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Two to Tango: Regulation of Mammalian Iron Metabolism
Open accessAbstract
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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“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]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“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
In the citing paper
“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]
In the citing paper
“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]
In the citing paper
“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]
In the citing paper
“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]
In the citing paper
“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
In the citing paper
“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]
In the citing paper
“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]
In the citing paper
“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]
In the citing paper
“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]
In the citing paper
“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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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
Cloning and characterization of a mammalian proton-coupled metal-ion transporter
Gunshin, H., Mackenzie, B., Berger, U. V., Gunshin, Y., Romero, M. F., Boron, W. F., Nussberger, S., Gollan, J. L., & Hediger, M. A. (1997) · Nature · doi:10.1038/41343 · Cited by 3,166
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
Self-citationThe iron exporter ferroportin/Slc40a1 is essential for iron homeostasis
Donovan, A., Lima, C. A., Pinkus, J. L., Pinkus, G. S., Zon, L. I., Robine, S., & Andrews, N. C. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.01.003 · Cited by 1,275
pH and the recycling of transferrin during receptor-mediated endocytosis.
Dautry‐Varsat, A., Ciechanover, A. J., & Lodish, H. F. (1983) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.80.8.2258 · Cited by 1,178
Dorsomorphin inhibits BMP signals required for embryogenesis and iron metabolism
Yu, P. B., Hong, C. C., Sachidanandan, C., Babitt, J. L., Deng, D. Y., Hoyng, S. A., Lin, H. Y.-F., Bloch, K. D., & Peterson, R. T. (2007) · Nature Chemical Biology · doi:10.1038/nchembio.2007.54 · Cited by 1,059
Bone morphogenetic protein signaling by hemojuvelin regulates hepcidin expression
Babitt, J. L., Huang, F. W., Wrighting, D. M., Xia, Y., Sidis, Y., Samad, T. A., Campagna, J. A., Chung, R. T., Schneyer, A. L., Woolf, C. J., et al. (2006) · Nature Genetics · doi:10.1038/ng1777 · Cited by 1,026
High levels of GDF15 in thalassemia suppress expression of the iron regulatory protein hepcidin
Tanno, T., Bhanu, N. V., Oneal, P. A., Goh, S.-H., Staker, P., Lee, Y. T., Moroney, J. W., Reed, C. H., Luban, N. L., Wang, R.-H., et al. (2007) · Nature Medicine · doi:10.1038/nm1629 · Cited by 854
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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
Self-citationThe 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
Camaschella, C. (2015) · New England Journal of Medicine · doi:10.1056/nejmra1401038 · Cited by 1,678
Self-citationFueling 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
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
Ganz, T. (2013) · Physiological Reviews · doi:10.1152/physrev.00008.2013 · Cited by 1,122
Regulation of cellular iron metabolism
Wang, J., & Pantopoulos, K. (2011) · Biochemical Journal · doi:10.1042/bj20101825 · Cited by 986
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
“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…”
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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
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
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
Mechanisms of mammalian iron homeostasis
Pantopoulos, K., Porwal, S. K., Tartakoff, A., & Devireddy, L. (2012) · Biochemistry · doi:10.1021/bi300752r · Cited by 598
Simcox, J. A., & McClain, D. A. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.02.007 · Cited by 545
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
Iron metabolism in the CNS: implications for neurodegenerative diseases
Rouault, T. A. (2013) · Nature Reviews Neuroscience · doi:10.1038/nrn3453 · Cited by 496
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
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
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
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
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
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
Nutrient acquisition strategies of mammalian cells
Palm, W., & Thompson, C. B. (2017) · Nature · doi:10.1038/nature22379 · Cited by 388
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
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
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
“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).”
BackgroundObesity as an emerging risk factor for iron deficiency
Aigner, E., Feldman, A., & Datz, C. (2014) · Nutrients · doi:10.3390/nu6093587 · Cited by 328
Gut Microbiota and Iron: The Crucial Actors in Health and Disease
Yilmaz, B., & Li, H. (2018) · Pharmaceuticals · doi:10.3390/ph11040098 · Cited by 317
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
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
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
“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].”
