Regulation of cellular iron metabolism

Wang, Jian; Pantopoulos, Kostas

doi:10.1042/bj20101825

Cited by 986Iron Metabolism and DisordersNeurological diseases and metabolismTrace Elements in Health

Regulation of cellular iron metabolism

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Wang, Jian, Pantopoulos, Kostas·2011·Biochemical Journal

DOI 10.1042/bj20101825PMC PMC3048577

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Abstract

Iron is an essential but potentially hazardous biometal. Mammalian cells require sufficient amounts of iron to satisfy metabolic needs or to accomplish specialized functions. Iron is delivered to tissues by circulating transferrin, a transporter that captures iron released into the plasma mainly from intestinal enterocytes or reticuloendothelial macrophages. The binding of iron-laden transferrin to the cell-surface transferrin receptor 1 results in endocytosis and uptake of the metal cargo. Internalized iron is transported to mitochondria for the synthesis of haem or iron-sulfur clusters, which are integral parts of several metalloproteins, and excess iron is stored and detoxified in cytosolic ferritin. Iron metabolism is controlled at different levels and by diverse mechanisms. The present review summarizes basic concepts of iron transport, use and storage and focuses on the IRE (iron-responsive element)/IRP (iron-regulatory protein) system, a well known post-transcriptional regulatory circuit that not only maintains iron homoeostasis in various cell types, but also contributes to systemic iron balance.

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IRPs regulate mRNAs of proteins required for iron utilization, uptake and export; DMT1 mRNA has an IRE in its 3' UTR and is upregulated by iron deficiency, while erythroid 5-aminolevulanata synthase and FPN1 have IREs in their 5' UTR and are upregulated under high iron conditions.
“IRPs, in addition to modulating ferritin and TfR1 levels can regulate the mRNAs or other proteins required for iron utilization (erythroid 5-aminolevulanata synthase), iron uptake (DMT1) and export (FPN1).DMT1 mRNA has IRE in its 3 ' UTR and is upregulated by iron deficiency while the other two proteins have IREs in their 5 ' UTR and are therefore upregulated under high iron conditions”
From Iron, Oxidative Stress and Health (2012) · cites this paper as Wang and Pantopoulos, 2011
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When iron concentration is high, IRPs are inactivated, resulting in degradation of TfR1 mRNA while translation of ferritin mRNA occurs, minimizing iron uptake and promoting storage.
“Conversely, when iron concentration is high, IRPs are inactivated resulting in degradation of TfR1 mRNA while translation of ferritin mRNA occurs.Thus when iron levels exceed the cellular needs, the IRE/IRP switch minimizes iron uptake and promotes iron storage”
From Iron, Oxidative Stress and Health (2012) · cites this paper as Wang and Pantopoulos, 2011
When iron is depleted, IRE-IRP interaction at the 3' UTR of TfR1 stabilizes mRNA and blocks ferritin mRNA translation, upregulating TfR1 and inhibiting ferritin synthesis.
“When iron is depleted, IRE-IRP interaction at the 3 ' UTR of TfR1 stabilizes mRNA, while imposing a steric blockade to ferritin mRNA translation.As a result, TfR1 is upregulated and stimulates acquisition of iron from plasma Tf to counteract low iron levels.Simultaneously ferritin synthesis is inhibited as storage of iron is not needed.”
From Iron, Oxidative Stress and Health (2012) · cites this paper as Wang and Pantopoulos, 2011
In erythroid progenitor cells, TfR1 stability is uncoupled from iron supply and TfR1 level is transcriptionally regulated by erythroid active element in its promoter region.
“However, in erythroid progenitor cells which require high amounts of iron for heme synthesis, TfR1 stability is uncoupled from iron supply and TfR1 level is transcriptionally regulated by erythroid active element in its promoter region (Wang and Pantopoulos, 2011).”
From Iron, Oxidative Stress and Health (2012) · cites this paper as Wang and Pantopoulos, 2011
Misregulation of iron homoeostasis can cause neurotoxicity through different mechanisms.
“Iron homoeostasis is needed to maintain normal physiological brain function, whereas misregulation of iron homoeostasis can cause neurotoxicity through different mechanisms.”
From The role of iron in brain ageing and neurodegenerative disorders (2014) · cites this paper as [3]

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Anemia of Chronic Disease
Weiss, G., & Goodnough, L. T. (2005) · New England Journal of Medicine · doi:10.1056/nejmra041809 · Cited by 3,800 · 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
Disorders of Iron Metabolism
Andrews, N. C. (1999) · New England Journal of Medicine · doi:10.1056/nejm199912233412607 · Cited by 2,130 · 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
Iron, brain ageing and neurodegenerative disorders
Zecca, L., Youdim, M. B. H., Riederer, P., Connor, J. R., & Crichton, R. R. (2004) · Nature Reviews Neuroscience · doi:10.1038/nrn1537 · Cited by 1,801 · see citing works
Identification of the haemoglobin scavenger receptor
Kristiansen, M., Graversen, J. H., Jacobsen, C., Sonne, O., Hoffman, H.-J., Law, S. K. A., & Moestrup, S. K. (2001) · Nature · doi:10.1038/35051594 · Cited by 1,712 · see citing works
Structure, function, and formation of biological iron-sulfur clusters
Johnson, D. C., Dean, D. R., Smith, A. D., & Johnson, M. K. (2005) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.74.082803.133518 · Cited by 1,438 · 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
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
A Novel Mammalian Iron-regulated Protein Involved in Intracellular Iron Metabolism
Abboud, S., & Haile, D. J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000713200 · Cited by 1,267 · see citing works
Regulation of ferritin genes and protein
Torti, F. M., & Torti, S. V. (2002) · Blood · doi:10.1182/blood.v99.10.3505 · Cited by 1,173 · see citing works
Function and biogenesis of iron-sulphur proteins
Lill, R. (2009) · Nature · doi:10.1038/nature08301 · Cited by 1,167 · 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
The role of iron regulatory proteins in mammalian iron homeostasis and disease
Rouault, T. A. (2006) · Nature Chemical Biology · doi:10.1038/nchembio807 · Cited by 1,055 · see citing works
Endocytic delivery of lipocalin-siderophore-iron complex rescues the kidney from ischemia-reperfusion injury
Mori, K., Lee, H. T., Rapoport, D., Drexler, I. R., Foster, K., Yang, J., Schmidt-Ott, K. M., Chen, X., Li, J. Y., Weiss, S., et al. (2005) · Journal of Clinical Investigation · doi:10.1172/jci23056 · Cited by 954 · 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
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
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
The heme synthesis and degradation pathways: role in oxidant sensitivity
Ryter, S. W., & Tyrrell, R. M. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00223-3 · Cited by 822 · see citing works
Chemistry and biology of eukaryotic iron metabolism
Aisen, P. (2001) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(01)00063-2 · Cited by 804 · 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
Systemic iron homeostasis and the iron-responsive element/iron-regulatory protein (IRE/IRP) regulatory network
Muckenthaler, M. U., Galy, B., & Hentze, M. W. (2008) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.28.061807.155521 · Cited by 701 · see citing works
Iron-Export Ferroxidase Activity of β-Amyloid Precursor Protein Is Inhibited by Zinc in Alzheimer's Disease
Duce, J. A., Tsatsanis, A., Cater, M. A., James, S., Robb, E. L., Wikhe, K., Leong, S. L., Perez, K. A., Johanssen, T., Greenough, M. A., et al. (2010) · Cell · doi:10.1016/j.cell.2010.08.014 · Cited by 682 · 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
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
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
Forging a field: the golden age of iron biology.
