Iron regulatory proteins are essential for intestinal function and control key iron absorption molecules in the duodenum
Open accessAbstract
Iron regulatory proteins (IRPs) orchestrate the posttranscriptional regulation of critical iron metabolism proteins at the cellular level. Redundancy between IRP1 and IRP2 associated with embryonic lethality of doubly IRP-deficient mice has precluded the study of IRP function in vivo. Here we use Cre/Lox technology to generate viable organisms lacking IRP expression in a single tissue, the intestine. Mice lacking intestinal IRP expression develop intestinal malabsorption and dehydration postnatally and die within 4 weeks of birth. We demonstrate that IRPs control the expression of divalent metal transporter 1 (DMT1) mRNA and protein, a limiting intestinal iron importer. IRPs are also shown to be critically important to secure physiological levels of the basolateral iron exporter ferroportin. IRPs are thus essential for intestinal function and organismal survival and coordinate the synthesis of key iron metabolism proteins in the duodenum.
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
Cites
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?
Mice lacking IRPs completely in hepatocytes or duodenal enterocytes die early after birth, showing IRPs are needed for organismal survival.
“Earlier work investigating mice with complete IRP deficiency in hepatocytes or duodenal enterocytes, respectively, had shown early post-natal death in both cases, reflecting essential functions of the IRPs for organismal survival (Galy et al., 2008, 2010).”
From Iron Regulatory Proteins Mediate Host Resistance to Salmonella Infection (2015) · cites this paper as Galy et al., 2008
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Hepcidin Regulates Cellular Iron Efflux by Binding to Ferroportin and Inducing Its Internalization
Nemeth, E., Tuttle, M. S., Powelson, J., Vaughn, M. B., Donovan, A., Ward, D. M., Ganz, T., & Kaplan, J. (2004) · Science · doi:10.1126/science.1104742 · Cited by 4,803 · 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
Hentze, M. W., Muckenthaler, M. U., & Andrews, N. C. (2004) · Cell · doi:10.1016/s0092-8674(04)00343-5 · Cited by 1,736 · see citing works
Self-citationMcKie, 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
Self-citationThe iron exporter ferroportin/Slc40a1 is essential for iron homeostasis
Donovan, A., Lima, C. A., Pinkus, J. L., Pinkus, G. S., Zon, L. I., Robine, S., & Andrews, N. C. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.01.003 · Cited by 1,275 · 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 Iron Metabolism by Hepcidin
Nemeth, E., & Ganz, T. (2006) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.26.061505.111303 · Cited by 756 · see citing works
Madison, B., Dunbar, L., Qiao, X. T., Braunstein, K., Braunstein, E. M., & Gumucio, D. L. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204935200 · Cited by 748 · see citing works
Andrews, N. C., & Schmidt, P. J. (2006) · Annual Review of Physiology · doi:10.1146/annurev.physiol.69.031905.164337 · Cited by 640 · see citing works
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
Hubert, N., & Hentze, M. W. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.192423399 · Cited by 428 · see citing works
Self-citationMeyron‐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
Suzuki, Y. A., López, V., & Lönnerdal, B. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-005-5371-1 · Cited by 384 · 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
Self-citationMolecular 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
Differentiation and self-renewal in the mouse gastrointestinal epithelium