BackgroundVinchi, 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
Self-citationDistinct 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
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
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
The Iron age of host–microbe interactions
Soares, M. P., & Weiss, G. (2015) · The EMBO Reports · doi:10.15252/embr.201540558 · Cited by 227
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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
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
D’Alessio, F., Hentze, M. W., & Muckenthaler, M. U. (2012) · Journal of Hepatology · doi:10.1016/j.jhep.2012.06.015 · Cited by 200
Terzi, E. M., Sviderskiy, V. O., Alvarez, S. W., Whiten, G. C., & Possemato, R. (2021) · Science Advances · doi:10.1126/sciadv.abg4302 · Cited by 195
Iron deficiency: new insights into diagnosis and treatment
Camaschella, C. (2015) · Hematology · doi:10.1182/asheducation-2015.1.8 · Cited by 201
Self-citationmTOR regulates cellular iron homeostasis through tristetraprolin
Bayeva, M., Khechaduri, A., Puig, S., Chang, H.-C., Patial, S., Blackshear, P. J., & Ardehali, H. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.10.001 · Cited by 197
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Korolnek, T., & Hamza, I. (2015) · Blood · doi:10.1182/blood-2014-12-567776 · Cited by 196
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Cherayil, B. J. (2011) · Immunologic Research · doi:10.1007/s12026-010-8199-1 · Cited by 191
Miao, R., Fang, X., Zhang, Y., Wei, J., Zhang, Y., & Tian, J. (2023) · Cell Death & Disease · doi:10.1038/s41419-023-05708-0 · Cited by 192
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Theurl, I., Schroll, A., Sonnweber, T., Nairz, M., Theurl, M., Willenbacher, W., Eller, K., Wolf, D., Seifert, M., Sun, C. C., et al. (2011) · Blood · doi:10.1182/blood-2011-03-345066 · Cited by 189
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Nairz, M., Theurl, I., Swirski, F. K., & Weiss, G. (2017) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-017-1944-8 · Cited by 178
Rusu, I. G., Suharoschi, R., Vodnar, D. C., Pop, C. R., Socaci, S. A., Vulturar, R., Istrati, M., Moroșan, I., Fărcaș, A. C., Kerezsi, A. D., et al. (2020) · Nutrients · doi:10.3390/nu12071993 · Cited by 185
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Camaschella, C., & Nai, A. (2016) · British Journal of Haematology · doi:10.1111/bjh.13820 · Cited by 172
Self-citationThe pleiotropic effects of erythropoietin in infection and inflammation
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Nairz, M., Theurl, I., Wolf, D., & Weiss, G. (2016) · Wiener Medizinische Wochenschrift · doi:10.1007/s10354-016-0505-7 · Cited by 152
Deletion of TMPRSS6 attenuates the phenotype in a mouse model of β-thalassemia
Nai, A., Pagani, A., Mandelli, G., Lidonnici, M. R., Silvestri, L., Ferrari, G., & Camaschella, C. (2012) · Blood · doi:10.1182/blood-2012-01-401885 · Cited by 161
Self-citationCoupling Heme and Iron Metabolism via Ferritin H Chain