Andrews, N. C. (2008) · Blood · doi:10.1182/blood-2007-12-077388 · Cited by 623 · see citing works
Genetic or Pharmacological Iron Chelation Prevents MPTP-Induced Neurotoxicity In Vivo
Kaur, D., Yantiri, F., Rajagopalan, S., Kumar, J., Mo, J. Q., Boonplueang, R., Viswanath, V., Jacobs, R., Yang, L., Beal, M. F., et al. (2003) · Neuron · doi:10.1016/s0896-6273(03)00126-0 · Cited by 620 · 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
The Role of Hepcidin in Iron Metabolism
Nemeth, E., & Ganz, T. (2009) · Acta Haematologica · doi:10.1159/000243791 · Cited by 607 · see citing works
The transferrin receptor: role in health and disease
Ponka, P., & Lok, C. (1999) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(99)00070-9 · Cited by 598 · see citing works
Hypoxia-inducible factor-2 (HIF-2) regulates hepatic erythropoietin in vivo
Rankin, E. B., Biju, M. P., Liu, Q., Unger, T. L., Rha, J., Johnson, R. S., Simon, M. C., Keith, B., & Haase, V. H. (2007) · Journal of Clinical Investigation · doi:10.1172/jci30117 · Cited by 596 · see citing works
JunD Reduces Tumor Angiogenesis by Protecting Cells from Oxidative Stress
Gerald, D., Berra, E., Frapart, Y. M., Chan, D. A., Giaccia, A. J., Mansuy, D., Pouysségur, J., Yaniv, M., & Mechta-Grigoriou, F. (2004) · Cell · doi:10.1016/j.cell.2004.08.025 · Cited by 588 · 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
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
Binding and uptake of H-ferritin are mediated by human transferrin receptor-1
Li, L., Fang, C. J., Ryan, J. C., Niemi, E. C., Lebrón, J. A., Björkman, P. J., Arase, H., Torti, F. M., Torti, S. V., Nakamura, M. C., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0913192107 · Cited by 558 · 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
Iron behaving badly: inappropriate iron chelation as a major contributor to the aetiology of vascular and other progressive inflammatory and degenerative diseases
Kell, D. B. (2009) · BMC Medical Genomics · doi:10.1186/1755-8794-2-2 · Cited by 554 · see citing works
Tissue-Specific Regulation of Iron Metabolism and Heme Synthesis: Distinct Control Mechanisms in Erythroid Cells
Ponka, P. (1997) · Blood · doi:10.1182/blood.v89.1.1 · Cited by 544 · 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
Function and regulation of transferrin and ferritin.
Ponka, P., Beaumont, C., & Richardson, D. R. (1998) · PubMed · Cited by 524 · 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
Identification of the receptor scavenging hemopexin-heme complexes
Hvidberg, V., Maniecki, M. B., Jacobsen, C., Højrup, P., Møller, H. J., & Moestrup, S. K. (2005) · Blood · doi:10.1182/blood-2005-03-1185 · Cited by 473 · 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
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
Acute postnatal ablation of Hif-2 α results in anemia
Gruber, M., Hu, C.-J., Johnson, R. S., Brown, E. J., Keith, B., & Simon, M. C. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0608382104 · Cited by 457 · see citing works
Serum ferritin is derived primarily from macrophages through a nonclassical secretory pathway
Cohen, L. A., Gutierrez, L., Weiss, A., Leichtmann-Bardoogo, Y., Zhang, D.-L., Crooks, D. R., Sougrat, R., Morgenstern, A., Galy, B., Hentze, M. W., et al. (2010) · Blood · doi:10.1182/blood-2009-11-253815 · Cited by 452 · see citing works
Iron regulates phosphorylation of Smad1/5/8 and gene expression of Bmp6, Smad7, Id1, and Atoh8 in the mouse liver
Kautz, L., Meynard, D., Monnier, A., Darnaud, V., Bouvet, R., Wang, R.-H., Deng, C., Vaulont, S., Mosser, J., Coppin, H., et al. (2008) · Blood · doi:10.1182/blood-2008-03-143354 · Cited by 437 · 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
Previously uncharacterized isoforms of divalent metal transporter (DMT)-1: Implications for regulation and cellular function
Hubert, N., & Hentze, M. W. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.192423399 · Cited by 428 · 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
Nramp2 is mutated in the anemic Belgrade (b) rat : evidence of a role for Nramp2 in endosomal iron transport
Flemming (1998) · Medical Entomology and Zoology · Cited by 412 · 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
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
TLR4-dependent hepcidin expression by myeloid cells in response to bacterial pathogens
Peyssonnaux, C., Zinkernagel, A. S., Datta, V., Lauth, X., Johnson, R. S., & Nizet, V. (2006) · Blood · doi:10.1182/blood-2005-06-2259 · Cited by 379 · see citing works
Glycosylphosphatidylinositol-anchored ceruloplasmin is required for iron efflux from cells in the central nervous system
Jeong, S. Y., & David, S. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301988200 · Cited by 377 · see citing works
Deficiency of glutaredoxin 5 reveals Fe-S clusters are required for vertebrate haem synthesis.
