Mechanisms of mammalian iron homeostasis

Pantopoulos, Kostas; Porwal, Suheel Kumar; Tartakoff, Alan; Devireddy, L.

doi:10.1021/bi300752r

Cited by 598Iron Metabolism and DisordersNeurological diseases and metabolismTrace Elements in Health

Mechanisms of mammalian iron homeostasis

Open access

Pantopoulos, Kostas, Porwal, Suheel Kumar, Tartakoff, Alan, Devireddy, L.·2012·Biochemistry

DOI 10.1021/bi300752rPMC PMC3572738

Open this paper in CoChat — free account

Abstract

Iron is vital for almost all organisms because of its ability to donate and accept electrons with relative ease. It serves as a cofactor for many proteins and enzymes necessary for oxygen and energy metabolism, as well as for several other essential processes. Mammalian cells utilize multiple mechanisms to acquire iron. Disruption of iron homeostasis is associated with various human diseases: iron deficiency resulting from defects in the acquisition or distribution of the metal causes anemia, whereas iron surfeit resulting from excessive iron absorption or defective utilization causes abnormal tissue iron deposition, leading to oxidative damage. Mammals utilize distinct mechanisms to regulate iron homeostasis at the systemic and cellular levels. These involve the hormone hepcidin and iron regulatory proteins, which collectively ensure iron balance. This review outlines recent advances in iron regulatory pathways as well as in mechanisms underlying intracellular iron trafficking, an important but less studied area of mammalian iron homeostasis.

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

Crossref · 10.1021/bi300752r

Cites

221 of 221 references verified0 citation errors · 0 not checkable

Statistics

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?

Hepcidin is a liver-derived hormone that regulates introduction of iron into plasma from three major sources: iron stored within hepatocytes, absorbed iron in the duodenal enterocytes, and iron recycled from macrophages.
“Hepcidin is a liver-derived hormone that regulates introduction of iron into plasma from three major sources: iron stored within hepatocytes, absorbed iron in the duodenal enterocytes and iron recycled from macrophages (Ganz and Nemeth, 2012; Pantopoulos et al., 2012).”
From Iron at the Centre of Candida albicans Interactions (2018) · cites this paper as Pantopoulos et al., 2012
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 Pantopoulos et al., 2012
Autophagy plays a critical role in maintaining iron homeostasis in PDAC cells.
“autophagy plays a critical role in maintaining iron homeostasis in PDAC cells214”
From Pancreatic cancer: Advances and challenges (2023) · cites this paper as [214]
Ferritin is trafficked to autophagosomes via NCOA4, and free iron is subsequently released by autophagy through ferritinophagy.
“ferritin is trafficked to autophagosomes via nuclear receptor coactivator 4 (NCOA4), and free iron is subsequently released by autophagy through a process termed “ferritinophagy”214”
From Pancreatic cancer: Advances and challenges (2023) · cites this paper as [214]
IFN-γ stimulates NO formation, which activates IRP-1 binding to the ferritin IRE, leading to inhibition of ferritin translation.
“IFN-γ stimulates NO formation, which then activates IRP-1 binding to the ferritin IRE, leading to inhibition of ferritin translation, whereas IRP-2 activity is affected depending on the type of cell and NO product (178).”
From Macrophage defense mechanisms against intracellular bacteria (2015) · cites this paper as [178]

IRP-2 activity is affected by NO depending on the cell type and the NO product.
“IFN-γ stimulates NO formation, which then activates IRP-1 binding to the ferritin IRE, leading to inhibition of ferritin translation, whereas IRP-2 activity is affected depending on the type of cell and NO product (178).”
From Macrophage defense mechanisms against intracellular bacteria (2015) · cites this paper as [178]
IFN-γ induces transcription of ferritin and also affects its translation by modulating iron regulatory protein (IRP) binding affinity.
“The Th1-derived cytokine IFN-γ induces the transcription but also affects the translation of the major iron storage protein ferritin, the latter being due to modulation of iron regulatory protein (IRP) binding affinity by the cytokine.”
From Macrophage defense mechanisms against intracellular bacteria (2015) · cites this paper as [178]
Hydrogen peroxide and superoxide anion modulate IRP-1 activity via kinase/phosphatase signal transduction pathways, resulting in divergent posttranscriptional regulation of IRE-regulated target genes such as TfR and ferritin.
“Moreover, hydrogen peroxide and superoxide anion modulate IRP-1 activity by a rapidly inducible process involving kinase/phosphatase signal transduction pathways resulting in divergent posttranscriptional regulation of IRE-regulated target genes such as transferrin receptor (TfR) and ferritin (178, 179).”
From Macrophage defense mechanisms against intracellular bacteria (2015) · cites this paper as [178]
Copper homeostasis is closely linked to iron metabolism.
“Copper homeostasis is closely linked to iron metabolism.”
From Macrophage defense mechanisms against intracellular bacteria (2015) · cites this paper as [178]
The ferroxidases hephaestin and ceruloplasmin, which mediate oxidation of ferrous to ferric iron and its incorporation into transferrin, are copper-containing enzymes.
“The ferroxidases hephaestin and ceruloplasmin, which mediate the oxidation of ferrous to ferric iron and thus its incorporation into transferrin, are copper-containing enzymes (178).”
From Macrophage defense mechanisms against intracellular bacteria (2015) · cites this paper as [178]
IFNγ induces iNOS/NOS2 expression via STAT transcription factors, and NO produced by iNOS/NOS2 regulates IRP binding affinities toward IRE in TfR and ferritin, inhibiting cellular iron import and intracellular retention.
“IFNc also induces the expression of iNOS/NOS2 [78], via a mechanism regulated at a transcriptional level by the activation of the signal transducers and activators of transcription (STAT) family of transcription factors (Fig 2).As described above, the NO produced by iNOS/NOS2 regulates the binding affinities of IRP toward target IRE in genes such as transferrin receptor (TfR) and ferritin, inhibit”
From The Iron age of host–microbe interactions (2015) · cites this paper as [58]
A shortage of iron represents a common challenge in most host niches of C. glabrata.
“A shortage of iron represents a common challenge in most host niches of C. glabrata (41, 42)”
From A novel hybrid iron regulation network combines features from pathogenic and nonpathogenic yeasts (2016) · cites this paper as [42]