Gozzelino, R., & Soares, M. P. (2014) · Antioxidants & Redox Signaling · doi:10.1089/ars.2013.5666 · Cited by 151
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Guo, Q., Li, L., Hou, S., Yuan, Z., Li, C., Zhang, W., Zheng, L., & Li, X. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.778492 · Cited by 150
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Sonnweber, T., Nachbaur, D., Schroll, A., Nairz, M., Seifert, M., Demetz, E., Haschka, D., Mitterstiller, A.-M., Kleinsasser, A., Burtscher, M., et al. (2014) · Gut · doi:10.1136/gutjnl-2013-305317 · Cited by 145
Self-citationAnaemia in inflammatory rheumatic diseases
Weiss, G., & Schett, G. (2013) · Nature Reviews Rheumatology · doi:10.1038/nrrheum.2012.183 · Cited by 146
Iron levels in polarized macrophages: regulation of immunity and autoimmunity
Recalcati, S., Locati, M., Gammella, E., Invernizzi, P., & Cairo, G. (2012) · Autoimmunity Reviews · doi:10.1016/j.autrev.2012.03.003 · Cited by 150
Jiang, L., Wang, J., Wang, K., Wang, H., Wu, Q., Yang, C., Yu, Y., Ni, P., Zhong, Y., Song, Z., et al. (2021) · Blood · doi:10.1182/blood.2020008986 · Cited by 138
Low hepcidin accounts for the proinflammatory status associated with iron deficiency
Pagani, A., Nai, A., Corna, G., Bosurgi, L., Rovere-Querini, P., Camaschella, C., & Silvestri, L. (2011) · Blood · doi:10.1182/blood-2011-02-337212 · Cited by 138
Self-citationCuadrado, E., van den Biggelaar, M., de Kivit, S., Chen, Y.-Y., Slot, M., Doubal, I., Meijer, A., van Lier, R. A. W., Borst, J., & Amsen, D. (2018) · Immunity · doi:10.1016/j.immuni.2018.04.008 · Cited by 132
Taniguchi, R., Kato, H. E., Font, J., Deshpande, C. N., Wada, M., Ito, K., Ishitani, R., Jormakka, M., & Nureki, O. (2015) · Nature Communications · doi:10.1038/ncomms9545 · Cited by 120
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Poli, M., Asperti, M., Ruzzenenti, P., Regoni, M., & Arosio, P. (2014) · Frontiers in Pharmacology · doi:10.3389/fphar.2014.00086 · Cited by 124
Altamura, S., Kessler, R., Gröne, H.-J., Gretz, N., Hentze, M. W., Galy, B., & Muckenthaler, M. U. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.07.007 · Cited by 119
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Correnti, C., & Strong, R. K. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.r111.311829 · Cited by 115
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Weiss, G. (2015) · Seminars in Hematology · doi:10.1053/j.seminhematol.2015.07.004 · Cited by 116
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Mastrogiannaki, M., Matak, P., & Peyssonnaux, C. (2013) · Blood · doi:10.1182/blood-2012-11-427765 · Cited by 116
Leal, S. M., Roy, S., Vareechon, C., Carrion, S. D., Clark, H., Lopez-Berges, M. S., diPietro, A., Schrettl, M., Beckmann, N., Redl, B., et al. (2013) · PLoS Pathogens · doi:10.1371/journal.ppat.1003436 · Cited by 111
Siegert, I., Schödel, J., Nairz, M., Schatz, V., Dettmer, K., Dick, C., Kalucka, J., Franke, K., Ehrenschwender, M., Schley, G., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.11.005 · Cited by 110
“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).”
