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A Novel Mammalian Iron-regulated Protein Involved in Intracellular Iron Metabolism
Open accessAbstract
We have isolated and characterized a novel iron-regulated gene that is homologous to the divalent metal transporter 1 family of metal transporters. This gene, termed metal transporter protein (mtp1), is expressed in tissues involved in body iron homeostasis including the developing and mature reticuloendothelial system, the duodenum, and the pregnant uterus. MTP1 is also expressed in muscle and central nervous system cells in the embryo. At the subcellular level, MTP1 is localized to the basolateral membrane of the duodenal epithelial cell and a cytoplasmic compartment of reticuloendothelial system cells. Overexpression of MTP1 in tissue culture cells results in intracellular iron depletion. In the adult mouse, MTP1 expression in the liver and duodenum are reciprocally regulated. Iron deficiency induces MTP1 expression in the duodenum but down-regulates expression in the liver. These data indicate that MTP1 is an iron-regulated membrane-spanning protein that is involved in intracellular iron metabolism.
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“Iron can then be transported across the phagolysosomal membrane by DMT1 and NRAMP1, whereas FPN1 mediates iron export to the circulation (Abboud and Haile, 2000;Soe-Lin et al., 2009), where iron is incorporated in TF for cargo to tissues and organs.”
From Iron in infection and immunity (2020) · cites this paper as Abboud and Haile, 2000
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“Cellular iron export – and, therefore, gastrointestinal absorption of iron – is uniquely mediated by the iron transporter ferroportin (FPN or SLC40A1). 21 , 22 , 23 , 24”
From The battle for iron in enteric infections (2020) · cites this paper as [21]
In the citing paper
“The basolateral iron transporter, discovered simultaneously by 3 labs, is ferroportin (also called IREG1, MTP1, SLC39A1, and now SLC40A1).54,77,78”
From Forging a field: the golden age of iron biology. (2008) · cites this paper as [77]
In the citing paper
“Simultaneous studies characterized Fpn, which is abundantly expressed on the basolateral membrane of polarized enterocytes in the duodenum, in the cytosol of reticuloendothelial cells, and on the basal surface of syncytiotrophoblasts of the placenta (1, 72, 198).”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [1]
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Cites
Tuerk, C., & Gold, L. (1990) · Science · doi:10.1126/science.2200121 · Cited by 10,421
Cloning and characterization of a mammalian proton-coupled metal-ion transporter
Gunshin, H., Mackenzie, B., Berger, U. V., Gunshin, Y., Romero, M. F., Boron, W. F., Nussberger, S., Gollan, J. L., & Hediger, M. A. (1997) · Nature · doi:10.1038/41343 · Cited by 3,166
Positional cloning of zebrafish ferroportin1 identifies a conserved vertebrate iron exporter
Donovan, A., Brownlie, A., Zhou, Y., Shepard, J., Pratt, S. J., Moynihan, J., Paw, B. H., Drejer, A., Barut, B., Zapata, A., et al. (2000) · Nature · doi:10.1038/35001596 · Cited by 1,667
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
Vulpe, C. D., Kuo, Y.-M., Murphy, T. L., Cowley, L., Askwith, C., Libina, N., Gitschier, J., & Anderson, G. J. (1999) · Nature Genetics · doi:10.1038/5979 · Cited by 1,084
Canonne-Hergaux, F., Gruenheid, S., Ponka, P., & Gros, P. (1999) · Blood · doi:10.1182/blood.v93.12.4406 · Cited by 451
Haile, D. J., Rouault, T. A., Tang, C., Chin, J., Harford, J. B., & Klausner, R. D. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.16.7536 · Cited by 270
Self-citationCrystal, R. G. (1997) · Nature Medicine · doi:10.1038/nm0497-383 · Cited by 204
Sibille, J., Kondo, H. G., & Aisen, P. (1988) · Hepatology · doi:10.1002/hep.1840080218 · Cited by 139
Pinner, E., Gruenheid, S., Raymond, M., & Gros, P. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.46.28933 · Cited by 115