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

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 · see citing works
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 · see citing works
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 · see citing works
Heme Oxygenase-1/Carbon Monoxide: From Basic Science to Therapeutic Applications
Ryter, S. W., Alam, J., & Choi, A. M. K. (2006) · Physiological Reviews · doi:10.1152/physrev.00011.2005 · Cited by 2,308 · see citing works
Hepcidin, a urinary antimicrobial peptide synthesized in the liver
Park, C. H., Valore, E. V., Waring, A. J., & Ganz, T. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008922200 · Cited by 2,168 · see citing works
Two to tango: Regulation of Mammalian iron metabolism
Hentze, M. W., Muckenthaler, M. U., Galy, B., & Camaschella, C. (2010) · Cell · doi:10.1016/j.cell.2010.06.028 · Cited by 2,120 · see citing works
Lipocalin 2 mediates an innate immune response to bacterial infection by sequestrating iron
Flo, T. H., Smith, K. D., Sato, S., Rodriguez, D. J., Holmes, M. A., Strong, R. K., Akira, S., & Aderem, A. (2004) · Nature · doi:10.1038/nature03104 · Cited by 1,877 · see citing works
Chemistry and biology of siderophores
Hider, R. C., & Kong, X. (2010) · Natural Product Reports · doi:10.1039/b906679a · Cited by 1,722 · see citing works
Siderophores: Structure and Function of Microbial Iron Transport Compounds
Neilands, J. B. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.45.26723 · Cited by 1,652 · see citing works
A Novel Duodenal Iron-Regulated Transporter, IREG1, Implicated in the Basolateral Transfer of Iron to the Circulation
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 · see citing works
The Neutrophil Lipocalin NGAL Is a Bacteriostatic Agent that Interferes with Siderophore-Mediated Iron Acquisition
Goetz, D. H., Holmes, M. A., Borregaard, N., Bluhm, M. E., Raymond, K. N., & Strong, R. K. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00708-6 · Cited by 1,355 · see citing works
LEAP-1, a novel highly disulfide-bonded human peptide, exhibits antimicrobial activity
Krause, A., Neitz, S., Mägert, H.-J., Schulz, A., Forssmann, W.-G., Schulz-Knappe, P., & Adermann, K. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)01920-7 · Cited by 1,324 · see citing works
The 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 · see citing works
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 · see citing works
Microcytic anaemia mice have a mutation in Nramp2, a candidate iron transporter gene
Fleming, M. D., Trenor, C. C., Su, M. A., Foernzler, D., Beier, D. R., Dietrich, W. F., & Andrews, N. C. (1997) · Nature Genetics · doi:10.1038/ng0897-383 · Cited by 1,159 · see citing works
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 1,039 · see citing works
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 · 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
Self-citation
Interleukin-6 induces hepcidin expression through STAT3
Wrighting, D. M., & Andrews, N. C. (2006) · Blood · doi:10.1182/blood-2006-06-027631 · Cited by 983 · see citing works
Mutations in HFE2 cause iron overload in chromosome 1q–linked juvenile hemochromatosis
Papanikolaou, G., Samuels, M. E., Ludwig, E. H., MacDonald, M. L. E., Franchini, P. L., Dubé, M.-P., Andres, L., MacFarlane, J., Sakellaropoulos, N., Politou, M., et al. (2004) · Nature Genetics · doi:10.1038/ng1274 · Cited by 974 · see citing works
Hepcidin and iron regulation, 10 years later
Ganz, T. (2011) · Blood · doi:10.1182/blood-2011-01-258467 · Cited by 962 · see citing works
Nramp 2 is mutated in the anemic Belgrade ( b ) rat: Evidence of a role for Nramp2 in endosomal iron transport
Fleming, M. D., Romano, M. A., Su, M. A., Garrick, L. M., Garrick, M. D., & Andrews, N. C. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.3.1148 · Cited by 936 · see citing works
Enterobactin: an archetype for microbial iron transport.
Raymond, K. N., Dertz, E. A., & Kim, S. S. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0630018100 · Cited by 933 · see citing works
Ferritins: A family of molecules for iron storage, antioxidation and more
Arosio, P., Ingrassia, R., & Cavadini, P. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2008.09.004 · Cited by 886 · see citing works
Mutant antimicrobial peptide hepcidin is associated with severe juvenile hemochromatosis
Roetto, A., Papanikolaou, G., Politou, M., Alberti, F., Girelli, D., Christakis, J., Loukopoulos, D., & Camaschella, C. (2003) · Nature Genetics · doi:10.1038/ng1053 · Cited by 860 · see citing works
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 · see citing works
Identification of an Intestinal Folate Transporter and the Molecular Basis for Hereditary Folate Malabsorption
Qiu, A., Jansen, M., Sakaris, A., Min, S. H., Chattopadhyay, S., Tsai, E., Sandoval, C., Zhao, R., Akabas, M. H., & Goldman, I. D. (2006) · Cell · doi:10.1016/j.cell.2006.09.041 · Cited by 847 · see citing works
The breast cancer resistance protein protects against a major chlorophyll-derived dietary phototoxin and protoporphyria
Jonker, J. W., Buitelaar, M., Wagenaar, E., van der Valk, M. A., Scheffer, G. L., Scheper, R. J., Plösch, T., Kuipers, F., Elferink, R. P. J. O., Rosing, H., et al. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.202607599 · Cited by 822 · see citing works
The gene TFR2 is mutated in a new type of haemochromatosis mapping to 7q22
Camaschella, C., Roetto, A., Calì, A., De Gobbi, M., Garozzo, G., Carella, M., Majorano, N., Totaro, A., & Gasparini, P. (2000) · Nature Genetics · doi:10.1038/75534 · Cited by 803 · see citing works
Genetics and Assembly Line Enzymology of Siderophore Biosynthesis in Bacteria
Crosa, J. H., & Walsh, C. T. (2002) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.66.2.223-249.2002 · Cited by 797 · see citing works
Identification of a ferrireductase required for efficient transferrin-dependent iron uptake in erythroid cells
Ohgami, R. S., Campagna, D. R., Greer, E. L., Antiochos, B., McDonald, A., Chen, J., Sharp, J. J., Fujiwara, Y., Barker, J. E., & Fleming, M. D. (2005) · Nature Genetics · doi:10.1038/ng1658 · Cited by 775 · see citing works
BMP6 is a key endogenous regulator of hepcidin expression and iron metabolism
Andriopoulos Jr, B., Corradini, E., Xia, Y., Faasse, S. A., Chen, S., Grgurevic, L., Knutson, M. D., Pietrangelo, A., Vukicevic, S., Lin, H. Y., et al. (2009) · Nature Genetics · doi:10.1038/ng.335 · Cited by 769 · see citing works
Identification of an Intestinal Heme Transporter
Shayeghi, M., Latunde-Dada, G. O., Oakhill, J. S., Laftah, A. H., Takeuchi, K., Halliday, N., Khan, Y., Warley, A., McCann, F. E., Hider, R. C., et al. (2005) · Cell · doi:10.1016/j.cell.2005.06.025 · Cited by 755 · see citing works
The Steap proteins are metalloreductases
Ohgami, R. S., Campagna, D. R., McDonald, A., & Fleming, M. D. (2006) · Blood · doi:10.1182/blood-2006-02-003681 · Cited by 744 · see citing works
The mitochondrial proteins Atm1p and Nfs1p are essential for biogenesis of cytosolic Fe/S proteins
Kispál, G., Csere, P., Prohl, C., & Lill, R. (1999) · The EMBO Journal · doi:10.1093/emboj/18.14.3981 · Cited by 699 · see citing works
Identification of a urate transporter, ABCG2, with a common functional polymorphism causing gout
Woodward, O. M., Köttgen, A., Coresh, J., Boerwinkle, E., Guggino, W. B., & Köttgen, M. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0901249106 · Cited by 684 · see citing works
Mutations in TMPRSS6 cause iron-refractory iron deficiency anemia (IRIDA)
Finberg, K. E., Heeney, M. M., Campagna, D. R., Aydınok, Y., Pearson, H. A., Hartman, K. R., Mayo, M. M., Samuel, S. M., Strouse, J. J., Markianos, K., et al. (2008) · Nature Genetics · doi:10.1038/ng.130 · Cited by 675 · see citing works
A Cell-Surface Receptor for Lipocalin 24p3 Selectively Mediates Apoptosis and Iron Uptake