Gordon, J. I., & Hermiston, M. L. (1994) · Current Opinion in Cell Biology · doi:10.1016/0955-0674(94)90047-7 · Cited by 258 · 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
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
Galy, B., Ferring–Appel, D., Miñana, B., Bell, O., Janser, H., Muckenthaler, M. U., Schümann, K., & Hentze, M. W. (2005) · Blood · doi:10.1182/blood-2005-04-1365 · Cited by 222 · see citing works
Self-citationIron homeostasis: new tales from the crypt
Roy, C. N., & Enns, C. A. (2000) · Blood · doi:10.1182/blood.v96.13.4020 · Cited by 175 · see citing works
CaMKII?-cre transgene expression and recombination patterns in the mouse brain
Dragatsis, I., & Zeitlin, S. O. (2000) · genesis · doi:10.1002/(sici)1526-968x(200002)26:2 · Cited by 171 · see citing works
Iron Imports. I. Intestinal iron absorption and its regulation
Frazer, D. M., & Anderson, G. J. (2005) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00220.2005 · Cited by 135 · see citing works
Functional differences between hepcidin 1 and 2 in transgenic mice
Lou, D.-Q., Nicolas, G., Lesbordes, J.-C., Viatte, L., Grimber, G., Szajnert, M.-F., Kahn, A., & Vaulont, S. (2004) · Blood · doi:10.1182/blood-2003-07-2524 · Cited by 123 · see citing works
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
Pietrangelo, A. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.05.013 · Cited by 99 · see citing works
Schalinske, K. L., Chen, O. S., & Eisenstein, R. S. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.6.3740 · Cited by 84 · see citing works
Iron regulatory protein as an endogenous sensor of iron in rat intestinal mucosa
Schümann, K., Moret, R., Künzle, H., & Kühn, L. C. (1999) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1999.00155.x · Cited by 78 · see citing works
Beneficial Effects of CCR1 Blockade on the Progression of Chronic Renal Allograft Damage
Bedke, J., Kiss, É., Schaefer, L., Behnes, C. L., Bonrouhi, M., Gretz, N., Horuk, R., Diedrichs-Moehring, M., Wildner, G., Nelson, P., et al. (2007) · American Journal of Transplantation · doi:10.1111/j.1600-6143.2006.01654.x · Cited by 56 · see citing works
Self-citationGaly, B., Ferring–Appel, D., Benešová, M., Beneš, V., & Hentze, M. W. (2004) · RNA · doi:10.1261/rna.7220704 · Cited by 55 · see citing works
Self-citationGeneration of conditional alleles of the murine iron regulatory protein (IRP)‐1 and ‐2 genes
Galy, B., Ferring, D., & Hentze, M. W. (2005) · genesis · doi:10.1002/gene.20169 · Cited by 53 · see citing works
Self-citationPorubský, Š., Schmid, H., Bonrouhi, M., Kretzler, M., Malle, E., Nelson, P. J., & Gröne, H. (2004) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)63775-3 · Cited by 51 · see citing works
Self-citationAdvances in understanding the molecular basis for the regulation of dietary iron absorption
Fleming, R. E. (2005) · Current Opinion in Gastroenterology · doi:10.1097/01.mog.0000153362.98276.db · Cited by 47 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
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
Self-citationIron and cancer: more ore to be mined
Torti, S. V., & Torti, F. M. (2013) · Nature Reviews Cancer · doi:10.1038/nrc3495 · Cited by 1,621 · see citing works
A Red carpet for iron metabolism
Muckenthaler, M. U., Rivella, S., Hentze, M. W., & Galy, B. (2017) · Cell · doi:10.1016/j.cell.2016.12.034 · Cited by 1,319 · see citing works
Self-citationRegulation of cellular iron metabolism
Wang, J., & Pantopoulos, K. (2011) · Biochemical Journal · doi:10.1042/bj20101825 · Cited by 986 · see citing works
Mechanisms controlling cellular and systemic iron homeostasis