The Tübingen 2000 Screen Consortium, Wingert, R. A., Galloway, J. L., Barut, B., Foott, H., Fraenkel, P., Axe, J. L., Weber, G. J., Dooley, K., Davidson, A. J., et al. (2005) · Nature · doi:10.1038/nature03887 · Cited by 370 · 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
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
Oxidative Stress and Iron Homeostasis: Mechanistic and Health Aspects
Galaris, D., & Pantopoulos, K. (2008) · Critical Reviews in Clinical Laboratory Sciences · doi:10.1080/10408360701713104 · Cited by 352 · see citing works
Self-citation
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
The endocytic receptor megalin binds the iron transporting neutrophil‐gelatinase‐associated lipocalin with high affinity and mediates its cellular uptake
Hvidberg, V., Jacobsen, C. B., Strong, R. K., Cowland, J. B., Moestrup, S. K., & Borregaard, N. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.12.031 · Cited by 351 · see citing works
Coordinated Regulation of Iron-Controlling Genes, H-Ferritin and IRP2 , by c-MYC
Wu, K., Polack, A., & Dalla‐Favera, R. (1999) · Science · doi:10.1126/science.283.5402.676 · Cited by 328 · see citing works
Interaction of the Hereditary Hemochromatosis Protein HFE with Transferrin Receptor 2 Is Required for Transferrin-Induced Hepcidin Expression
Gao, J., Chen, J., Kramer, M., Tsukamoto, H., Zhang, A.-S., & Enns, C. A. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.01.010 · Cited by 326 · see citing works
ER Stress Controls Iron Metabolism Through Induction of Hepcidin
Vecchi, C., Montosi, G., Zhang, K., Lamberti, I., Duncan, S. A., Kaufman, R. J., & Pietrangelo, A. (2009) · Science · doi:10.1126/science.1176639 · Cited by 310 · see citing works
Alcohol Metabolism-mediated Oxidative Stress Down-regulates Hepcidin Transcription and Leads to Increased Duodenal Iron Transporter Expression
Harrison-Findik, D. D., Schafer, D., Klein, E., Timchenko, N. A., Kulaksiz, H., Clemens, D. L., Fein, E., Andriopoulos, B., Pantopoulos, K., & Gollan, J. L. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602098200 · Cited by 308 · see citing works
Self-citation
The centennial of the Fenton reaction
Koppenol, W. H. (1993) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(93)90168-t · Cited by 302 · see citing works
Structure of Dual Function Iron Regulatory Protein 1 Complexed with Ferritin IRE-RNA
Walden, W. E., Selezneva, A. I., Dupuy, J., Volbeda, A., Fontecilla-Camps, J. C., Theil, E. C., & Volz, K. W. (2006) · Science · doi:10.1126/science.1133116 · Cited by 301 · 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
Iron-regulatory proteins limit hypoxia-inducible factor-2α expression in iron deficiency
Sanchez, M., Galy, B., Muckenthaler, M. U., & Hentze, M. W. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1222 · Cited by 294 · see citing works
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
Molecular control of vertebrate iron homeostasis by iron regulatory proteins
Wallander, M. L., Leibold, E. A., & Eisenstein, R. S. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.05.004 · 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
Early Embryonic Lethality of H Ferritin Gene Deletion in Mice
Ferreira, C., Bucchini, D., Martin, M.-E., Levi, S., Arosio, P., Grandchamp, B., & Beaumont, C. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.5.3021 · Cited by 275 · see citing works
Megalin-dependent cubilin-mediated endocytosis is a major pathway for the apical uptake of transferrin in polarized epithelia
Kozyraki, R., Fyfe, J. C., Verroust, P. J., Jacobsen, C. B., Dautry‐Varsat, A., Gburek, J., Willnow, T. E., Christensen, E., & Moestrup, S. K. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.211291398 · Cited by 271 · see citing works
Hepatitis C virus–induced oxidative stress suppresses hepcidin expression through increased histone deacetylase activity
Miura, K., Taura, K., Kodama, Y., Schnabl, B., & Brenner, D. A. (2008) · Hepatology · doi:10.1002/hep.22486 · Cited by 270 · 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
Mammalian Tissue Oxygen Levels Modulate Iron-Regulatory Protein Activities in Vivo
Meyron‐Holtz, E. G., Ghosh, M. C., & Rouault, T. A. (2004) · Science · doi:10.1126/science.1103786 · Cited by 246 · 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
Glutaredoxin 5 deficiency causes sideroblastic anemia by specifically impairing heme biosynthesis and depleting cytosolic iron in human erythroblasts
Ye, H., Jeong, S. Y., Ghosh, M. C., Kovtunovych, G., Silvestri, L., Ortillo, D., Uchida, N., Tisdale, J. F., Camaschella, C., & Rouault, T. A. (2010) · Journal of Clinical Investigation · doi:10.1172/jci40372 · Cited by 239 · see citing works
Erythropoietin mediates hepcidin expression in hepatocytes through EPOR signaling and regulation of C/EBPα
Pinto, J. P., Ribeiro, S., Pontes, H., Thowfeequ, S., Tosh, D., Carvalho, F. D., & Porto, G. (2008) · Blood · doi:10.1182/blood-2007-08-106195 · Cited by 239 · see citing works
Human Iron−Sulfur Cluster Assembly, Cellular Iron Homeostasis, and Disease
Ye, H., & Rouault, T. A. (2010) · Biochemistry · doi:10.1021/bi1004798 · 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
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
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
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
Friedreich ataxia: the oxidative stress paradox
Seznec, H., Simon, D., Bouton, C., Reutenauer, L., Hertzog, A., Golik, P., Procaccio, V., Patel, M., Drapier, J.-C., Koenig, M., et al. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi042 · 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
Trafficking of Heme and Porphyrins in Metazoa
Severance, S., & Hamza, I. (2009) · Chemical Reviews · doi:10.1021/cr9001116 · 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
Managed care for viruses
Crystal, R. G. (1997) · Nature Medicine · doi:10.1038/nm0497-383 · Cited by 205 · see citing works
Mitochondrial ferritin expression in erythroid cells from patients with sideroblastic anemia
Cazzola, M., Invernizzi, R., Bergamaschi, G., Levi, S., Corsi, B., Travaglino, E., Rolandi, V., Biasiotto, G., Drysdale, J., & Arosio, P. (2003) · Blood · doi:10.1182/blood-2002-07-2006 · Cited by 205 · 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
Small-molecule inhibitors of HIF-2a translation link its 5'UTR iron-responsive element to oxygen sensing
Zimmer, M., Ebert, B. L., Neil, C., Brenner, K., Papaioannou, I., Melas, A., Tolliday, N., Lamb, J., Pantopoulos, K., Golub, T., et al. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.12.004 · Cited by 191 · see citing works
Self-citation
Tah18 transfers electrons to Dre2 in cytosolic iron-sulfur protein biogenesis
Netz, D. J. A., Stümpfig, M., Doré, C., Mühlenhoff, U., Pierik, A. J., & Lill, R. (2010) · Nature Chemical Biology · doi:10.1038/nchembio.432 · Cited by 189 · see citing works