Devireddy, L. R., Gazin, C., Zhu, X., & Green, M. R. (2005) · Cell · doi:10.1016/j.cell.2005.10.027 · Cited by 672 · see citing works
Self-citation
Non-transferrin bound iron: a key role in iron overload and iron toxicity
Brissot, P., Ropert, M., Le Lan, C., & Loréal, O. (2012) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2011.07.014 · Cited by 654 · see citing works
An Iron Delivery Pathway Mediated by a Lipocalin
Yang, J., Goetz, D., Li, J.-Y., Wang, W., Mori, K., Setlik, D., Du, T., Erdjument-Bromage, H., Tempst, P., Strong, R., et al. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00710-4 · Cited by 651 · see citing works
Molecular Cloning of Transferrin Receptor 2
Kawabata, H., Yang, R., Hirama, T., Vuong, P. T., Kawano, S., Gombart, A. F., & Koeffler, H. P. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.30.20826 · Cited by 646 · see citing works
Regulation of iron homeostasis by the hypoxia-inducible transcription factors (HIFs)
Peyssonnaux, C., Zinkernagel, A. S., Schuepbach, R. A., Rankin, E., Vaulont, S., Haase, V. H., Nizet, V., & Johnson, R. S. (2007) · Journal of Clinical Investigation · doi:10.1172/jci31370 · Cited by 639 · see citing works
Crystal structure of the hemochromatosis protein HFE and characterization of its interaction with transferrin receptor.
Lebrón, J., Bennett, M. J., Vaughn, D., Chirino, A., Snow, P., Mintier, G., Feder, J., & Bjorkman, P. (1998) · Cell · doi:10.1016/s0092-8674(00)81151-4 · Cited by 636 · see citing works
Mitoferrin is essential for erythroid iron assimilation
Shaw, G. C., Cope, J. J., Li, L., Corson, K., Hersey, C., Ackermann, G. E., Gwynn, B., Lambert, A. J., Wingert, R. A., Traver, D., et al. (2006) · Nature · doi:10.1038/nature04512 · Cited by 624 · see citing works
Disrupted hepcidin regulation in HFE-associated haemochromatosis and the liver as a regulator of body iron homoeostasis
Bridle, K. R., Frazer, D. M., Wilkins, S. J., Dixon, J. L., Purdie, D. M., Crawford, D. H., Subramaniam, V. N., Powell, L. W., Anderson, G. J., & Ramm, G. A. (2003) · The Lancet · doi:10.1016/s0140-6736(03)12602-5 · Cited by 620 · see citing works
Hereditary Hemochromatosis: Pathogenesis, Diagnosis, and Treatment
Pietrangelo, A. (2010) · Gastroenterology · doi:10.1053/j.gastro.2010.06.013 · Cited by 615 · see citing works
A role of SMAD4 in iron metabolism through the positive regulation of hepcidin expression
Wang, R.-H., Li, C., Xu, X., Zheng, Y., Xiao, C., Zerfas, P., Cooperman, S., Eckhaus, M., Rouault, T., Mishra, L., et al. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.10.010 · Cited by 614 · see citing works
Maturation of Iron-Sulfur Proteins in Eukaryotes: Mechanisms, Connected Processes, and Diseases
Lill, R., & Mühlenhoff, U. (2008) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.76.052705.162653 · Cited by 595 · see citing works
Lack of the bone morphogenetic protein BMP6 induces massive iron overload
Meynard, D., Kautz, L., Darnaud, V., Canonne-Hergaux, F., Coppin, H., & Roth, M.-P. (2009) · Nature Genetics · doi:10.1038/ng.320 · Cited by 587 · see citing works
Iron Homeostasis, Oxidative Stress, and DNA Damage
Meneghini, R. (1997) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(97)00016-6 · Cited by 578 · see citing works
The serine protease TMPRSS6 is required to sense iron deficiency
Du, X., She, E., Gelbart, T., Truksa, J., Lee, P., Xia, Y., Khovananth, K., Mudd, S., Mann, N., Moresco, E. M. Y., et al. (2008) · Science · doi:10.1126/science.1157121 · Cited by 578 · see citing works
Zip14 (Slc39a14) mediates non-transferrin-bound iron uptake into cells
Liuzzi, J. P., Aydemir, F., Nam, H., Knutson, M. D., & Cousins, R. J. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0606424103 · Cited by 577 · see citing works
Transferrin receptor is necessary for development of erythrocytes and the nervous system
Levy, J. E., Jin, O., Fujiwara, Y., Kuo, F., & Andrews, N. (1999) · Nature Genetics · doi:10.1038/7727 · Cited by 574 · see citing works
The type IV mucolipidosis-associated protein TRPML1 is an endolysosomal iron release channel
Dong, X., Cheng, X., Mills, E., Delling, M., Wang, F., Kurz, T., & Xu, H. (2008) · Nature · doi:10.1038/nature07311 · Cited by 572 · see citing works
STAT3 mediates hepatic hepcidin expression and its inflammatory stimulation
Verga Falzacappa, M. V., Vujic Spasic, M., Kessler, R., Stolte, J., Hentze, M. W., & Muckenthaler, M. U. (2007) · Blood · doi:10.1182/blood-2006-07-033969 · Cited by 567 · see citing works
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 · see citing works
The Serine Protease Matriptase-2 (TMPRSS6) Inhibits Hepcidin Activation by Cleaving Membrane Hemojuvelin
Silvestri, L., Pagani, A., Nai, A., De Domenico, I., Kaplan, J., & Camaschella, C. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.09.012 · Cited by 555 · see citing works
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 555 · see citing works
Mitochondrial iron trafficking and the integration of iron metabolism between the mitochondrion and cytosol
Richardson, D. R., Lane, D. J. R., Becker, E. M., Huang, M. L.-H., Whitnall, M., Rahmanto, Y. S., Sheftel, A. D., & Ponka, P. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0912925107 · Cited by 536 · see citing works
A cytosolic iron chaperone that delivers iron to ferritin
Shi, H., Bencze, K. Z., Stemmler, T. L., & Philpott, C. C. (2008) · Science · doi:10.1126/science.1157643 · Cited by 536 · see citing works
Labile iron pool: the main determinant of cellular response to oxidative stress
Kruszewski, M. K. (2003) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2003.08.004 · Cited by 529 · 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
Targeted deletion of the gene encoding iron regulatory protein-2 causes misregulation of iron metabolism and neurodegenerative disease in mice
LaVaute, T., Smith, S., Cooperman, S., Iwai, K., Land, W., Meyron-Holtz, E., Drake, S. K., Miller, G., Abu-Asab, M., Tsokos, M., et al. (2001) · Nature Genetics · doi:10.1038/84859 · Cited by 509 · see citing works
HIF-2α, but not HIF-1α, promotes iron absorption in mice
Mastrogiannaki, M., Matak, P., Keith, B., Simon, M. C., Vaulont, S., & Peyssonnaux, C. (2009) · Journal of Clinical Investigation · doi:10.1172/jci38499 · Cited by 502 · see citing works
Biosynthesis of heme in mammals
Ajioka, R. S., Phillips, J. D., & Kushner, J. P. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.05.005 · Cited by 493 · see citing works
L-type Ca2+ channels provide a major pathway for iron entry into cardiomyocytes in iron-overload cardiomyopathy
Oudit, G. Y., Sun, H., Trivieri, M. G., Koch, S. E., Dawood, F., Ackerley, C., Yazdanpanah, M., Wilson, G. J., Schwartz, A., Liu, P. P., et al. (2003) · Nature Medicine · doi:10.1038/nm920 · Cited by 480 · see citing works
Suppression of hepcidin during anemia requires erythropoietic activity
Pak, M., Lopez, M. A., Gabayan, V., Ganz, T., & Rivera, S. (2006) · Blood · doi:10.1182/blood-2006-06-028787 · Cited by 472 · see citing works
Hepcidin and disorders of iron metabolism
Ganz, T., & Nemeth, E. (2011) · Annual Review of Medicine · doi:10.1146/annurev-med-050109-142444 · Cited by 466 · see citing works
Regulation of iron acquisition and storage: consequences for iron-linked disorders
De Domenico, I., McVey Ward, D., & Kaplan, J. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2295 · Cited by 464 · see citing works
Lipocalin 2-deficient mice exhibit increased sensitivity to Escherichia coli infection but not to ischemia-reperfusion injury
Berger, T., Togawa, A., Duncan, G. S., Elia, A. J., You-Ten, A., Wakeham, A., Fong, H. E. H., Cheung, C. C., & Mak, T. W. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0510847103 · Cited by 460 · see citing works
Modulation of bone morphogenetic protein signaling in vivo regulates systemic iron balance