Galy, B., Conrad, M., & Muckenthaler, M. U. (2023) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-023-00648-1 · Cited by 806 · see citing works
Self-citationMuckenthaler, 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
Self-citationMechanisms of mammalian iron homeostasis
Pantopoulos, K., Porwal, S. K., Tartakoff, A., & Devireddy, L. (2012) · Biochemistry · doi:10.1021/bi300752r · Cited by 598 · see citing works
Iron Overload in Human Disease
Fleming, R. E., & Ponka, P. (2012) · New England Journal of Medicine · doi:10.1056/nejmra1004967 · Cited by 592 · 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
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
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
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
Salazar, J., Mena, N., Hunot, S., Prigent, A., Alvarez-Fischer, D., Arredondo, M., Duyckaerts, C., Sazdovitch, V., Zhao, L., Garrick, L. M., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0804373105 · Cited by 409 · see citing works
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
Mechanistic and regulatory aspects of intestinal iron absorption
Gulec, S., Anderson, G. J., & Collins, J. F. (2014) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00348.2013 · Cited by 406 · 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
Mutations in SLC39A14 disrupt manganese homeostasis and cause childhood-onset parkinsonism–dystonia
Tuschl, K., Meyer, E., Valdivia, L. E., Zhao, N., Dadswell, C., Abdul‐Sada, A. K., Hung, C., Simpson, M. A., Chong, W. K., Jacques, T. S., et al. (2016) · Nature Communications · doi:10.1038/ncomms11601 · Cited by 317 · see citing works
Anderson, G. J., & Vulpe, C. D. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-0051-1 · Cited by 317 · see citing works
Middendorp, S., Schneeberger, K., Wiegerinck, C. L., Mokrý, M., Akkerman, R. D. L., Wijngaarden, S., Clevers, H. C., & Nieuwenhuis, E. E. S. (2014) · Stem Cells · doi:10.1002/stem.1655 · Cited by 302 · see citing works
The physiological functions of iron regulatory proteins in iron homeostasis - an update
Zhang, D., Ghosh, M. C., & Rouault, T. A. (2014) · Frontiers in Pharmacology · doi:10.3389/fphar.2014.00124 · Cited by 301 · see citing works
Marro, S., Chiabrando, D., Messana, E., Stolte, J., Turco, E., Tolosano, E., & Muckenthaler, M. U. (2010) · Haematologica · doi:10.3324/haematol.2009.020123 · Cited by 297 · see citing works
Evstatiev, R., & Gasché, C. (2011) · Gut · doi:10.1136/gut.2010.214312 · Cited by 292 · see citing works
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
Iron Acquisition and Transcriptional Regulation
Kaplan, C. D., & Kaplan, J. (2009) · Chemical Reviews · doi:10.1021/cr9001676 · Cited by 275 · see citing works
Metabolic Enzymes Enjoying New Partnerships as RNA-Binding Proteins
Castelló, A., Hentze, M. W., & Preiß, T. (2015) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2015.09.012 · Cited by 274 · see citing works
Self-citationLiving with Iron (and Oxygen): Questions and Answers about Iron Homeostasis
Theil, E. C., & Goss, D. J. (2009) · Chemical Reviews · doi:10.1021/cr900052g · Cited by 265 · see citing works
Iron regulatory proteins and their role in controlling iron metabolism
Kühn, L. C. (2015) · Metallomics · doi:10.1039/c4mt00164h · Cited by 242 · see citing works
Nairz, M., Schleicher, U., Schroll, A., Sonnweber, T., Theurl, I., Ludwiczek, S., Talasz, H., Brandacher, G., Moser, P. L., Muckenthaler, M. U., et al. (2013) · Journal of Experimental Medicine · doi:10.1084/jem.20121946 · Cited by 204 · see citing works
Iron absorption and metabolism
Anderson, G. J., Frazer, D. M., & McLaren, G. D. (2009) · Current Opinion in Gastroenterology · doi:10.1097/mog.0b013e32831ef1f7 · Cited by 203 · see citing works
