-02-337907 · Cited by 303 · see citing works
Iron as a central player and promising target in cancer progression
Jung, M., Mertens, C., Tomat, E., & Brüne, B. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20020273 · Cited by 268 · see citing works
“When intracellular iron is low, IRPs interact with conserved iron-responsive elements (IREs) in the untranslated regions (UTRs) of central genes accounting for iron homeostasis [32,33].”
Background
Hemopexin therapy reverts heme-induced proinflammatory phenotypic switching of macrophages in a mouse model of sickle cell disease
Vinchi, F., Costa da Silva, M., Ingoglia, G., Petrillo, S., Brinkman, N., Zuercher, A., Cerwenka, A., Tolosano, E., & Muckenthaler, M. U. (2016) · Blood · doi:10.1182/blood-2015-08-663245 · Cited by 269 · see citing works
Self-citation
Distinct mechanisms of ferritin delivery to lysosomes in iron-depleted and iron-replete cells
Asano, T., Komatsu, M., Yamaguchi-Iwai, Y., Ishikawa, F., Mizushima, N., & Iwai, K. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.01437-10 · Cited by 265 · see citing works
NCOA4 deficiency impairs systemic iron homeostasis
Bellelli, R., Federico, G., Matte’, A., Colecchia, D., Iolascon, A., Chiariello, M., Santoro, M., De Franceschi, L., & Carlomagno, F. (2016) · Cell Reports · doi:10.1016/j.celrep.2015.12.065 · Cited by 248 · see citing works
Hepcidin in Human Iron Disorders: Diagnostic Implications
Kroot, J. J., Tjalsma, H., Fleming, R. E., & Swinkels, D. W. (2011) · Clinical Chemistry · doi:10.1373/clinchem.2009.140053 · Cited by 246 · see citing works
The Iron age of host–microbe interactions
Soares, M. P., & Weiss, G. (2015) · The EMBO Reports · doi:10.15252/embr.201540558 · Cited by 227 · see citing works
Macrophages support pathological erythropoiesis in polycythemia vera and β-thalassemia
Ramos, P., Casu, C., Gardenghi, S., Breda, L., Crielaard, B. J., Guy, E., Marongiu, M. F., Gupta, R., Levine, R. L., Abdel-Wahab, O., et al. (2013) · Nature Medicine · doi:10.1038/nm.3126 · Cited by 227 · see citing works
17β-Estradiol Inhibits Iron Hormone Hepcidin Through an Estrogen Responsive Element Half-Site
Yang, Q., Jian, J., Katz, S., Abramson, S. B., & Huang, X. (2012) · Endocrinology · doi:10.1210/en.2011-2045 · Cited by 208 · see citing works
The hemochromatosis proteins HFE, TfR2, and HJV form a membrane-associated protein complex for hepcidin regulation
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Authors: Hentze, M. W., Muckenthaler, M. U., Galy, B., & Camaschella, C.
Affiliations: Heidelberg University (DE)
European Molecular Biology Laboratory (DE)
Vita-Salute San Raffaele University (IT)
Corresponding author: Hentze, Matthias W.
ORCID: Hentze, Matthias W.
Muckenthaler, Martina U.
Galy, Bruno
Camaschella, Clara
Venue: Cell
Publisher: Elsevier BV
Published: 2010-07
Volume: 142
Issue: 1
Pages: 24-38
ISSN: 0092-8674 (ISSN-L)
DOI: 10.1016/j.cell.2010.06.028
OpenAlex: W2107704801
Cited by: 2,120
References: 111
Citations by year: 2026: 98 · 2025: 117 · 2024: 161 · 2023: 169 · 2022: 156 · 2021: 162 · 2020: 159 · 2019: 159 · 2018: 129 · 2017: 125 · 2016: 106 · 2015: 118 · 2014: 133 · 2013: 113 · 2012: 113
FWCI: 16.63
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 1112 d)
Locations: Cell (publishedVersion)
PubMed (publishedVersion)
INFM-OAR (INFN Catania) (submittedVersion, cc-by)
Funders: European Commission
Deutsche Forschungsgemeinschaft
Topics: Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
Health Sciences › Medicine › Pulmonary and Respiratory Medicine › Ferroptosis and cancer prognosis
Life Sciences › Neuroscience › Neurology › Neurological diseases and metabolism
Keywords: iron metabolism, iron homeostasis, hepcidin, ferroportin, iron regulatory proteins, iron-responsive element, iron deficiency, iron overload, therapeutic target
MeSH terms: Animals, Cell Physiological Phenomena, Humans, Iron, Anemia, Iron-Deficiency, Iron Overload, Antimicrobial Cationic Peptides, Hepcidins

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Two to tango: Regulation of Mammalian iron metabolism

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