Babitt, J. L., Huang, F. W., Xia, Y. Y., Sidis, Y., Andrews, N. C., & Lin, H. Y.-F. (2007) · Journal of Clinical Investigation · doi:10.1172/jci31342 · Cited by 454 · see citing works
Hepcidin in iron overload disorders
Papanikolaou, G., Tzilianos, M., Christakis, J. I., Bogdanos, D., Tsimirika, K., MacFarlane, J., Goldberg, Y. P., Sakellaropoulos, N., Ganz, T., & Nemeth, E. (2005) · Blood · doi:10.1182/blood-2004-12-4844 · Cited by 445 · see citing works
The Molecular Mechanism of Hepcidin-mediated Ferroportin Down-Regulation
De Domenico, I., Ward, D. M., Langelier, C., Vaughn, M. B., Nemeth, E., Sundquist, W. I., Ganz, T., Musci, G., & Kaplan, J. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-01-0060 · Cited by 434 · see citing works
An E3 ligase possessing an iron-responsive hemerythrin domain is a regulator of iron homeostasis
Salahudeen, A. A., Thompson, J. W., Ruiz, J. C., Ma, H.-W., Kinch, L. N., Li, Q., Grishin, N. V., & Bruick, R. K. (2009) · Science · doi:10.1126/science.1176326 · Cited by 432 · see citing works
Intestinal Hypoxia-Inducible Transcription Factors Are Essential for Iron Absorption following Iron Deficiency
Shah, Y. M., Matsubara, T., Ito, S., Yim, S.-H., & Gonzalez, F. J. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2008.12.012 · Cited by 431 · see citing works
Control of iron homeostasis by an iron-regulated ubiquitin ligase
Vashisht, A. A., Zumbrennen, K. B., Huang, X., Powers, D. N., Durazo, A., Sun, D., Bhaskaran, N., Persson, A., Uhlen, M., Sangfelt, O., et al. (2009) · Science · doi:10.1126/science.1176333 · Cited by 429 · see citing works
Identification of a Human Heme Exporter that Is Essential for Erythropoiesis
Quigley, J. G., Yang, Z., Worthington, M., Phillips, J. D., Sabo, K. M., Sabath, D. E., Berg, C. L., Sassa, S., Wood, B. L., & Abkowitz, J. L. (2004) · Cell · doi:10.1016/j.cell.2004.08.014 · Cited by 423 · see citing works
Cytokine-mediated regulation of iron transport in human monocytic cells
Ludwiczek, S., Aigner, E., Theurl, I., & Weiss, G. (2003) · Blood · doi:10.1182/blood-2002-08-2459 · Cited by 420 · see citing works
Slc11a2 is required for intestinal iron absorption and erythropoiesis but dispensable in placenta and liver
Gunshin, H., Fujiwara, Y., Custodio, A. O., DiRenzo, C., Robine, S., & Andrews, N. C. (2005) · Journal of Clinical Investigation · doi:10.1172/jci24356 · Cited by 419 · see citing works
Iron homeostasis: insights from genetics and animal models
Andrews, N. C. (2000) · Nature Reviews Genetics · doi:10.1038/35042073 · Cited by 418 · see citing works
Genetic ablations of iron regulatory proteins 1 and 2 reveal why iron regulatory protein 2 dominates iron homeostasis.
Meyron‐Holtz, E. G., Ghosh, M. C., Iwai, K., LaVaute, T., Brazzolotto, X., Berger, U. V., Land, W., Ollivierre‐Wilson, H., Grinberg, A., Love, P., et al. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600041 · Cited by 408 · see citing works
Mutation of a Putative Mitochondrial Iron Transporter Gene (ABC7) in X-Linked Sideroblastic Anemia and Ataxia (XLSA/A)
Allikmets, R. L., Raskind, W. H., Hutchinson, A. A., Schueck, N. D., Dean, M. C., & Koeller, D. M. (1999) · Human Molecular Genetics · doi:10.1093/hmg/8.5.743 · Cited by 406 · see citing works
A Heme Export Protein Is Required for Red Blood Cell Differentiation and Iron Homeostasis
Keel, S. B., Doty, R. T., Yang, Z., Quigley, J. G., Chen, J., Knoblaugh, S., Kingsley, P. D., De Domenico, I., Vaughn, M. B., Kaplan, J., et al. (2008) · Science · doi:10.1126/science.1151133 · Cited by 404 · see citing works
A human mitochondrial ferritin encoded by an intronless gene
Levi, S., Corsi, B., Bosisio, M., Invernizzi, R., Volz, A., Sanford, D., Arosio, P., & Drysdale, J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.c100141200 · Cited by 400 · see citing works
Hemojuvelin is essential for dietary iron sensing, and its mutation leads to severe iron overload
Niederkofler, V. (2005) · Journal of Clinical Investigation · doi:10.1172/jci25683 · Cited by 368 · see citing works
A mouse model of juvenile hemochromatosis
Huang, F. W. (2005) · Journal of Clinical Investigation · doi:10.1172/jci25049 · Cited by 363 · see citing works
Regulation of Mitochondrial Iron Import through Differential Turnover of Mitoferrin 1 and Mitoferrin 2
Paradkar, P. N., Zumbrennen, K. B., Paw, B. H., Ward, D. M., & Kaplan, J. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01685-08 · Cited by 362 · see citing works
Identification of a mammalian mitochondrial porphyrin transporter
Krishnamurthy, P. C., Du, G., Fukuda, Y., Sun, D., Sampath, J., Mercer, K. E., Wang, J., Sosa‐Pineda, B., Murti, K. G., & Schuetz, J. D. (2006) · Nature · doi:10.1038/nature05125 · Cited by 358 · see citing works
Scara5 Is a Ferritin Receptor Mediating Non-Transferrin Iron Delivery
Li, J. Y., Paragas, N., Ned, R. M., Qiu, A., Viltard, M., Leete, T., Drexler, I. R., Chen, X., Sanna‐Cherchi, S., Mohammed, F., et al. (2009) · Developmental Cell · doi:10.1016/j.devcel.2008.12.002 · Cited by 355 · see citing works
Hereditary hemochromatosis protein, HFE, interaction with transferrin receptor 2 suggests a molecular mechanism for mammalian iron sensing.
Goswami, T., & Andrews, N. C. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.c600197200 · Cited by 352 · see citing works
Identification of TWSG1 as a second novel erythroid regulator of hepcidin expression in murine and human cells
Tanno, T., Porayette, P., Sripichai, O., Noh, S.-J., Byrnes, C., Bhupatiraju, A., Lee, Y. T., Goodnough, J. B., Harandi, O., Ganz, T., et al. (2009) · Blood · doi:10.1182/blood-2008-12-195503 · Cited by 352 · see citing works
Iron Metabolism in the Reticuloendothelial System
Knutson, M. D., & Wessling‐Resnick, M. (2003) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/713609210 · Cited by 349 · see citing works
The Transferrin Receptor Modulates Hfe-Dependent Regulation of Hepcidin Expression
Schmidt, P. J., Toran, P. T., Giannetti, A. M., Bjorkman, P. J., & Andrews, N. C. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2007.11.016 · Cited by 345 · see citing works
Iron in biochemistry and medicine.
Jacobs, A. K., & Worwood, M. (1974) · Medical Entomology and Zoology · Cited by 338 · see citing works
Transferrin receptor 1
Aisen, P. (2004) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2004.02.007 · Cited by 329 · see citing works
Iron metabolism in the anemia of chronic disease
Weiss, G. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2008.08.006 · Cited by 322 · see citing works
How pathogenic bacteria evade mammalian sabotage in the battle for iron
Fischbach, M. A., Lin, H., Liu, D. R., & Walsh, C. T. (2006) · Nature Chemical Biology · doi:10.1038/nchembio771 · Cited by 321 · see citing works
Cytosolic and mitochondrial ferritins in the regulation of cellular iron homeostasis and oxidative damage
Arosio, P., & Levi, S. (2010) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2010.02.005 · Cited by 320 · see citing works
Haem homeostasis is regulated by the conserved and concerted functions of HRG-1 proteins
Rajagopal, A., Rao, A. U., Amigo, J., Tian, M., Upadhyay, S. K., Hall, C., Uhm, S., Mathew, M. K., Fleming, M. D., Paw, B. H., et al. (2008) · Nature · doi:10.1038/nature06934 · Cited by 316 · see citing works
STAT3 Is Required for IL-6-gp130–Dependent Activation of Hepcidin In Vivo
Pietrangelo, A., Dierssen, U., Valli, L., Garuti, C., Rump, A., Corradini, E., Ernst, M., Klein, C., & Trautwein, C. (2007) · Gastroenterology · doi:10.1053/j.gastro.2006.10.018 · Cited by 315 · see citing works
Iron-dependent regulation of the divalent metal ion transporter
Gunshin, H., Allerson, C. R., Polycarpou-Schwarz, M., Rofts, A., Rogers, J. T., Kishi, F., Hentze, M. W., Rouault, T. A., Andrews, N. C., & Hediger, M. A. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)03189-1 · Cited by 305 · see citing works
Membrane-bound serine protease matriptase-2 (Tmprss6) is an essential regulator of iron homeostasis