Hypoxia-inducible factors link iron homeostasis and erythropoiesis
Shah, Y. M., & Xie, L. (2014) · Gastroenterology · doi:10.1053/j.gastro.2013.12.031 · Cited by 187 · 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
Iron Homeostasis: Recently Identified Proteins Provide Insight into Novel Control Mechanisms
Zhang, A.-S., & Enns, C. A. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.r800017200 · Cited by 153 · see citing works
Iron in the Tumor Microenvironment-Connecting the Dots
Pfeifhofer-Obermair, C., Tymoszuk, P., Petzer, V., Weiss, G., & Nairz, M. (2018) · Frontiers in Oncology · doi:10.3389/fonc.2018.00549 · Cited by 151 · see citing works
Duodenal Cytochrome b (DCYTB) in Iron Metabolism: An Update on Function and Regulation
Lane, D. J. R., Bae, D.-H., Merlot, A. M., Sahni, S., & Richardson, D. R. (2015) · Nutrients · doi:10.3390/nu7042274 · Cited by 153 · 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
Self-citationIron homeostasis and organismal aging
Zeidan, R. S., Han, S. M., Leeuwenburgh, C., & Xiao, R. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101510 · Cited by 150 · see citing works
Molecular mechanisms of normal iron homeostasis
Zhang, A.-S., & Enns, C. A. (2009) · Hematology · doi:10.1182/asheducation-2009.1.207 · Cited by 145 · see citing works
Mammalian iron transporters: Families SLC11 and SLC40
Montalbetti, N., Simonin, A., Kovács, G., & Hediger, M. A. (2013) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2013.01.002 · Cited by 147 · see citing works
Inhibition of ferroptosis attenuates busulfan-induced oligospermia in mice
Zhao, X., Liu, Z., Gao, J., Li, H., Wang, X., Li, Y., & Sun, F. (2020) · Toxicology · doi:10.1016/j.tox.2020.152489 · Cited by 144 · see citing works
Iron and Intracerebral Hemorrhage: From Mechanism to Translation
Xiong, X.-Y., Wang, J., Qian, Z., & Yang, Q. (2013) · Translational Stroke Research · doi:10.1007/s12975-013-0317-7 · Cited by 142 · 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
Sánchez, M., Galy, B., Schwanhaeusser, B., Blake, J., Bähr-Ivacevic, T., Beneš, V., Selbach, M., Muckenthaler, M. U., & Hentze, M. W. (2011) · Blood · doi:10.1182/blood-2011-04-343541 · Cited by 132 · see citing works
Self-citationMcKie, A. T., & Simpson, R. J. (2011) · Humana Press eBooks · doi:10.1007/978-1-60327-485-2_6 · Cited by 132 · see citing works
Iron and Porphyrin Trafficking in Heme Biogenesis
Schultz, I. J., Chen, C., Paw, B. H., & Hamza, I. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.r110.119503 · Cited by 129 · see citing works
Mechanisms and regulations of ferroptosis
Zhang, X.-D., Liu, Z., Wang, M.-S., Guo, Y.-X., Wang, X., Luo, K., Huang, S., & Li, R. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1269451 · Cited by 131 · see citing works
Up-regulation of divalent metal transporter 1 in 6-hydroxydopamine intoxication is IRE/IRP dependent
Jiang, H. F., Song, N., Xu, H., Zhang, S., Wang, J., & Xie, J. (2010) · Cell Research · doi:10.1038/cr.2010.20 · Cited by 122 · 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
Iron Homeostasis: Fitting the Puzzle Pieces Together
Ganz, T. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.03.008 · Cited by 120 · see citing works
The gut in iron homeostasis: role of HIF-2 under normal and pathological conditions
Mastrogiannaki, M., Matak, P., & Peyssonnaux, C. (2013) · Blood · doi:10.1182/blood-2012-11-427765 · Cited by 116 · see citing works
SIREs: searching for iron-responsive elements
Campillos, M., Cases, I., Hentze, M. W., & Sanchez, M. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq371 · Cited by 102 · see citing works