Selective Translational Control of the Alzheimer Amyloid Precursor Protein Transcript by Iron Regulatory Protein-1
Cho, H.-H., Cahill, C. M., Vanderburg, C. R., Scherzer, C. R., Wang, B., Huang, X., & Rogers, J. T. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.149161 · Cited by 188 · see citing works
The molecular defect in hypotransferrinemic mice
Trenor, C. C., Campagna, D. R., Sellers, V. M., Andrews, N. C., & Fleming, M. D. (2000) · Blood · doi:10.1182/blood.v96.3.1113 · Cited by 187 · see citing works
The 5′-untranslated region of Parkinson's disease α-synuclein messengerRNA contains a predicted iron responsive element
Friedlich, A. L., Tanzi, R. E., & Rogers, J. T. (2007) · Molecular Psychiatry · doi:10.1038/sj.mp.4001937 · Cited by 181 · 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
Iron–sulfur protein maturation in human cells: evidence for a function of frataxin
Stehling, O., Elsässer, H.-P., Brückel, B., Mühlenhoff, U., & Lill, R. (2004) · Human Molecular Genetics · doi:10.1093/hmg/ddh324 · Cited by 176 · see citing works
Intracellular labile iron
Breuer, W., Shvartsman, M., & Cabantchik, Z. I. (2008) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2007.03.010 · Cited by 175 · see citing works
The Cfd1–Nbp35 complex acts as a scaffold for iron-sulfur protein assembly in the yeast cytosol
Netz, D. J. A., Pierik, A. J., Stümpfig, M., Mühlenhoff, U., & Lill, R. (2007) · Nature Chemical Biology · doi:10.1038/nchembio872 · Cited by 174 · see citing works
Regulation of Hepcidin and Iron-Overload Disease
Lee, P. L., & Beutler, E. (2009) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev.pathol.4.110807.092205 · Cited by 174 · 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
Nramp1 promotes efficient macrophage recycling of iron following erythrophagocytosis in vivo
Soe-Lin, S., Apte, S. S., Andriopoulos, B., Andrews, M. C., Schranzhofer, M., Kahawita, T., Garcia-Santos, D., & Ponka, P. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0900808106 · Cited by 167 · see citing works
ZRT/IRT-like Protein 14 (ZIP14) Promotes the Cellular Assimilation of Iron from Transferrin
Zhao, N., Gao, J., Enns, C. A., & Knutson, M. D. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.143248 · Cited by 166 · see citing works
Role of human mitochondrial Nfs1 in cytosolic iron-sulfur protein biogenesis and iron regulation
Biederbick, A., Stehling, O., Rösser, R., Niggemeyer, B., Nakai, Y., Elsässer, H.-P., & Lill, R. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00112-06 · Cited by 164 · see citing works
A novel eukaryotic factor for cytosolic Fe–S cluster assembly
Roy, A., Solodovnikova, N., Nicholson, T., Antholine, W. E., & Walden, W. E. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg455 · Cited by 160 · see citing works
Bacillus subtilis aconitase is an RNA-binding protein
Amaro, C. A., & Sonenshein, A. L. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.18.10412 · Cited by 159 · see citing works
Metabolic regulation of citrate and iron by aconitases: role of iron–sulfur cluster biogenesis
Tong, W.-H., & Rouault, T. A. (2007) · BioMetals · doi:10.1007/s10534-006-9047-6 · Cited by 158 · see citing works
Direct evidence for mRNA binding and post-transcriptional regulation by Escherichia coli aconitases
Tang, Y., & Guest, J. R. (1999) · Microbiology · doi:10.1099/00221287-145-11-3069 · Cited by 158 · see citing works
Human ISD11 is essential for both iron-sulfur cluster assembly and maintenance of normal cellular iron homeostasis
Shi, Y., Ghosh, M. C., Tong, W.-H., & Rouault, T. A. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp239 · Cited by 155 · see citing works
Dre2, a Conserved Eukaryotic Fe/S Cluster Protein, Functions in Cytosolic Fe/S Protein Biogenesis
Zhang, Y., Lyver, E. R., Nakamaru‐Ogiso, E., Yoon, H., Amutha, B., Lee, D., Bi, E., Ohnishi, T., Daldal, F., Pain, D., et al. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.00642-08 · Cited by 148 · 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
Crystal Structure of Human Iron Regulatory Protein 1 as Cytosolic Aconitase
Dupuy, J., Volbeda, A., Carpentier, P., Darnault, C., Moulis, J., & Fontecilla-Camps, J. C. (2006) · Structure · doi:10.1016/j.str.2005.09.009 · Cited by 145 · see citing works
The aconitase family: three structural variations on a common theme
Gruer, M. J., Artymiuk, P. J., & Guest, J. R. (1997) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(96)10069-4 · Cited by 144 · see citing works
Oxygen and Iron Regulation of Iron Regulatory Protein 2
Hanson, E. S., Rawlins, M. L., & Leibold, E. A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302798200 · Cited by 140 · see citing works
Nature of nontransferrin‐bound iron
Hider, R. C. (2002) · European Journal of Clinical Investigation · doi:10.1046/j.1365-2362.2002.0320s1050.x · Cited by 139 · 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
Localized Unfolding at the Junction of Three Ferritin Subunits
Takagi, H., Shi, D., Ha, Y., Allewell, N. M., & Theil, E. C. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.30.18685 · Cited by 130 · see citing works
The Essential WD40 Protein Cia1 Is Involved in a Late Step of Cytosolic and Nuclear Iron-Sulfur Protein Assembly
Balk, J., Netz, D. J. A., Tepper, K., Pierik, A. J., & Lill, R. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.24.10833-10841.2005 · Cited by 129 · see citing works
Nitrogen monoxide (NO)-mediated iron release from cells is linked to NO-induced glutathione efflux via multidrug resistance-associated protein 1
Watts, R., Hawkins, C. L., Ponka, P., & Richardson, D. R. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0602515103 · Cited by 128 · see citing works
Iron Regulatory Proteins: From Molecular Mechanisms to Drug Development
Recalcati, S., Minotti, G., & Cairo, G. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2983 · Cited by 123 · see citing works
Complete loss of iron regulatory proteins 1 and 2 prevents viability of murine zygotes beyond the blastocyst stage of embryonic development
Smith, S., Ghosh, M. C., Ollivierre, H., Tong, W. H., & Rouault, T. A. (2006) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2005.12.006 · Cited by 123 · see citing works
Brain iron homeostasis, the choroid plexus, and localization of iron transport proteins
Rouault, T. A., Zhang, D., & Jeong, S. Y. (2009) · Metabolic Brain Disease · doi:10.1007/s11011-009-9169-y · Cited by 123 · see citing works
ROS mediate the hypoxic repression of the hepcidin gene by inhibiting C/EBPα and STAT-3
Choi, S.-O., Cho, Y.-S., Kim, H.-L., & Park, J.-W. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.02.137 · Cited by 122 · 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