Folgueras, A. R., de Lara, F. M., Pendás, A. M., Garabaya, C., Rodríguez, F. J., Astudillo, A., Bernal, T., Cabanillas, R., López-Otı́n, C., & Velasco, G. (2008) · Blood · doi:10.1182/blood-2008-04-149773 · Cited by 300 · see citing works
A Mammalian Siderophore Synthesized by an Enzyme with a Bacterial Homolog Involved in Enterobactin Production
Devireddy, L. R., Hart, D. O., Goetz, D. H., & Green, M. R. (2010) · Cell · doi:10.1016/j.cell.2010.04.040 · Cited by 295 · see citing works
Self-citation
Functions of mitochondrial ISCU and cytosolic ISCU in mammalian iron-sulfur cluster biogenesis and iron homeostasis
Tong, W.-H., & Rouault, T. A. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.02.003 · Cited by 294 · see citing works
Iron trafficking in the mitochondrion: novel pathways revealed by disease
Napier, I. A., Ponka, P., & Richardson, D. R. (2004) · Blood · doi:10.1182/blood-2004-10-3856 · Cited by 287 · see citing works
A ferroportin transcript that lacks an iron-responsive element enables duodenal and erythroid precursor cells to evade translational repression
Zhang, D.-L., Hughes, R. M., Ollivierre-Wilson, H., Ghosh, M. C., & Rouault, T. A. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.03.006 · Cited by 281 · see citing works
Cytosolic Monothiol Glutaredoxins Function in Intracellular Iron Sensing and Trafficking via Their Bound Iron-Sulfur Cluster
Mühlenhoff, U., Molik, S., Godoy, J. R., Uzarska, M. A., Richter, N., Seubert, A., Zhang, Y., Stubbe, J., Pierrel, F., Herrero, E., et al. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.08.001 · Cited by 276 · see citing works
The importance of non-transferrin bound iron in disorders of iron metabolism
Breuer, W., Hershko, C., & Cabantchik, Z. I. (2000) · Transfusion Science · doi:10.1016/s0955-3886(00)00087-4 · Cited by 268 · see citing works
Hepcidin mRNA levels in mouse liver respond to inhibition of erythropoiesis
Vokurka, M., Krijt, J., Šulc, K., & Nečas, E. (2006) · Physiological Research · doi:10.33549/physiolres.930841 · Cited by 263 · see citing works
Mechanisms of heme iron absorption: Current questions and controversies
West, A. R., & Oates, P. S. (2008) · World Journal of Gastroenterology · doi:10.3748/wjg.14.4101 · Cited by 257 · see citing works
Comparison of the Interactions of Transferrin Receptor and Transferrin Receptor 2 with Transferrin and the Hereditary Hemochromatosis Protein HFE
West, A. P., Bennett, M. J., Sellers, V. M., Andrews, N. C., Enns, C. A., & Bjorkman, P. J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.c000664200 · Cited by 257 · see citing works
Intracellular labile iron pools as direct targets of iron chelators: a fluorescence study of chelator action in living cells
Glickstein, H., El, R. B., Shvartsman, M., & Cabantchik, Z. I. (2005) · Blood · doi:10.1182/blood-2005-02-0460 · Cited by 249 · see citing works
C/EBPα Regulates Hepatic Transcription of Hepcidin, an Antimicrobial Peptide and Regulator of Iron Metabolism
Courselaud, B., Pigeon, C., Inoue, Y., Inoue, J., Gonzalez, F. J., Leroyer, P., Gilot, D., Boudjema, K., Guguen-Guillouzo, C., Brissot, P., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202653200 · Cited by 245 · see citing works
Expression of hepcidin in hereditary hemochromatosis: evidence for a regulation in response to the serum transferrin saturation and to non-transferrin-bound iron
Gehrke, S. G., Kulaksiz, H., Herrmann, T. R. W., Riedel, H.-D., Bents, K., Veltkamp, C., & Stremmel, W. (2003) · Blood · doi:10.1182/blood-2002-11-3610 · Cited by 244 · see citing works
Competitive regulation of hepcidin mRNA by soluble and cell-associated hemojuvelin
Lin, L., Goldberg, Y. P., & Ganz, T. (2005) · Blood · doi:10.1182/blood-2005-05-1845 · Cited by 241 · see citing works
Expression of hepcidin is down-regulated in TfR2 mutant mice manifesting a phenotype of hereditary hemochromatosis
Kawabata, H., Fleming, R. E., Gui, D., Moon, S. Y., Saitoh, T., O’Kelly, J., Umehara, Y., Wano, Y., SAID, J. W., & Koeffler, H. P. (2004) · Blood · doi:10.1182/blood-2004-04-1416 · Cited by 238 · see citing works
Ferroportin‐mediated mobilization of ferritin iron precedes ferritin degradation by the proteasome
De Domenico, I., Vaughn, M. B., Li, L., Bagley, D., Musci, G., Ward, D. M., & Kaplan, J. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601409 · Cited by 235 · see citing works
Microcytic anemia, erythropoietic protoporphyria, and neurodegeneration in mice with targeted deletion of iron-regulatory protein 2
Cooperman, S. S., Meyron-Holtz, E. G., Olivierre-Wilson, H., Ghosh, M. C., McConnell, J. P., & Rouault, T. A. (2005) · Blood · doi:10.1182/blood-2004-12-4703 · Cited by 235 · see citing works
Evidence for distinct pathways of hepcidin regulation by acute and chronic iron loading in mice
Ramos, E., Kautz, L., Rodriguez, R., Hansen, M., Gabayan, V. R., Ginzburg, Y. Z., Roth, M., Nemeth, E., & Ganz, T. (2011) · Hepatology · doi:10.1002/hep.24178 · Cited by 235 · see citing works
Posttranslational processing of hepcidin in human hepatocytes is mediated by the prohormone convertase furin.
Valore, E. V., & Ganz, T. (2008) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2007.07.009 · Cited by 234 · see citing works
Cellular iron: Ferroportin is the only way out
Ganz, T. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.02.005 · Cited by 232 · see citing works
Diferric transferrin regulates transferrin receptor 2 protein stability
Johnson, M. B., & Enns, C. A. (2004) · Blood · doi:10.1182/blood-2004-06-2477 · Cited by 230 · see citing works
Intestinal DMT1 cotransporter is down-regulated by hepcidin via proteasome internalization and degradation
Brasse–Lagnel, C., Karim, Z., Letteron, P., Bekri, S., Bado, A., & Beaumont, C. (2011) · Gastroenterology · doi:10.1053/j.gastro.2010.12.037 · Cited by 230 · see citing works
The Chelatable Iron Pool in Living Cells: A Methodically Defined Quantity
Petrat, F. M., de GROOT, H., Sustmann, R., & Rauen, U. (2002) · Biological Chemistry · doi:10.1515/bc.2002.051 · Cited by 230 · see citing works
The molecular basis of ferroportin-linked hemochromatosis
De Domenico, I., Ward, D. M., Nemeth, E., Vaughn, M. B., Musci, G., Ganz, T., & Kaplan, J. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0503804102 · Cited by 230 · see citing works
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
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
Identification of a human mutation of DMT1 in a patient with microcytic anemia and iron overload
Mims, M. P., Guan, Y., Pospı́šilová, D., Priwitzerova, M., Indrák, K., Ponka, P., Divoký, V., & Prchal, J. T. (2005) · Blood · doi:10.1182/blood-2004-07-2966 · Cited by 219 · 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
Discovery of Genes Essential for Heme Biosynthesis through Large-Scale Gene Expression Analysis
Nilsson, R., Schultz, I. J., Pierce, E. L., Soltis, K. A., Naranuntarat, A., Ward, D. M., Baughman, J. M., Paradkar, P. N., Kingsley, P. D., Culotta, V., et al. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.06.012 · Cited by 213 · see citing works
H-ferritin subunit overexpression in erythroid cells reduces the oxidative stress response and induces multidrug resistance properties
Epsztejn, S., Glickstein, H., Picard, V., Slotki, I. N., Breuer, W., Beaumont, C., & Cabantchik, Z. I. (1999) · Blood · doi:10.1182/blood.v94.10.3593.422k26_3593_3603 · Cited by 209 · see citing works
The mitochondrial ATP-binding cassette transporter Abcb7 is essential in mice and participates in cytosolic iron–sulfur cluster biogenesis
Pondarré, C., Antiochos, B., Campagna, D. R., Clarke, S. L., Greer, E. L., Deck, K. M., McDonald, A. A., Han, A., Medlock, A. E., Kutok, J. L., et al. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl012 · Cited by 208 · 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
Regulation of transferrin receptor 2 protein levels by transferrin