BackgroundSelf-citationIron regulatory proteins control a mucosal block to intestinal iron absorption
Galy, B., Ferring-Appel, D., Becker, C., Gretz, N., Gröne, H.-J., Schümann, K., & Hentze, M. W. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.02.026 · Cited by 98
Self-citationGill, D., Del Greco M., F., Walker, A. P., Srai, S. K. S., Laffan, M. A., & Minelli, C. (2017) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.117.309757 · Cited by 95
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Mühlenhoff, U., Hoffmann, B., Richter, N., Rietzschel, N., Spantgar, F., Stehling, O., Uzarska, M. A., & Lill, R. (2015) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2015.05.003 · Cited by 95
Nevitt, T., & Thiele, D. J. (2011) · PLoS Pathogens · doi:10.1371/journal.ppat.1001322 · Cited by 95
“and, as a consequence, organisms have evolved sophisticated homeostatic mechanisms to tightly regulate the acquisition, utilization, storage and mobilization of Fe”
BackgroundLipopolysaccharides Upregulate Hepcidin in Neuron via Microglia and the IL-6/STAT3 Signaling Pathway
Qian, Z.-M., He, X., Liang, T., Wu, K.-C., Yan, Y.-C., Lu, L.-N., Yang, G., Luo, Q. Q., Yung, W.-H., & Ke, Y. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-8671-3 · Cited by 89
‘Ride on the ferrous wheel’ – The cycle of iron in macrophages in health and disease
Nairz, M., Schroll, A., Demetz, E., Tancevski, I., Theurl, I., & Weiss, G. (2015) · Immunobiology · doi:10.1016/j.imbio.2014.09.010 · Cited by 89
The role of iron in tumour cell proliferation
Steegmann-Olmedillas, J. L. (2011) · Clinical and Translational Oncology · doi:10.1007/s12094-011-0621-1 · Cited by 84
Diagnosis of iron-deficient states
Archer, N. M., & Brugnara, C. (2015) · Critical Reviews in Clinical Laboratory Sciences · doi:10.3109/10408363.2015.1038744 · Cited by 82
Dopamine promotes cellular iron accumulation and oxidative stress responses in macrophages
Dichtl, S., Haschka, D., Nairz, M., Seifert, M., Volani, C., Lutz, O., & Weiss, G. (2018) · Biochemical Pharmacology · doi:10.1016/j.bcp.2017.12.001 · Cited by 76
The European Hematology Association Roadmap for European Hematology Research: a consensus document
Engert, A., Balduini, C., Brand, A., Coiffier, B., Cordonnier, C., Dohner, H., de Wit, T. D., Eichinger, S., Fibbe, W., Green, T., et al. (2016) · Haematologica · doi:10.3324/haematol.2015.136739 · Cited by 81
“European research contributions European researchers have contributed identifying hepcidin, the key liver hormone regulating systemic iron homeostasis, defining its role in genetic iron-related disorders and clarifying how high hepcidin induces iron sequestration and iron-deficient erythropoiesis in ACD.(160) Our adva…”
BackgroundFluorescent probes for the detection of catalytic Fe(II) ion
Hirayama, T. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.07.004 · Cited by 79
Ueta, R., Fujiwara, N., Iwai, K., & Yamaguchi-Iwai, Y. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.00726-12 · Cited by 78
Hickok, J. R., Sahni, S., Mikhed, Y., Bonini, M. G., & Thomas, D. D. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.287052 · Cited by 80
Mleczko-Sanecka, K., Roche, F., Rita da Silva, A., Call, D., D’Alessio, F., Ragab, A., Lapinski, P. E., Ummanni, R., Korf, U., Oakes, C., et al. (2014) · Blood · doi:10.1182/blood-2013-07-515957 · Cited by 74
Self-citationThompson, J. W., Salahudeen, A. A., Chollangi, S., Ruiz, J. C., Brautigam, C. A., Makris, T. M., Lipscomb, J. D., Tomchick, D. R., & Bruick, R. K. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.308684 · Cited by 71
Enns, C. A., Ahmed, R., Wang, J., Ueno, A., Worthen, C., Tsukamoto, H., & Zhang, A.-S. (2013) · PLoS ONE · doi:10.1371/journal.pone.0060534 · Cited by 69
The Repair of Skeletal Muscle Requires Iron Recycling through Macrophage Ferroportin
Corna, G., Caserta, I., Monno, A., Apostoli, P., Manfredi, A. A., Camaschella, C., & Rovere-Querini, P. (2016) · The Journal of Immunology · doi:10.4049/jimmunol.1501417 · Cited by 63