Assessment of Chelatable Mitochondrial Iron by Using Mitochondrion‐Selective Fluorescent Iron Indicators with Different Iron‐Binding Affinities
Rauen, U., Springer, A., Weisheit, D., Petrat, F., Korth, H., de Groot, H., & Sustmann, R. (2007) · ChemBioChem · doi:10.1002/cbic.200600311 · Cited by 121 · 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
Mitochondrial ferritin
Levi, S., & Arosio, P. (2004) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2003.10.020 · Cited by 120 · see citing works
Iron-Refractory Iron Deficiency Anemia
Finberg, K. E. (2009) · Seminars in Hematology · doi:10.1053/j.seminhematol.2009.06.006 · Cited by 119 · see citing works
Modulation of Cellular Iron Metabolism by Hydrogen Peroxide
Caltagirone, A., Weiß, G., & Pantopoulos, K. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100245200 · Cited by 118 · see citing works
Self-citation
Iron-Mediated Degradation of IRP2, an Unexpected Pathway Involving a 2-Oxoglutarate-Dependent Oxygenase Activity
Wang, J., Chen, G., Muckenthaler, M. U., Galy, B., Hentze, M. W., & Pantopoulos, K. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.3.954-965.2004 · Cited by 116 · see citing works
Self-citation
Iron Regulation and the Cell Cycle
Sánchez, M., Galy, B., Dandekar, T., Bengert, P., Vainshtein, Y., Stolte, J., Muckenthaler, M. U., & Hentze, M. W. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603876200 · Cited by 112 · see citing works
Human Nbp35 Is Essential for both Cytosolic Iron-Sulfur Protein Assembly and Iron Homeostasis
Stehling, O., Netz, D. J. A., Niggemeyer, B., Rösser, R., Eisenstein, R. S., Puccio, H. M., Pierik, A. J., & Lill, R. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.00545-08 · Cited by 107 · see citing works
Diversity and distribution of hemerythrin-like proteins in prokaryotes
French, C. E., Bell, J. M., & Ward, F. B. (2008) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2007.01011.x · Cited by 102 · see citing works
ER Stress-Inducible Factor CHOP Affects the Expression of Hepcidin by Modulating C/EBPalpha Activity
Oliveira, S. J., Pinto, J. P., Picarote, G., Costa, V. M., Carvalho, F. D., Rangel, M., de Sousa, M. A. B., & de Almeida, S. F. (2009) · PLoS ONE · doi:10.1371/journal.pone.0006618 · Cited by 101 · see citing works
Myeloperoxidase-derived Hypochlorous Acid Antagonizes the Oxidative Stress-mediated Activation of Iron Regulatory Protein 1
Mütze, S., Hebling, U., Stremmel, W., Wang, J., Arnhold, J., Pantopoulos, K., & Mueller, S. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m307159200 · Cited by 101 · see citing works
Self-citation
Roles of the Mammalian Cytosolic Cysteine Desulfurase, ISCS, and Scaffold Protein, ISCU, in Iron-Sulfur Cluster Assembly
Li, K., Tong, W.-H., Hughes, R. M., & Rouault, T. A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600582200 · Cited by 97 · 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
Severity of Neurodegeneration Correlates with Compromise of Iron Metabolism in Mice with Iron Regulatory Protein Deficiencies
Smith, S., Cooperman, S. S., LaVaute, T. M., Tresser, N. J., Ghosh, M. C., Meyron‐Holtz, E. G., Land, W., Ollivierre, H., Jortner, B. S., Switzer, R., et al. (2004) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1306.006 · Cited by 94 · 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
Tempol-mediated activation of latent iron regulatory protein activity prevents symptoms of neurodegenerative disease in IRP2 knockout mice
Ghosh, M. C., Tong, W.-H., Zhang, D., Ollivierre, H., Singh, A., Krishna, M. C., Mitchell, J. B., & Rouault, T. A. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0805361105 · 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
S-Nitrosylation of IRP2 Regulates Its Stability via the Ubiquitin-Proteasome Pathway
Kim, S.-W., Wing, S. S., & Ponka, P. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.24.1.330-337.2004 · Cited by 87 · see citing works
Conditional deletion of ferritin H in mice induces loss of iron storage and liver damage #
Darshan, D., Vanoaica, L., Richman, L., Beermann, F., & Kühn, L. C. (2009) · Hepatology · doi:10.1002/hep.23058 · Cited by 86 · see citing works
Neuroferritinopathy: a neurodegenerative disorder associated with L-ferritin mutation
Levi, S., Cozzi, A., & Arosio, P. (2005) · Best Practice & Research Clinical Haematology · doi:10.1016/j.beha.2004.08.021 · Cited by 84 · see citing works
Oxidation-induced ferritin turnover in microglial cells: role of proteasome
Mehlhase, J., Sandig, G., Pantopoulos, K., & Grune, T. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.10.025 · Cited by 84 · see citing works
Self-citation
Iron feeding induces ferroportin 1 and hephaestin migration and interaction in rat duodenal epithelium
Yeh, K., YEH, M. K. Y., Mims, L., & Glass, J. (2008) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.90298.2008 · Cited by 84 · see citing works
Iron transport and the kidney
Smith, C. P., & Thévenod, F. (2008) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2008.10.010 · Cited by 80 · see citing works
A Role for IOP1 in Mammalian Cytosolic Iron-Sulfur Protein Biogenesis
Song, D., & Lee, F. S. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m708077200 · Cited by 76 · see citing works
Disruption of ferroportin 1 regulation causes dynamic alterations in iron homeostasis and erythropoiesis in polycythaemia mice
Mok, H., Jelinek, J., Pai, S., Cattanach, B. M., Prchal, J. T., Youssoufian, H., & Schumacher, A. (2004) · Development · doi:10.1242/dev.01081 · Cited by 73 · 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
Tumorigenic Properties of Iron Regulatory Protein 2 (IRP2) Mediated by Its Specific 73-Amino Acids Insert
Maffettone, C., Chen, G., Drozdov, I. A., Ouzounis, C. A., & Pantopoulos, K. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010163 · Cited by 68 · see citing works
Self-citation
A novel iron responsive element in the 3′UTR of human MRCKα
Čmejla, R., Petrák, J., & Čmejlová, J. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.12.155 · Cited by 68 · see citing works
Hypoxic up-regulation of erythroid 5-aminolevulinate synthase
Höfer, T., Wenger, R. H., Kramer, M. F., Ferreira, G. C., & Gassmann, M. (2002) · Blood · doi:10.1182/blood-2002-03-0773 · Cited by 65 · see citing works
Iron homeostasis in the brain: complete iron regulatory protein 2 deficiency without symptomatic neurodegeneration in the mouse
Galy, B., Hölter, S. M., Klopstock, T., Ferring–Appel, D., Becker, L., Kaden, S., Wurst, W., Gröne, H., & Hentze, M. W. (2006) · Nature Genetics · doi:10.1038/ng0906-967 · Cited by 62 · see citing works
Iron-Induced Expression of Bone Morphogenic Protein 6 in Intestinal Cells Is the Main Regulator of Hepatic Hepcidin Expression In Vivo
Arndt, S., Maegdefrau, U., Dorn, C., Schardt, K., Hellerbrand, C., & Bosserhoff, A. (2009) · Gastroenterology · doi:10.1053/j.gastro.2009.09.048 · Cited by 60 · see citing works