Self-citationPelizzoni, I., Macco, R., Morini, M. F., Zacchetti, D., Grohovaz, F., & Codazzi, F. (2010) · Aging Cell · doi:10.1111/j.1474-9726.2010.00652.x · Cited by 110 · see citing works
Hirota, K. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.07.018 · Cited by 106 · see citing works
Iron Regulatory Proteins Mediate Host Resistance to Salmonella Infection
Nairz, M., Ferring-Appel, D., Casarrubea, D., Sonnweber, T., Viatte, L., Schroll, A., Haschka, D., Fang, F. C., Hentze, M. W., Weiss, G., et al. (2015) · Cell Host & Microbe · doi:10.1016/j.chom.2015.06.017 · Cited by 103 · see citing works
Self-citationGarrick, M. D., & Garrick, L. M. (2009) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2009.03.018 · Cited by 102 · see citing works
Iron regulatory proteins control a mucosal block to intestinal iron absorption
Galy, B., Ferring-Appel, D., Becker, C., Gretz, N., Gröne, H.-J., Schümann, K., & Hentze, M. W. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.02.026 · Cited by 98 · see citing works
Self-citationIron Absorption in Drosophila melanogaster
Mandilaras, K., Pathmanathan, T., & Missirlis, F. (2013) · Nutrients · doi:10.3390/nu5051622 · Cited by 96 · see citing works
Iron-Sensing Proteins that Regulate Hepcidin and Enteric Iron Absorption
Knutson, M. D. (2010) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.012809.104801 · Cited by 96 · see citing works
Andolfo, I., Falco, L. D., Asci, R., Russo, R., Colucci, S., Gorrese, M., Zollo, M., & Iolascon, A. (2010) · Haematologica · doi:10.3324/haematol.2009.020685 · Cited by 90 · see citing works
A general map of iron metabolism and tissue-specific subnetworks
Hower, V., Mendes, P., Torti, F. M., Laubenbacher, R., Akman, S. A., Shulaev, V., & Torti, S. V. (2009) · Molecular BioSystems · doi:10.1039/b816714c · Cited by 92 · see citing works
Iron and the heart: A paradigm shift from systemic to cardiomyocyte abnormalities
Paterek, A., Mackiewicz, U., & Ma̧czewski, M. (2019) · Journal of Cellular Physiology · doi:10.1002/jcp.28820 · Cited by 85 · see citing works
Irp2 regulates insulin production through iron-mediated Cdkal1-catalyzed tRNA modification
Ferreira, M. C., Anderson, C. P., Neschen, S., Zumbrennen‐Bullough, K. B., Romney, S. J., Kahle, M., Rathkolb, B., Gailus‐Durner, V., Fuchs, H., Wolf, E., et al. (2020) · Nature Communications · doi:10.1038/s41467-019-14004-5 · Cited by 83 · see citing works
Are There Common Biochemical and Molecular Mechanisms Controlling Manganism and Parkisonism
Roth, J. A. (2009) · NeuroMolecular Medicine · doi:10.1007/s12017-009-8088-8 · Cited by 82 · see citing works
Adachi, M., Kai, K., Yamaji, K., Ide, T., Noshirο, H., Kawaguchi, A., & Aishima, S. (2019) · Histopathology · doi:10.1111/his.13847 · Cited by 81 · see citing works
Chung, B., Chaston, T. B., Marks, J., Srai, S. K., & Sharp, P. (2009) · Journal of Nutrition · doi:10.3945/jn.108.102905 · Cited by 78 · see citing works
Romney, S. J., Newman, B. S., Thacker, C. M., & Leibold, E. A. (2011) · PLoS Genetics · doi:10.1371/journal.pgen.1002394 · Cited by 74 · see citing works
Lipiński, P., Styś, A., & Starzyński, R. R. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1018-1 · Cited by 73 · see citing works
The Relevance of Iron in the Pathogenesis of Multiple System Atrophy: A Viewpoint
Kaindlstorfer, C., Jellinger, K. A., Eschlböck, S., Stefanova, N., Weiß, G., & Wenning, G. K. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-170601 · Cited by 71 · see citing works
Goforth, J. B., Anderson, S. A., Nizzi, C. P., & Eisenstein, R. S. (2010) · RNA · doi:10.1261/rna.1857210 · Cited by 71 · see citing works
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
Aging-related changes in the iron status of skeletal muscle