Robb, A., & Wessling‐Resnick, M. (2004) · Blood · doi:10.1182/blood-2004-06-2481 · Cited by 204 · 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
A new role for the transferrin receptor in the release of iron from transferrin
Bali, P. K., Zak, O., & Aisen, P. (1991) · Biochemistry · doi:10.1021/bi00216a003 · Cited by 186 · see citing works
Perturbation of hepcidin expression by BMP type I receptor deletion induces iron overload in mice
Steinbicker, A. U., Bartnikas, T. B., Isbell, L. K., Leyton, P., Mayeur, C., Kao, S. M., Pappas, A. E., Peterson, R. T., Bloch, D. B., Yu, P. B., et al. (2011) · Blood · doi:10.1182/blood-2011-03-339952 · Cited by 181 · see citing works
The role of the iron responsive element in the control of ferroportin1/IREG1/MTP1 gene expression
Lymboussaki, A., Pignatti, E., Montosi, G., Garuti, C., Haile, D. J., & Pietrangelo, A. (2003) · Journal of Hepatology · doi:10.1016/s0168-8278(03)00408-2 · Cited by 177 · see citing works
Specific iron chelators determine the route of ferritin degradation
De Domenico, I., Ward, D. M., & Kaplan, J. (2009) · Blood · doi:10.1182/blood-2009-05-224188 · Cited by 176 · see citing works
The Zinc Transporter SLC39A14/ZIP14 Controls G-Protein Coupled Receptor-Mediated Signaling Required for Systemic Growth
Hojyo, S., Fukada, T., Shimoda, S., Ohashi, W., Bin, B.-H., Koseki, H., & Hirano, T. (2011) · PLoS ONE · doi:10.1371/journal.pone.0018059 · Cited by 175 · see citing works
Mitochondrial Ferritin Expression in Adult Mouse Tissues
Santambrogio, P., Biasiotto, G., Sanvito, F., Olivieri, S., Arosio, P., & Levi, S. (2007) · Journal of Histochemistry & Cytochemistry · doi:10.1369/jhc.7a7273.2007 · Cited by 168 · see citing works
Evolution of the iron-responsive element
Piccinelli, P., & Samuelsson, T. (2007) · RNA · doi:10.1261/rna.464807 · Cited by 168 · see citing works
The FBXL5-IRP2 Axis Is Integral to Control of Iron Metabolism In Vivo
Moroishi, T., Nishiyama, M., Takeda, Y., Iwaï, K., & Nakayama, K. I. (2011) · Cell Metabolism · doi:10.1016/j.cmet.2011.07.011 · Cited by 163 · see citing works
Hepatic hypoxia-inducible factor-2 down-regulates hepcidin expression in mice through an erythropoietin-mediated increase in erythropoiesis
Mastrogiannaki, M., Matak, P., Mathieu, J. R. R., Delga, S., Mayeux, P., Vaulont, S., & Peyssonnaux, C. (2011) · Haematologica · doi:10.3324/haematol.2011.056119 · Cited by 161 · 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
First phenotypic description of transferrin receptor 2 knockout mouse, and the role of hepcidin
Wallace, D. F., Summerville, L., Lusby, P. E., & Subramaniam, V. N. (2005) · Gut · doi:10.1136/gut.2004.062018 · Cited by 160 · see citing works
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
Modulation of Iron Uptake in Heart by L-Type Ca2+Channel Modifiers
Tsushima, R. G., Wickenden, A. D., Bouchard, R. A., Oudit, G. Y., Liu, P. P., & Backx, P. H. (1999) · Circulation Research · doi:10.1161/01.res.84.11.1302 · Cited by 157 · see citing works
The effects of erythropoetic activity and iron burden on hepcidin expression in patients with thalassemia major.
Kattamis, A., Papassotiriou, I., Palaiologou, D., Apostolakou, F., Galani, A., Ladis, V., Sakellaropoulos, N., & Papanikolaou, G. (2006) · PubMed · Cited by 156 · see citing works
Hfe Acts in Hepatocytes to Prevent Hemochromatosis
Spasić, M. V., Kiss, J., Herrmann, T. R. W., Galy, B., Martinache, S., Stolte, J., Gröne, H., Stremmel, W., Hentze, M. W., & Muckenthaler, M. U. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2007.11.014 · Cited by 150 · 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
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
Frataxin and Mitochondrial FeS Cluster Biogenesis
Stemmler, T. L., Lesuisse, E., Pain, D., & Dancis, A. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.r110.118679 · Cited by 145 · see citing works
Juvenile hemochromatosis associated with pathogenic mutations of adult hemochromatosis genes
Pietrangelo, A., Caleffi, A., Henrion, J., Ferrara, F., Corradini, E., Kulaksiz, H., Stremmel, W., Andreoné, P., & Garuti, C. (2005) · Gastroenterology · doi:10.1053/j.gastro.2004.11.057 · Cited by 145 · see citing works
HFE and Transferrin Directly Compete for Transferrin Receptor in Solution and at the Cell Surface
Giannetti, A. M., & Björkman, P. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m401467200 · Cited by 143 · see citing works
Iron, lipocalin, and kidney epithelia
Yang, J., Mori, K., Li, J. Y., & Barasch, J. M. (2003) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00008.2003 · Cited by 139 · see citing works
Genetic and epigenetic silencing of SCARA5 may contribute to human hepatocellular carcinoma by activating FAK signaling
Huang, J., Zheng, D., Qin, F., et al. (2009) · Journal of Clinical Investigation · doi:10.1172/jci38012 · Cited by 139 · see citing works
Identification of differentially expressed genes in response to dietary iron deprivation in rat duodenum
Collins, J. F., Franck, C. A., Kowdley, K. V., & Ghishan, F. K. (2005) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00489.2004 · Cited by 138 · see citing works
Intestinal Ferritin H Is Required for an Accurate Control of Iron Absorption
Vanoaica, L., Darshan, D., Richman, L., Schümann, K., & Kühn, L. C. (2010) · Cell Metabolism · doi:10.1016/j.cmet.2010.08.003 · Cited by 137 · see citing works
Hepcidin Levels and Their Determinants in Different Types of Myelodysplastic Syndromes
Santini, V., Girelli, D., Sanna, A., Martinelli, N., Duca, L., Campostrini, N., Cortelezzi, A., Corbella, M., Bosi, A., Reda, G., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0023109 · Cited by 133 · see citing works
Analysis of the biologic functions of H- and L-ferritins in HeLa cells by transfection with siRNAs and cDNAs: evidence for a proliferative role of L-ferritin
Cozzi, A., Corsi, B., Levi, S., Santambrogio, P., Biasiotto, G., & Arosio, P. (2004) · Blood · doi:10.1182/blood-2003-06-1842 · Cited by 132 · see citing works
The Fowler Syndrome-Associated Protein FLVCR2 Is an Importer of Heme
Duffy, S. P., Shing, J. C., Saraon, P., Berger, L., Eiden, M. V., Wilde, A., & Tailor, C. S. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.00690-10 · Cited by 130 · see citing works
Beyond the superfamily: the lipocalin receptors
Flower, D. R. (2000) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(00)00169-2 · Cited by 128 · see citing works
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
Mutational analysis of the transferrin receptor reveals overlapping HFE and transferrin binding sites
West, A. P., Giannetti, A. M., Herr, A. B., Bennett, M. J., Nangiana, J. S., Pierce, J. R., Weiner, L. P., Snow, P. M., & Björkman, P. J. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.5048 · Cited by 125 · see citing works
Targeted Disruption of the Hepatic Transferrin Receptor 2 Gene in Mice Leads to Iron Overload
Wallace, D. F., Summerville, L., & Subramaniam, V. N. (2006) · Gastroenterology · doi:10.1053/j.gastro.2006.11.028 · Cited by 124 · see citing works
Divalent metal transporter 1
Mims, M. P., & Prchal, J. T. (2005) · Hematology · doi:10.1080/10245330500093419 · Cited by 123 · see citing works
Regulation of TMPRSS6 by BMP6 and iron in human cells and mice
Meynard, D., Vaja, V., Sun, C. C., Corradini, E., Chen, S., López-Otı́n, C., Grgurević, L., Hong, C. C., Stirnberg, M., Gütschow, M., et al. (2011) · Blood · doi:10.1182/blood-2011-04-348698 · 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
Cross-talk between the mitogen activated protein kinase and bone morphogenetic protein/hemojuvelin pathways is required for the induction of hepcidin by holotransferrin in primary mouse hepatocytes
Ramey, G., Deschemin, J., & Vaulont, S. (2009) · Haematologica · doi:10.3324/haematol.2008.003541 · Cited by 122 · see citing works