Identification of an Erythroid Active Element in the Transferrin Receptor Gene
Lok, C., & Ponka, P. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000944200 · Cited by 57 · see citing works
Overexpression of iron regulatory protein 1 suppresses growth of tumor xenografts
Chen, G., Fillebeen, C., Wang, J., & Pantopoulos, K. (2006) · Carcinogenesis · doi:10.1093/carcin/bgl210 · Cited by 55 · see citing works
Self-citation
Iron and inflammation: cross-talk between pathways regulating hepcidin
Fleming, R. E. (2008) · Journal of Molecular Medicine · doi:10.1007/s00109-008-0349-8 · Cited by 54 · see citing works
RNA Silencing of Mitochondrial m-Nfs1 Reduces Fe-S Enzyme Activity Both in Mitochondria and Cytosol of Mammalian Cells
Fosset, C., Chauveau, M.-J., Guillon, B., Canal, F., Drapier, J., & Bouton, C. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602979200 · Cited by 53 · see citing works
Cell-autonomous and systemic context-dependent functions of iron regulatory protein 2 in mammalian iron metabolism
Ferring–Appel, D., Hentze, M. W., & Galy, B. (2008) · Blood · doi:10.1182/blood-2008-05-155093 · Cited by 53 · see citing works
Cysteine Oxidation Regulates the RNA-Binding Activity of Iron Regulatory Protein 2
由幸, 松., 直人, 篠., Romney, S. J., & Leibold, E. A. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00004-09 · Cited by 51 · see citing works
The role of endogenous heme synthesis and degradation domain cysteines in cellular iron-dependent degradation of IRP2
Bourdon, E., Kang, D., Ghosh, M. C., Drake, S. K., Wey, J. S., Levine, R. L., & Rouault, T. A. (2003) · Blood Cells Molecules and Diseases · doi:10.1016/s1079-9796(03)00161-x · Cited by 51 · see citing works
Conditional Derepression of Ferritin Synthesis in Cells Expressing a Constitutive IRP1 Mutant
Wang, J., & Pantopoulos, K. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.13.4638-4651.2002 · Cited by 49 · see citing works
Self-citation
Chronic expression of H-ferritin in dopaminergic midbrain neurons results in an age-related expansion of the labile iron pool and subsequent neurodegeneration: implications for Parkinson's disease
Kaur, D., Rajagopalan, S., & Andersen, J. K. (2009) · Brain Research · doi:10.1016/j.brainres.2009.08.043 · Cited by 48 · see citing works
Sustained Hydrogen Peroxide Induces Iron Uptake by Transferrin Receptor-1 Independent of the Iron Regulatory Protein/Iron-responsive Element Network
Andriopoulos, B., Hegedüsch, S., Mangin, J., Riedel, H.-D., Hebling, U., Wang, J., Pantopoulos, K., & Mueller, S. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702463200 · Cited by 48 · see citing works
Self-citation
A Phosphomimetic Mutation at Ser-138 Renders Iron Regulatory Protein 1 Sensitive to Iron-Dependent Degradation
Fillebeen, C., Chahine, D., Caltagirone, A., Segal, P., & Pantopoulos, K. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.19.6973-6981.2003 · Cited by 48 · see citing works
Self-citation
Redox control of iron regulatory proteins
Fillebeen, C., & Pantopoulos, K. (2002) · Redox Report · doi:10.1179/135100002125000136 · Cited by 44 · see citing works
Self-citation
Recycling of RNA Binding Iron Regulatory Protein 1 into an Aconitase after Nitric Oxide Removal Depends on Mitochondrial ATP
Bouton, C., Chauveau, M.-J., Lazereg, S., & Drapier, J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203276200 · Cited by 44 · see citing works
Pathogenesis of Hyperferritinemia Cataract Syndrome
Roetto, A., Bosio, S., Gramaglia, E., Barilaro, M. R., Zecchina, G., & Camaschella, C. (2002) · Blood Cells Molecules and Diseases · doi:10.1006/bcmd.2002.0590 · Cited by 41 · see citing works
The Connectivity Map Links Iron Regulatory Protein-1–Mediated Inhibition of Hypoxia-Inducible Factor-2a Translation to the Anti-inflammatory 15-deoxy-Δ12,14-Prostaglandin J2
Zimmer, M., Lamb, J., Ebert, B. L., Lynch, M. C., Neil, C. R., Schmidt, E. V., Golub, T. R., & Iliopoulos, O. (2010) · Cancer Research · doi:10.1158/0008-5472.can-09-2877 · Cited by 40 · see citing works
Maintaining Mammalian Iron and Oxygen Homeostasis
Salahudeen, A. A., & Bruick, R. K. (2009) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2009.05038.x · Cited by 40 · see citing works
Activated macrophages induce hepcidin expression in HuH7 hepatoma cells
Matak, P., Chaston, T. B., Chung, B., Srai, S. K., McKie, A. T., & Sharp, P. (2009) · Haematologica · doi:10.3324/haematol.2008.003400 · Cited by 40 · see citing works
Nitric Oxide Inhibits the Degradation of IRP2
Wang, J., Chen, G., & Pantopoulos, K. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.4.1347-1353.2005 · Cited by 38 · see citing works
Self-citation
Sodium Nitroprusside Promotes IRP2 Degradation via an Increase in Intracellular Iron and in the Absence of S Nitrosylation at C178
Wang, J., Fillebeen, C., Chen, G., Andriopoulos, B., & Pantopoulos, K. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.5.1948-1954.2006 · Cited by 34 · see citing works
Self-citation
Evidence That Phosphorylation of Iron Regulatory Protein 1 at Serine 138 Destabilizes the [4Fe-4S] Cluster in Cytosolic Aconitase by Enhancing 4Fe-3Fe Cycling
Deck, K. M., Vasanthakumar, A., Anderson, S. A., Goforth, J. B., Kennedy, M. C., Antholine, W. E., & Eisenstein, R. S. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m807717200 · Cited by 33 · see citing works
Toll-like receptors mediate induction of hepcidin in mice infected with Borrelia burgdorferi
Koening, C. L., Miller, J. C., Nelson, J. M., Ward, D. M., Kushner, J. P., Bockenstedt, L. K., Weis, J. J., Kaplan, J., & Domenico, I. D. (2009) · Blood · doi:10.1182/blood-2009-03-209577 · Cited by 32 · see citing works
IRP1-independent alterations of cardiac iron metabolism in doxorubicin-treated mice
Corna, G., Galy, B., Hentze, M. W., & Cairo, G. (2006) · Journal of Molecular Medicine · doi:10.1007/s00109-006-0068-y · Cited by 31 · see citing works
IRP1 Ser-711 is a phosphorylation site, critical for regulation of RNA-binding and aconitase activities
Fillebeen, C., Caltagirone, A., Martelli, A., Moulis, J., & Pantopoulos, K. (2005) · Biochemical Journal · doi:10.1042/bj20041623 · Cited by 30 · see citing works
Self-citation
Selective inhibition of the citrate-to-isocitrate reaction of cytosolic aconitase by phosphomimetic mutation of serine-711
Pitula, J. S., Deck, K. M., Clarke, S. L., Anderson, S. A., Vasanthakumar, A., & Eisenstein, R. S. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0404308101 · Cited by 30 · see citing works
Redox control of iron regulatory protein 2 stability
Hausmann, A., Lee, J., & Pantopoulos, K. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.01.036 · Cited by 29 · see citing works
Self-citation
Systematic genomic screening and analysis of mRNA in untranslated regions and mRNA precursors: combining experimental and computational approaches.