DeRuisseau, K. C., Park, Y.-M., DeRuisseau, L. R., Cowley, P. M., Fazen, C. H., & Doyle, R. P. (2013) · Experimental Gerontology · doi:10.1016/j.exger.2013.08.011 · Cited by 69 · see citing works
Perturbation of Iron Metabolism by Cisplatin through Inhibition of Iron Regulatory Protein 2
Miyazawa, M., Bogdan, A. R., & Tsuji, Y. (2018) · Cell chemical biology · doi:10.1016/j.chembiol.2018.10.009 · Cited by 70 · see citing works
Bonadonna, M., Altamura, S., Tybl, E., Palais, G., Qatato, M., Polycarpou‐Schwarz, M., Schneider, M., Kalk, C., Rüdiger, W., Ertl, A., et al. (2022) · Science Advances · doi:10.1126/sciadv.abq4469 · Cited by 67 · see citing works
Self-citationZhang, S., Cao, Y., & Yang, Q. (2020) · PLoS Pathogens · doi:10.1371/journal.ppat.1008682 · Cited by 65 · see citing works
Molecular mechanism of intestinal iron absorption
Han, O. (2011) · Metallomics · doi:10.1039/c0mt00043d · Cited by 64 · see citing works
Iron misregulation and neurodegenerative disease in mouse models that lack iron regulatory proteins
Ghosh, M. C., Zhang, D., & Rouault, T. A. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.02.026 · Cited by 63 · see citing works
Lingli, J., Garrick, M. D., Garrick, L. M., Zhao, L., & Collins, J. F. (2013) · Journal of Nutrition · doi:10.3945/jn.113.181867 · Cited by 61 · see citing works
von Drygalski, A., & Adamson, J. W. (2012) · Journal of Parenteral and Enteral Nutrition · doi:10.1177/0148607112459648 · Cited by 61 · see citing works
Interactions Between Ferroportin and Hephaestin in Rat Enterocytes Are Reduced After Iron Ingestion
Yeh, K., YEH, M. K. Y., & Glass, J. (2011) · Gastroenterology · doi:10.1053/j.gastro.2011.03.059 · Cited by 57 · see citing works
Nobre, R. J., Herráez-Hernández, E., Fei, J.-W., Langbein, L., Kaden, S., Gröne, H., & de Villiers, E. (2009) · Journal of Virology · doi:10.1128/jvi.02490-08 · Cited by 60 · see citing works
Self-citationp53 tumor suppressor and iron homeostasis
Zhang, J., & Chen, X. (2018) · FEBS Journal · doi:10.1111/febs.14638 · Cited by 57 · see citing works
Cell‐type‐specific insights into iron regulatory processes
Mleczko‐Sanecka, K., & Silvestri, L. (2020) · American Journal of Hematology · doi:10.1002/ajh.26001 · Cited by 59 · see citing works
Lipid droplets and ferritin heavy chain: a devilish liaison in human cancer cell radioresistance
Tirinato, L., Marafioti, M. G., Pagliari, F., Jansen, J., Aversa, I., Hanley, R., Nisticò, C., García-Calderón, D., Genard, G. C., Guerreiro, J. F., et al. (2021) · eLife · doi:10.7554/elife.72943 · Cited by 55 · see citing works
Ferring–Appel, D., Hentze, M. W., & Galy, B. (2008) · Blood · doi:10.1182/blood-2008-05-155093 · Cited by 53 · see citing works
Self-citationTsuji, Y. (2020) · PLoS ONE · doi:10.1371/journal.pone.0235563 · Cited by 50 · see citing works
Role of duodenal iron transporters and hepcidin in patients with alcoholic liver disease
Dostalikova‐Cimburova, M., Balušíková, K., Krátká, K., Chmelíková, J., Hejda, V., Hnaníček, J., Neubauerová, J., Vránová, J., Kovár̆, J., & Horák, J. (2014) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.12310 · Cited by 50 · see citing works
Staroń, R., Lipiński, P., Lenartowicz, M., Bednarz, A., Gajowiak, A., Smuda, E., Krzeptowski, W., Pieszka, M., Korolonek, T., Hamza, I., et al. (2017) · PLoS ONE · doi:10.1371/journal.pone.0181117 · Cited by 49 · see citing works
Protein degradation and iron homeostasis
Thompson, J. W., & Bruick, R. K. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.02.003 · Cited by 48 · see citing works
Xie, T., Yao, L., & Li, X. (2024) · Antioxidants · doi:10.3390/antiox13060659 · Cited by 50 · see citing works
Regulation of Intestinal Iron Absorption: The Mucosa Takes Control?