Lysosomal proteolysis is the primary degradation pathway for cytosolic ferritin and cytosolic ferritin degradation is necessary for iron exit
Zhang, Y., Mikhael, M., Xu, D., Li, Y., Soe-Lin, S., Ning, B., Li, W., Nie, G., Zhao, Y., & Ponka, P. (2010) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3129 · Cited by 120 · 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
Intracellular kinetics of iron in reticulocytes: evidence for endosome involvement in iron targeting to mitochondria
Zhang, A., Sheftel, A. D., & Ponka, P. (2004) · Blood · doi:10.1182/blood-2004-06-2226 · Cited by 119 · see citing works
Transferrin, the transferrin receptor, and the uptake of iron by cells.
Aisen, P. (1998) · PubMed · Cited by 117 · see citing works
Mutations in FLVCR1 Cause Posterior Column Ataxia and Retinitis Pigmentosa
Rajadhyaksha, A. M., Elemento, O., Puffenberger, E. G., Schierberl, K. C., Xiang, J., Putorti, M. L., Berciano, J., Poulin, C., Brais, B., Michaelides, M., et al. (2010) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2010.10.013 · Cited by 108 · see citing works
Identification of a Steap3 endosomal targeting motif essential for normal iron metabolism
Lambe, T., Simpson, R. J., Dawson, S., Bouriez‐Jones, T., Crockford, T. L., Lepherd, M. L., Latunde-Dada, G. O., Robinson, H., Raja, K. B., Campagna, D. R., et al. (2008) · Blood · doi:10.1182/blood-2007-11-120402 · Cited by 103 · see citing works
Iron Regulation of Hepcidin Despite Attenuated Smad1,5,8 Signaling in Mice Without Transferrin Receptor 2 or Hfe
Corradini, E., Rozier, M., Meynard, D., Odhiambo, A., Lin, H. Y.-F., Feng, Q., Migas, M. C., Britton, R. S., Babitt, J. L., & Fleming, R. E. (2011) · Gastroenterology · doi:10.1053/j.gastro.2011.06.077 · Cited by 102 · 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
Targeted deletion of the mouse Mitoferrin1 gene: from anemia to protoporphyria
Troadec, M.-B., Warner, D., Wallace, J., Thomas, K., Spangrude, G. J., Phillips, J., Khalimonchuk, O., Paw, B. H., Ward, D. M., & Kaplan, J. (2011) · Blood · doi:10.1182/blood-2010-11-319483 · Cited by 97 · see citing works
Serum hepcidin levels are innately low in HFE‐related haemochromatosis but differ between C282Y‐homozygotes with elevated and normal ferritin levels
van Dijk, B. A. C., Laarakkers, C. M., Klaver, S. M., Jacobs, E. M. G., van Tits, L. J. H., Janssen, M. C. H., & Swinkels, D. W. (2008) · British Journal of Haematology · doi:10.1111/j.1365-2141.2008.07273.x · Cited by 95 · see citing works
Iron‐responsive degradation of iron‐regulatory protein 1 does not require the Fe–S cluster
Clarke, S. L., Vasanthakumar, A., Anderson, S. A., Pondarré, C., Koh, C. M., Deck, K. M., Pitula, J. S., Epstein, C. J., Fleming, M. D., & Eisenstein, R. S. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7600954 · Cited by 95 · see citing works
Evidence for a lack of a direct transcriptional suppression of the iron regulatory peptide hepcidin by hypoxia-inducible factors
Volke, M., Gale, D. P., Maegdefrau, U., Schley, G., Klanke, B., Bosserhoff, A.-K., Maxwell, P. H., Eckardt, K.-U., & Warnecke, C. (2009) · PLoS ONE · doi:10.1371/journal.pone.0007875 · Cited by 93 · see citing works
Remodeling the regulation of iron metabolism during erythroid differentiation to ensure efficient heme biosynthesis
Schranzhofer, M., Schifrer, M., Cabrera, J. A., Kopp, S., Chiba, P., Beug, H., & Müllner, E. W. (2006) · Blood · doi:10.1182/blood-2005-05-1809 · Cited by 89 · see citing works
The Hereditary Hemochromatosis Protein, HFE, Inhibits Iron Uptake via Down-regulation of Zip14 in HepG2 Cells
Gao, J., Zhao, N., Knutson, M. D., & Enns, C. A. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803150200 · Cited by 89 · see citing works
Plasma hepcidin is a modest predictor of dietary iron bioavailability in humans, whereas oral iron loading, measured by stable-isotope appearance curves, increases plasma hepcidin
Zimmermann, M. B., Troesch, B., Biebinger, R., Egli, I. M., Zeder, C., & Hurrell, R. F. (2009) · American Journal of Clinical Nutrition · doi:10.3945/ajcn.2009.28129 · Cited by 84 · see citing works
HFE Modulates Transferrin Receptor 2 Levels in Hepatoma Cells via Interactions That Differ from Transferrin Receptor 1-HFE Interactions
Chen, J., Chloupková, M., Gao, J., Arvedson, T., & Enns, C. A. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m706720200 · Cited by 81 · see citing works
Transferrin receptor 2 and HFE regulate furin expression via mitogen-activated protein kinase/extracellular signal-regulated kinase (MAPK/Erk) signaling. Implications for transferrin-dependent hepcidin regulation
Poli, M., Luscieti, S., Gandini, V., Maccarinelli, F., Finazzi, D., Silvestri, L., Roetto, A., & Arosio, P. (2010) · Haematologica · doi:10.3324/haematol.2010.027003 · Cited by 81 · see citing works
A time course of hepcidin response to iron challenge in patients with HFE and TFR2 hemochromatosis
Girelli, D., Trombini, P., Busti, F., Campostrini, N., Sandri, M. F., Pelucchi, S., Westerman, M., Ganz, T., Nemeth, E., Piperno, A., et al. (2010) · Haematologica · doi:10.3324/haematol.2010.033449 · Cited by 79 · see citing works
Mouse models to study L-type calcium channel function
Moosmang, S., Lenhardt, P., Haider, N., Hofmann, F. B., & Wegener, J. W. (2005) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2004.12.003 · Cited by 79 · see citing works
nm1054: a spontaneous, recessive, hypochromic, microcytic anemia mutation in the mouse
Ohgami, R. S., Campagna, D. R., Antiochos, B., Wood, E., Sharp, J. J., Barker, J. E., & Fleming, M. D. (2005) · Blood · doi:10.1182/blood-2005-01-0379 · Cited by 74 · see citing works
A Spontaneous, Recurrent Mutation in Divalent Metal Transporter-1 Exposes a Calcium Entry Pathway
Xu, H., Jin, J., DeFelice, L. J., Andrews, N. C., & Clapham, D. E. (2004) · PLoS Biology · doi:10.1371/journal.pbio.0020050 · Cited by 72 · see citing works
Isolation and characterization of a siderophore-like growth factor from mutants of SV40-transformed cells adapted to picolinic acid
Fernandez-Pol, J. A. (1978) · Cell · doi:10.1016/0092-8674(78)90235-0 · Cited by 72 · see citing works
Iron-Dependent Degradation of Apo-IRP1 by the Ubiquitin-Proteasome Pathway
Wang, J., Fillebeen, C., Chen, G., Biederbick, A., Lill, R., & Pantopoulos, K. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01111-06 · Cited by 72 · see citing works
Self-citation
Functional role of DMT1 in transferrin-independent iron uptake by human hepatocyte and hepatocellular carcinoma cell, HLF
SHINDO, M., Torimoto, Y., SAITO, H., Motomura, W., Ikuta, K., SATO, K., FUJIMOTO, Y., & KOHGO, Y. (2006) · Hepatology Research · doi:10.1016/j.hepres.2006.03.011 · Cited by 71 · see citing works
THE MOLECULAR BASIS
Pandolfo, M. (2002) · Cited by 70 · see citing works
T Cell, Ig Domain, Mucin Domain-2 Gene-Deficient Mice Reveal a Novel Mechanism for the Regulation of Th2 Immune Responses and Airway Inflammation
Rennert, P. D., Ichimura, T., Sizing, I. D., Bailly, V., Li, Z., Rennard, R., McCoon, P., Pablo, L., Miklasz, S., Tarilonte, L., et al. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.177.7.4311 · Cited by 67 · see citing works
Defective Bone Morphogenic Protein Signaling Underlies Hepcidin Deficiency in HFE Hereditary Hemochromatosis
Ryan, J. D., Ryan, E. M., Fabre, A., Lawless, M. W., & Crowe, J. (2010) · Hepatology · doi:10.1002/hep.23814 · Cited by 66 · see citing works
24p3 and Its Receptor: Dawn of a New Iron Age?
Richardson, D. R. (2005) · Cell · doi:10.1016/j.cell.2005.12.008 · Cited by 64 · see citing works
Identification of Mutations in SLC40A1 That Affect Ferroportin Function and Phenotype of Human Ferroportin Iron Overload
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 · see citing works
Skeletal muscle hemojuvelin is dispensable for systemic iron homeostasis
Chen, W., Huang, F. W., Renshaw, T. B. D., & Andrews, N. C. (2011) · Blood · doi:10.1182/blood-2010-12-327957 · Cited by 58 · see citing works