Dandekar, T., Beyer, K., Peer Bork, B., et al. (1998) · Bioinformatics · doi:10.1093/bioinformatics/14.3.271 · Cited by 26 · see citing works
Human iron regulatory protein 2 is easily cleaved in its specific domain: consequences for the haem binding properties of the protein
Dycke, C., Bougault, C., Gaillard, J., Andrieu, J., Pantopoulos, K., & Moulis, J. (2007) · Biochemical Journal · doi:10.1042/bj20070983 · Cited by 24 · see citing works
Self-citation
Subcellular localization of iron regulatory proteins to Golgi and ER membranes
Patton, S. M., Piñero, D. J., Surguladze, N., Beard, J., & Connor, J. R. (2005) · Journal of Cell Science · doi:10.1242/jcs.02570 · Cited by 23 · see citing works
Iron-independent Phosphorylation of Iron Regulatory Protein 2 Regulates Ferritin during the Cell Cycle
Wallander, M. L., Zumbrennen‐Bullough, K. B., Rodansky, E. S., Romney, S. J., & Leibold, E. A. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803005200 · Cited by 22 · see citing works

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Reactive oxygen species (ROS) homeostasis and redox regulation in cellular signaling
Ray, P. D., Huang, B.-W., & Tsuji, Y. (2012) · Cellular Signalling · doi:10.1016/j.cellsig.2012.01.008 · Cited by 4,373 · see citing works
The role of iron in brain ageing and neurodegenerative disorders
Ward, R. J., Zucca, F. A., Duyn, J. H., Crichton, R. R., & Zecca, L. (2014) · The Lancet Neurology · doi:10.1016/s1474-4422(14)70117-6 · Cited by 1,819 · see citing works
Mechanisms of mammalian iron homeostasis
Pantopoulos, K., Porwal, S. K., Tartakoff, A., & Devireddy, L. (2012) · Biochemistry · doi:10.1021/bi300752r · Cited by 598 · see citing works
Self-citation
Iron and cancer: recent insights
Manz, D. H., Blanchette, N. L., Paul, B. T., Torti, F. M., & Torti, S. V. (2016) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.13008 · Cited by 507 · see citing works
“Cells use this iron pool for (1) incorporation into prosthetic groups of iron-dependent enzymes and proteins, (2) incorporation into heme (after transport across the mitochondrial membrane) and iron–sulfur cluster biogenesis, and (3) storage in ferritin.”
Background
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
Mammalian iron metabolism and its control by iron regulatory proteins
Anderson, C. P., Shen, M., Eisenstein, R. S., & Leibold, E. A. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.05.010 · Cited by 493 · see citing works
Iron deficiency across chronic inflammatory conditions: International expert opinion on definition, diagnosis, and management
Cappellini, M. D., Comin‐Colet, J., de Francisco, A., Dignass, A., Doehner, W., Lam, C. S., Macdougall, I. C., Rogler, G., Camaschella, C., Kadir, R., et al. (2017) · American Journal of Hematology · doi:10.1002/ajh.24820 · Cited by 502 · see citing works
Iron deficiency and heart failure: diagnostic dilemmas and therapeutic perspectives
Jankowska, E. A., von Haehling, S., Anker, S. D., Macdougall, I. C., & Ponikowski, P. (2013) · European Heart Journal · doi:10.1093/eurheartj/ehs224 · Cited by 399 · see citing works
The IRP/IRE system in vivo: insights from mouse models
Wilkinson, N., & Pantopoulos, K. (2014) · Frontiers in Pharmacology · doi:10.3389/fphar.2014.00176 · Cited by 366 · see citing works
Self-citation
Gut Microbiota and Iron: The Crucial Actors in Health and Disease
Yilmaz, B., & Li, H. (2018) · Pharmaceuticals · doi:10.3390/ph11040098 · Cited by 317 · see citing works
Shared and distinct mechanisms of iron acquisition by bacterial and fungal pathogens of humans
Caza, M., & Kronstad, J. W. (2013) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2013.00080 · Cited by 306 · see citing works
Iron metabolism and the innate immune response to infection
Johnson, E. E., & Wessling-Resnick, M. (2012) · Microbes and Infection · doi:10.1016/j.micinf.2011.10.001 · Cited by 253 · see citing works
“This mechanism delivers iron to peripheral tissues for metabolic purposes [4].”
Background
Intestinal iron absorption
Fuqua, B. K., Vulpe, C. D., & Anderson, G. J. (2012) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2012.03.015 · Cited by 241 · see citing works
Iron-sulfur cluster deficiency can be sensed by IRP2 and regulates iron homeostasis and sensitivity to ferroptosis independent of IRP1 and FBXL5
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 · see citing works
mTOR 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 · 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
Mitochondrial death effectors: Relevance to sarcopenia and disuse muscle atrophy
Marzetti, E., Hwang, J. C. Y., Lees, H. A., Wohlgemuth, S. E., Dupont-Versteegden, E. E., Carter, C. S., Bernabei, R., & Leeuwenburgh, C. (2010) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2009.05.007 · Cited by 174 · see citing works
The role of vitamin D in regulating the iron-hepcidin-ferroportin axis in monocytes
Zughaier, S. M., Alvarez, J. A., Sloan, J. H., Konrad, R. J., & Tangpricha, V. (2014) · Journal of Clinical & Translational Endocrinology · doi:10.1016/j.jcte.2014.01.003 · Cited by 174 · see citing works
Trace elements as an activator of antioxidant enzymes
Wołonciej, M., Milewska, E., & Roszkowska-Jakimiec, W. (2016) · Postępy Higieny i Medycyny Doświadczalnej · doi:10.5604/17322693.1229074 · Cited by 171 · see citing works
Physiological roles of ovotransferrin
Giansanti, F., Leboffe, L., Pitari, G., Ippoliti, R., & Antonini, G. (2012) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2011.08.004 · Cited by 145 · see citing works
Systemic Analysis of Atg5-Null Mice Rescued from Neonatal Lethality by Transgenic ATG5 Expression in Neurons
Yoshii, S. R., Kuma, A., Akashi, T., Hara, T., Yamamoto, A., Kurikawa, Y., Itakura, E., Tsukamoto, S., Shitara, H., Eishi, Y., et al. (2016) · Developmental Cell · doi:10.1016/j.devcel.2016.09.001 · Cited by 127 · see citing works
High-fat diet causes iron deficiency via hepcidin-independent reduction of duodenal iron absorption
Sonnweber, T., Ress, C., Nairz, M., Theurl, I., Schroll, A., Murphy, A. T., Wroblewski, V., Witcher, D. R., Moser, P., Ebenbichler, C. F., et al. (2012) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2011.10.013 · Cited by 117 · see citing works
Why cells need iron: a compendium of iron utilisation
Teh, M. R., Armitage, A. E., & Drakesmith, H. (2024) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2024.04.015 · Cited by 114 · see citing works
Targeting multidrug resistance-associated protein 1 (MRP1)-expressing cancers: Beyond pharmacological inhibition
Hanssen, K. M., Haber, M., & Fletcher, J. I. (2021) · Drug Resistance Updates · doi:10.1016/j.drup.2021.100795 · Cited by 102 · see citing works
Impaired iron status in aging research
Xu, J., Jia, Z., Knutson, M. D., & Leeuwenburgh, C. (2012) · International Journal of Molecular Sciences · doi:10.3390/ijms13022368 · Cited by 103 · see citing works