Simpson, R. J., & McKie, A. T. (2009) · Cell Metabolism · doi:10.1016/j.cmet.2009.06.009 · Cited by 47 · see citing works
Vitamin A deficiency modulates iron metabolism via ineffective erythropoiesis
da Cunha, M. D. S. B., Siqueira, E. M. A., Trindade, L. S., & Arruda, S. F. (2014) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2014.05.005 · Cited by 46 · see citing works
Enculescu, M., Metzendorf, C., Sparla, R., Hahnel, M. J., Bode, J. G., Muckenthaler, M. U., & Legewie, S. (2017) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1005322 · Cited by 45 · see citing works
Ruiz, J. C., Walker, S. D., Anderson, S. A., Eisenstein, R. S., & Bruick, R. K. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.426171 · Cited by 44 · see citing works
Cystathionine β‐synthase is required for body iron homeostasis
Zhou, Y., Wu, X., Zhou, G., Mu, M., Zhang, F., Li, F., Qian, C., Du, F., Yung, W., Qian, Z., et al. (2017) · Hepatology · doi:10.1002/hep.29499 · Cited by 44 · see citing works
Isoform specific regulation of divalent metal (ion) transporter (DMT1) by proteasomal degradation
Garrick, M. D., Zhao, L., Roth, J. A., Jiang, H., Feng, J., Foot, N. J., Dalton, H. E., Kumar, S., & Garrick, L. M. (2012) · BioMetals · doi:10.1007/s10534-012-9522-1 · Cited by 42 · see citing works
Iron delocalisation in the pathogenesis of malarial anaemia
Nweneka, C. V., Doherty, C. P., Cox, S. E., & Prentice, A. M. (2009) · Transactions of the Royal Society of Tropical Medicine and Hygiene · doi:10.1016/j.trstmh.2009.08.007 · Cited by 41 · see citing works
Knockout Mouse Models of Iron Homeostasis
Fleming, R. E., Qi, F., & Britton, R. S. (2011) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-072610-145117 · Cited by 39 · see citing works
Núñez, M. T. (2010) · BioFactors · doi:10.1002/biof.84 · Cited by 36 · see citing works
Regulation of iron homeostasis: Lessons from mouse models
Altamura, S., Marques, O., Colucci, S., Mertens, C., Alikhanyan, K., & Muckenthaler, M. U. (2020) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2020.100872 · Cited by 35 · see citing works
Güleç, Ş., & Collins, J. F. (2013) · Journal of Nutrition · doi:10.3945/jn.113.183160 · Cited by 35 · see citing works
The actin-binding protein profilin 2 is a novel regulator of iron homeostasis
Luscieti, S., Galy, B., Gutiérrez, L., Reinke, M., Couso, J., Shvartsman, M., Pascale, A. D., Witke, W., Hentze, M. W., Boyl, P. P., et al. (2017) · Blood · doi:10.1182/blood-2016-11-754382 · Cited by 32 · see citing works
Self-citation
- Authors
- Galy, B., Ferring-Appel, D., Kaden, S., Gröne, H.-J., & Hentze, M. W.
- Affiliations
- European Molecular Biology Laboratory (DE)
- German Cancer Research Center (DE)
- Corresponding author
- Hentze, Matthias W.
- Venue
- Cell Metabolism
- Publisher
- Elsevier BV
- Published
- 2008-01
- Volume
- 7
- Issue
- 1
- Pages
- 79-85
- ISSN
- 1550-4131 (ISSN-L)
- OpenAlex
- W2031180114
- Cited by
- 195
- References
- 32
- Citations by year
- 2026: 6 · 2025: 8 · 2024: 5 · 2023: 10 · 2022: 7 · 2021: 5 · 2020: 12 · 2019: 6 · 2018: 9 · 2017: 7 · 2016: 4 · 2015: 7 · 2014: 15 · 2013: 14 · 2012: 15
- FWCI
- 14.07
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 2024 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Cell Metabolism (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Health Sciences › Nursing › Nutrition and Dietetics › Trace Elements in Health
- Life Sciences › Neuroscience › Neurology › Neurological diseases and metabolism
- Keywords
- iron regulatory proteins, iron regulatory protein 1, IRP2, intestinal iron absorption, duodenum, DMT1, ferroportin, post-transcriptional regulation, iron metabolism, malabsorption, tissue-specific knockout mice, Cre-loxP recombination
- MeSH terms
- Ferroportin, Solute Carrier Family 11, Member 2, Animals, Duodenum, Epithelial Cells, Intestinal Mucosa, Intestines, Iron, Mice, Transgenic, Immunoblotting, Polymerase Chain Reaction, Cation Transport Proteins, Iron-Regulatory Proteins, Iron Regulatory Protein 1, Iron Regulatory Protein 2, Microscopy, Electron, Transmission, Mice
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