Flagged first, then by citations

Research works printed but not linked: 3

[117]Johnson MB Enns CA 2004 Differic transferrin regulates transferrin receptor 2 protein stability Blood 104 4287 4293 15319290
[118]Robb A Wessling-Resnick M 2004 Regulation of transferrin receptor 2 protein levels by transferrin Blood 104 4294 4299 15319276
[120]Wallace DF Summerville L Subramaniam VN 2007 Targeted disruption of the hepatic transferrin receptor 2 gene in mice leads to iron overload Gastroenterol 132 301 310 17241880

Sorted by citations

Quantitative proteomics identifies NCOA4 as the cargo receptor mediating ferritinophagy
Mancias, J. D., Wang, X., Gygi, S. P., Harper, J. W., & Kimmelman, A. C. (2014) · Nature · doi:10.1038/nature13148 · Cited by 2,084 · see citing works
Pancreatic cancer: Advances and challenges
Halbrook, C. J., Lyssiotis, C. A., Pasca di Magliano, M., & Maitra, A. (2023) · Cell · doi:10.1016/j.cell.2023.02.014 · Cited by 1,321 · see citing works
Cargo recognition and degradation by selective autophagy
Gatica, D., Lahiri, V., & Klionsky, D. J. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0037-z · Cited by 1,067 · see citing works
Macrophage defense mechanisms against intracellular bacteria
Weiss, G., & Schaible, U. E. (2015) · Immunological Reviews · doi:10.1111/imr.12266 · Cited by 989 · see citing works
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
Ferritinophagy via NCOA4 is required for erythropoiesis and is regulated by iron dependent HERC2-mediated proteolysis
Mancias, J. D., Pontano Vaites, L., Nissim, S., Biancur, D. E., Kim, A. J., Wang, X., Liu, Y., Goessling, W., Kimmelman, A. C., & Harper, J. W. (2015) · eLife · doi:10.7554/elife.10308 · Cited by 552 · see citing works
The role of zinc, copper, manganese and iron in neurodegenerative diseases
Mezzaroba, L., Alfieri, D. F., Colado Simão, A. N., & Vissoci Reiche, E. M. (2019) · NeuroToxicology · doi:10.1016/j.neuro.2019.07.007 · Cited by 524 · see citing works
Heme-mediated SPI-C induction promotes monocyte differentiation into iron-recycling macrophages
Haldar, M., Kohyama, M., So, A. Y.-L., KC, W., Wu, X., Briseño, C. G., Satpathy, A. T., Kretzer, N. M., Arase, H., Rajasekaran, N. S., et al. (2014) · Cell · doi:10.1016/j.cell.2014.01.069 · Cited by 431 · 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 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
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
Diverging roles of bacterial siderophores during infection
Holden, V. I., & Bachman, M. A. (2015) · Metallomics · doi:10.1039/c4mt00333k · Cited by 274 · 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
NCOA4-Mediated Ferritinophagy: A Potential Link to Neurodegeneration
Quiles del Rey, M., & Mancias, J. D. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00238 · Cited by 227 · see citing works
Mechanisms of Selective Autophagy in Normal Physiology and Cancer
Mancias, J. D., & Kimmelman, A. C. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.02.027 · Cited by 196 · see citing works
Nrf2 attenuates ferroptosis-mediated IIR-ALI by modulating TERT and SLC7A11
Dong, H., Xia, Y., Jin, S., Xue, C., Wang, Y., Hu, R., & Jiang, H. (2021) · Cell Death & Disease · doi:10.1038/s41419-021-04307-1 · Cited by 196 · see citing works
“Pumping iron”—how macrophages handle iron at the systemic, microenvironmental, and cellular levels
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 · see citing works
Role of divalent metals in infectious disease susceptibility and outcome
Weiss, G., & Carver, P. L. (2018) · Clinical Microbiology and Infection · doi:10.1016/j.cmi.2017.01.018 · Cited by 123 · see citing works
Iron at the Centre of Candida albicans Interactions
Fourie, R., Kuloyo, O. O., Mochochoko, B. M., Albertyn, J., & Pohl, C. H. (2018) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2018.00185 · Cited by 118 · see citing works
Iron and innate antimicrobial immunity-depriving the pathogen, defending the host
Nairz, M., Dichtl, S., Schroll, A., Haschka, D., Tymoszuk, P., Theurl, I., & Weiss, G. (2018) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2018.03.007 · Cited by 123 · see citing works
Steap4 Plays a Critical Role in Osteoclastogenesis in Vitro by Regulating Cellular Iron/Reactive Oxygen Species (ROS) Levels and cAMP Response Element-binding Protein (CREB) Activation
Zhou, J., Ye, S., Fujiwara, T., Manolagas, S. C., & Zhao, H. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.478750 · Cited by 88 · see citing works
‘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 · see citing works
Simultaneous Fe 2+ /Fe 3+ imaging shows Fe 3+ over Fe 2+ enrichment in Alzheimer’s disease mouse brain
Wu, Y., Torabi, S.-F., Lake, R. J., Hong, S., Yu, Z., Wu, P., Yang, Z., Nelson, K., Guo, W., Pawel, G. T., et al. (2023) · Science Advances · doi:10.1126/sciadv.ade7622 · Cited by 91 · see citing works
The human innate immune protein calprotectin induces iron starvation responses in Pseudomonas aeruginosa
Zygiel, E. M., Nelson, C. E., Brewer, L. K., Oglesby-Sherrouse, A. G., & Nolan, E. M. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.006819 · Cited by 76 · see citing works
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 · see citing works
Coordinated transcriptional and catabolic programs support iron-dependent adaptation to RAS-MAPK pathway inhibition in pancreatic cancer
Ravichandran, M., Hu, J., Cai, C., Ward, N. P., Venida, A., Foakes, C., Kuljanin, M., Yang, A., Hennessey, C. J., Yang, Y., et al. (2022) · Cancer Discovery · doi:10.1158/2159-8290.cd-22-0044 · Cited by 80 · see citing works
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 · see citing works
Multiple Myeloma Tumor Cells are Selectively Killed by Pharmacologically-dosed Ascorbic Acid
Xia, J., Xu, H., Zhang, X., Allamargot, C., Coleman, K. L., Nessler, R., Frech, I., Tricot, G., & Zhan, F. (2017) · EBioMedicine · doi:10.1016/j.ebiom.2017.02.011 · Cited by 63 · see citing works
Heme oxygenase 1 controls early innate immune response of macrophages toSalmonellaTyphimurium infection: Heme oxygenase 1 expression affects Salmonellainfection
Mitterstiller, 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 · see citing works
A novel hybrid iron regulation network combines features from pathogenic and nonpathogenic yeasts
Gerwien, F., Safyan, A., Wisgott, S., Hille, F., Kaemmer, P., Linde, J., Brunke, S., Kasper, L., & Hube, B. (2016) · mBio · doi:10.1128/mbio.01782-16 · Cited by 47 · see citing works
Hepcidin as a predictive factor and therapeutic target in erythropoiesis-stimulating agent treatment for anemia of chronic disease in rats
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 · see citing works
Endogenous siderophore 2,5-dihydroxybenzoic acid deficiency promotes anemia and splenic iron overload in mice
Liu, Z., Ciocea, A., & Devireddy, L. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.00231-14 · Cited by 41 · see citing works
Regulatory and pathogenic mechanisms in response to iron deficiency and excess in fungi
Pijuan, J., Moreno, D. F., Yahya, G., Moisa, M., Ul Haq, I., Krukiewicz, K., Mosbah, R., Metwally, K., & Cavalu, S. (2023) · Microbial Biotechnology · doi:10.1111/1751-7915.14346 · Cited by 37 · see citing works
Contrasting regulation of macrophage iron homeostasis in response to infection with Listeria monocytogenes depending on localization of bacteria
Haschka, D., Nairz, M., Demetz, E., Wienerroither, S., Decker, T., & Weiss, G. (2015) · Metallomics · doi:10.1039/c4mt00328d · Cited by 29 · see citing works
Long-Term dexamethasone exposure down-regulates hepatic TFR1 and reduces liver iron concentration in rats
Li, H., Jiang, S., Yang, C., Yang, S., He, B., Ma, W., & Zhao, R. (2017) · Nutrients · doi:10.3390/nu9060617 · Cited by 27 · see citing works
Metallomics for Alzheimer's disease treatment: Use of new generation of chelators combining metal-cation binding and transport properties
D'Acunto, C. W., Kaplánek, R., Gbelcová, H., Kejík, Z., Bříza, T., Vasina, L., Havlík, M., Ruml, T., & Král, V. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.02.084 · Cited by 26 · see citing works

Authors: Pantopoulos, K., Porwal, S. K., Tartakoff, A., & Devireddy, L.
Affiliations: Jewish General Hospital (CA)
Case Comprehensive Cancer Center (US)
Corresponding author: Devireddy, L.
ORCID: Pantopoulos, Kostas
Porwal, Suheel Kumar
Tartakoff, Alan
Devireddy, L.
Venue: Biochemistry
Publisher: American Chemical Society (ACS)
Published: 2012-07-09
Volume: 51
Issue: 29
Pages: 5705-5724
ISSN: 0006-2960 (ISSN-L)
1520-4995
DOI: 10.1021/bi300752r
PMC: PMC3572738
OpenAlex: W2033465391
Cited by: 598
References: 221
Citations by year: 2026: 28 · 2025: 50 · 2024: 59 · 2023: 57 · 2022: 56 · 2021: 47 · 2020: 42 · 2019: 51 · 2018: 45 · 2017: 32 · 2016: 29 · 2015: 28 · 2014: 48 · 2013: 23 · 2012: 1
FWCI: 5.07
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Biochemistry (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
Funders: Canadian Institutes of Health Research (MOP-86514)
National Cancer Institute (K01CA113838)
National Institute of Diabetes and Digestive and Kidney Diseases (R01DK081395)
Topics: Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
Life Sciences › Neuroscience › Neurology › Neurological diseases and metabolism
Health Sciences › Nursing › Nutrition and Dietetics › Trace Elements in Health
Keywords: iron homeostasis, iron acquisition, hepcidin, iron regulatory proteins, iron deficiency anemia, iron overload, oxidative damage, iron metabolism
MeSH terms: Anemia, Animals, Hypoxia, Biological Transport, Gene Expression Regulation, Homeostasis, Humans, Iron, Liver, Iron Metabolism Disorders, Antimicrobial Cationic Peptides, 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

Mechanisms of mammalian iron homeostasis

Abstract

Integrity signals

Claims the paper makes

Claims other papers make about this one

Self-check

Cites

Cited by

Related

Record

About these checks