2-Oxoglutarate-dependent dioxygenases are sensors of energy metabolism, oxygen availability, and iron homeostasis: potential role in the regulation of aging process
Salminen, A., Kauppinen, A., & Kaarniranta, K. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-1978-z · Cited by 99 · see citing works
RNA sequencing and proteomics approaches reveal novel deficits in the cortex of Mecp2-deficient mice, a model for Rett syndrome
Pacheco, N. L., Heaven, M. R., Holt, L. M., Crossman, D. K., Boggio, K. J., Shaffer, S. A., Flint, D. L., & Olsen, M. L. (2017) · Molecular Autism · doi:10.1186/s13229-017-0174-4 · Cited by 90 · see citing works
Iron Deposition Leads to Hyperphosphorylation of Tau and Disruption of Insulin Signaling
Wan, W., Cao, L., Kalionis, B., Murthi, P., Xia, S., & Guan, Y. (2019) · Frontiers in Neurology · doi:10.3389/fneur.2019.00607 · Cited by 84 · see citing works
A delicate balance between bacterial iron and reactive oxygen species supports optimal C. elegans development
Zhang, J., Li, X., Olmedo, M., Holdorf, A. D., Shang, Y., Artal-Sanz, M., Yilmaz, L. S., & Walhout, A. J. M. (2019) · Cell Host & Microbe · doi:10.1016/j.chom.2019.07.010 · Cited by 77 · 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
Fluorescent 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 · see citing works
Nitric Oxide Suppresses Tumor Cell Migration through N-Myc Downstream-regulated Gene-1 (NDRG1) Expression
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 · see citing works
Host iron redistribution as a risk factor for incident tuberculosis in HIV infection: an 11-year retrospective cohort study
McDermid, J. M., Hennig, B. J., van der Sande, M., Hill, A. V., Whittle, H. C., Jaye, A., & Prentice, A. M. (2013) · BMC Infectious Diseases · doi:10.1186/1471-2334-13-48 · Cited by 75 · see citing works
Lipocalin 2 Bolsters Innate and Adaptive Immune Responses to Blood-Stage Malaria Infection by Reinforcing Host Iron Metabolism
Zhao, H., Konishi, A., Fujita, Y., Yagi, M., Ohata, K., Aoshi, T., Itagaki, S., Sato, S., Narita, H., Abdelgelil, N. H., et al. (2012) · Cell Host & Microbe · doi:10.1016/j.chom.2012.10.010 · Cited by 65 · see citing works
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 · see citing works
Neisseria gonorrhoeae modulates iron-limiting innate immune defenses in macrophages
Zughaier, S. M., Kandler, J. L., & Shafer, W. M. (2014) · PLoS ONE · doi:10.1371/journal.pone.0087688 · Cited by 59 · see citing works
Interleukin-6 triggers toxic neuronal iron sequestration in response to pathological α-synuclein
Sterling, J. K., Kam, T.-I., Guttha, S., Park, H., Baumann, B., Mehrabani-Tabari, A. A., Schultz, H., Anderson, B., Alnemri, A., Chou, S.-C., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.110358 · Cited by 58 · see citing works
Conditional deletion of ferritin H in mice reduces B and T lymphocyte populations
Vanoaica, L., Richman, L., Jaworski, M., Darshan, D., Luther, S. A., & Kühn, L. C. (2014) · PLoS ONE · doi:10.1371/journal.pone.0089270 · Cited by 56 · see citing works
Nramp
(2012) · Current Topics in Membranes · doi:10.1016/b978-0-12-394390-3.00010-0 · Cited by 47 · see citing works
Unraveling the Burden of Iron in Neurodegeneration: Intersections with Amyloid Beta Peptide Pathology
Uranga, R. M., & Salvador, G. A. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/2850341 · Cited by 48 · 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
Iron alters cell survival in a mitochondria-dependent pathway in ovarian cancer cells
Bauckman, K., Haller, E., Taran, N., Rockfield, S., Ruiz-Rivera, A., & Nanjundan, M. (2015) · Biochemical Journal · doi:10.1042/bj20140878 · Cited by 41 · see citing works
Inflammation and ER stress downregulate BDH2 expression and dysregulate intracellular iron in macrophages
Zughaier, S. M., Stauffer, B. B., & McCarty, N. A. (2014) · Journal of Immunology Research · doi:10.1155/2014/140728 · Cited by 34 · 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
The phosphoinositide 3-kinase regulates retrograde trafficking of the iron permease CgFtr1 and iron homeostasis in Candida glabrata
Sharma, V., Purushotham, R., & Kaur, R. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.751529 · Cited by 22 · see citing works
Alternative ferritin mRNA translation via internal initiation
Daba, A., Koromilas, A. E., & Pantopoulos, K. (2012) · RNA · doi:10.1261/rna.029322.111 · Cited by 17 · see citing works
Self-citation
Iron, Oxidative Stress and Health
Udipi, S., Ghugre, P., & Gokhale, C. (2012) · Oxidative Stress - Molecular Mechanisms and Biological Effects · doi:10.5772/34975 · Cited by 17 · see citing works
“Thus when iron levels exceed the cellular needs, the IRE/IRP switch minimizes iron uptake and promotes iron storage (Mackenzie, Iwasaki and Tsuji, 2008; Wang and Pantopoulos, 2011).”
BackgroundInfluential
Siderite (FeCO3) and magnetite (Fe3O4) overload-dependent pulmonary toxicity is determined by the poorly soluble particle not the iron content
Pauluhn, J., & Wiemann, M. (2011) · Inhalation Toxicology · doi:10.3109/08958378.2011.606431 · Cited by 16 · see citing works
Dietary and Sentinel Factors Leading to Hemochromatosis
Oh, C.-K., & Moon, Y. (2019) · Nutrients · doi:10.3390/nu11051047 · Cited by 12 · see citing works
Nutraceuticals in immunosenescence
Magrone, T., & Jirillo, E. (2015) · Anti‐ageing nutrients · doi:10.1002/9781118823408.ch5 · Cited by 4 · see citing works

Authors: Wang, J., & Pantopoulos, K.
Affiliations: Jewish General Hospital (CA)
Corresponding author: Pantopoulos, Kostas
ORCID: Pantopoulos, Kostas
Venue: Biochemical Journal
Publisher: Portland Press Ltd.
Published: 2011-02-24
Volume: 434
Issue: 3
Pages: 365-381
ISSN: 0264-6021 (ISSN-L)
1470-8728
DOI: 10.1042/bj20101825
PMC: PMC3048577
OpenAlex: W2158115535
Cited by: 986
References: 208
Citations by year: 2026: 38 · 2025: 41 · 2024: 54 · 2023: 72 · 2022: 69 · 2021: 70 · 2020: 71 · 2019: 72 · 2018: 67 · 2017: 64 · 2016: 56 · 2015: 67 · 2014: 77 · 2013: 76 · 2012: 60
FWCI: 10.28
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by-nc
creativecommons.org/licenses/by-nc/2.5/ (vor, 3073 d)
Locations: Biochemical Journal (publishedVersion, cc-by-nc)
PubMed Central (publishedVersion, cc-by-nc)
PubMed (publishedVersion)
Funders: Canadian Institutes of Health Research (MOP-86514)
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, transferrin, transferrin receptor 1, iron absorption, endocytosis, mitochondrial iron transport, haem synthesis, iron-sulfur clusters, ferritin, iron storage, post-transcriptional regulation
MeSH terms: Animals, Biological Transport, Ferritins, Humans, Iron, Mitochondria, Neoplasms, Oxidation-Reduction, RNA, Messenger, Transferrin, Response Elements, Iron-Regulatory Proteins

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Regulation of cellular iron metabolism

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