Self-citationMitterstiller, A.-M., Haschka, D., Dichtl, S., Nairz, M., Demetz, E., Talasz, H., Soares, M. P., Einwallner, E., Esterbauer, H., Fang, F. C., et al. (2016) · Cellular Microbiology · doi:10.1111/cmi.12578 · Cited by 62
Calcium is an essential cofactor for metal efflux by the ferroportin transporter family
Deshpande, C. N., Ruwe, T. A., Shawki, A., Xin, V., Vieth, K. R., Valore, E. V., Qiao, B., Ganz, T., Nemeth, E., Mackenzie, B., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-05446-4 · Cited by 57
Dietary iron loading negatively affects liver mitochondrial function
Volani, C., Doerrier, C., Demetz, E., Haschka, D., Paglia, G., Lavdas, A. A., Gnaiger, E., & Weiss, G. (2017) · Metallomics · doi:10.1039/c7mt00177k · Cited by 59
Erythropoietin's inhibiting impact on hepcidin expression occurs indirectly
Gammella, E., Diaz, V., Recalcati, S., Buratti, P., Samaja, M., Dey, S., Noguchi, C. T., Gassmann, M., & Cairo, G. (2015) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00410.2014 · Cited by 59
Inherited disorders of iron metabolism
Camaschella, C., & Poggiali, E. (2011) · Current Opinion in Pediatrics · doi:10.1097/mop.0b013e3283425591 · Cited by 59
Self-citationSerum Hepcidin in Inflammatory Bowel Diseases: Biological and Clinical Significance
Bergamaschi, G., Di Sabatino, A., Albertini, R., Costanzo, F., Guerci, M., Masotti, M., Pasini, A., Massari, A., Campostrini, N., Corbella, M., et al. (2013) · Inflammatory Bowel Diseases · doi:10.1097/mib.0b013e31829a6e43 · Cited by 56
Chuvash polycythemia VHLR200W mutation is associated with down-regulation of hepcidin expression
Gordeuk, V. R., Miasnikova, G. Y., Sergueeva, A. I., Niu, X., Nouraie, M., Okhotin, D. J., Polyakova, L. A., Ammosova, T., Nekhai, S., Ganz, T., et al. (2011) · Blood · doi:10.1182/blood-2011-03-345512 · Cited by 51
(2012) · Current Topics in Membranes · doi:10.1016/b978-0-12-394390-3.00010-0 · Cited by 47
Dichtl, S., Demetz, E., Haschka, D., Tymoszuk, P., Petzer, V., Nairz, M., Seifert, M., Hoffmann, A., Brigo, N., Würzner, R., et al. (2019) · mBio · doi:10.1128/mbio.02624-18 · Cited by 50
Cozzi, A., Santambrogio, P., Privitera, D., Broccoli, V., Rotundo, L. I., Garavaglia, B., Benz, R., Altamura, S., Goede, J. S., Muckenthaler, M. U., et al. (2013) · Journal of Experimental Medicine · doi:10.1084/jem.20130315 · Cited by 47
Self-citationJonker, F. A. M., Calis, J. C. J., Phiri, K., Kraaijenhagen, R. J., Brabin, B. J., Faragher, B., Wiegerinck, E. T., Tjalsma, H., Swinkels, D. W., & Boele van Hensbroek, M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0078964 · Cited by 42
Cheng, X., Zhao, F., Ke, B., Chen, D., & Liu, F. (2023) · Cancers · doi:10.3390/cancers15215209 · Cited by 44
Bellmann-Weiler, R., Schroll, A., Engl, S., Nairz, M., Talasz, H., Seifert, M., & Weiss, G. (2013) · Immunobiology · doi:10.1016/j.imbio.2012.11.004 · Cited by 43
Theurl, M., Nairz, M., Schroll, A., Sonnweber, T., Asshoff, M., Haschka, D., Seifert, M., Willenbacher, W., Wilflingseder, D., Posch, W., et al. (2014) · Haematologica · doi:10.3324/haematol.2013.099481 · Cited by 42
Iron regulatory protein-1 protects against mitoferrin-1-deficient porphyria
Chung, J., Anderson, S. A., Gwynn, B., Deck, K. M., Chen, M. J., Langer, N. B., Shaw, G. C., Huston, N. C., Boyer, L. F., Datta, S., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.547778 · Cited by 39
Self-citation
Metadata
- 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.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2010-07
- Volume
- 142
- Issue
- 1
- Pages
- 24-38
- ISSN
- 0092-8674 (ISSN-L)
- 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
- 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
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › 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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