Research works printed but not linked: 2
- Umbreit, 1998, Semin. Hematol., 35, 13
- Oates, 1997, Am. J. Physiol., 273, G636
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Davis, M. R., Shawron, K., Rendina-Ruedy, E., Peterson, S., Lucas, E. A., Smith, B. J., & Clarke, S. L. (2011) · Journal of Nutrition · doi:10.3945/jn.111.144105 · Cited by 30
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Collins, J. F., Flores, S. R., Wang, X., & Anderson, G. J. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-809954-4.00060-8 · Cited by 30
Iron metabolism: microbes, mouse, and man
Latunde‐Dada, G. O. (2009) · BioEssays · doi:10.1002/bies.200900101 · Cited by 29
Subramaniam, V., Golik, P., Murdock, D. G., Levy, S., Kerstann, K. W., Coskun, P. E., Melkonian, G., & Wallace, D. C. (2008) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.03.015 · Cited by 31
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Zhang, X., Song, T., Zhao, M., Tao, X., Zhang, B., Sun, C., Wang, P., Wang, K., & Zhao, L. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.827016 · Cited by 29
Barisani, D., & Conte, D. (2002) · Blood Cells Molecules and Diseases · doi:10.1006/bcmd.2002.0588 · Cited by 29
The anticancer properties of iron core–gold shell nanoparticles in colorectal cancer cells
Wu, Y., Wu, Yang, L., Ratinac, K. R., Thordarson, Jahn, Shieh, Braet, F., & Chen, D. (2013) · International Journal of Nanomedicine · doi:10.2147/ijn.s47742 · Cited by 30
Iron uptake mediated by the plant-derived chelator nicotianamine in the small intestine
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Nutrients Released by Gastric Epithelial Cells Enhance Helicobacter pylori Growth
Amsterdam, K. V., & ENDE, A. V. D. (2004) · Helicobacter · doi:10.1111/j.1083-4389.2004.00272.x · Cited by 29
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Colucci, S., Marques, O., & Altamura, S. (2021) · Seminars in Hematology · doi:10.1053/j.seminhematol.2021.05.001 · Cited by 28
Kong, W., Zhao, S., Duan, X., Yang, Z., Qian, Z., & Chang, Y. (2008) · Journal of Cellular Biochemistry · doi:10.1002/jcb.21654 · Cited by 28
Recent advances in intestinal iron transport
Anderson, G. J., & Frazer, D. M. (2005) · Current Gastroenterology Reports · doi:10.1007/s11894-005-0005-1 · Cited by 31
Protective effects of 1α,25-Dihydroxyvitamin D3 on cultured neural cells exposed to catalytic iron
Uberti, F., Morsanuto, V., Bardelli, C., & Molinari, C. G. (2016) · Physiological Reports · doi:10.14814/phy2.12769 · Cited by 27
Iron transport across the human placenta is regulated by hepcidin
McDonald, E. A., Gündoğan, F., Olveda, R. M., Bartnikas, T. B., Kurtis, J. D., & Friedman, J. F. (2020) · Pediatric Research · doi:10.1038/s41390-020-01201-y · Cited by 27
Iron metabolism in mammalian cells
Walker, B., Tiong, J., & Jefferies, W. A. (2001) · International review of cytology · doi:10.1016/s0074-7696(01)11020-x · Cited by 27
Immunolocalization of Ferroportin in Healthy and Anemic Mice
D’Anna, M. C., Veuthey, T., & Roque, M. E. (2008) · Journal of Histochemistry & Cytochemistry · doi:10.1369/jhc.2008.951616 · Cited by 27
Li, X., Xie, J., Lü, L., Zhang, L., Zhang, L., Zou, Y., Wang, Q., Luo, X., & Li, S. (2013) · BioMetals · doi:10.1007/s10534-013-9670-y · Cited by 27
Greene, C., Sharma, N. J., Fiorica, P. N., Forrester, E. J., Smith, G. J., Gross, K. W., & KAUFFMAN, E. C. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.12.013 · Cited by 28
Bach, V., Remacha, A. F., Altés, A., Barceló, M. J., Molina, M. A., & Baiget, M. (2005) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2005.09.001 · Cited by 27
Zebrafish myelopoiesis and blood cell development
Hsu, K., Kanki, J. P., & Look, A. T. (2001) · Current Opinion in Hematology · doi:10.1097/00062752-200107000-00011 · Cited by 27
Intestinal metal ion absorption: an update
Rolfs, A., & Hediger, M. A. (2001) · Current Opinion in Gastroenterology · doi:10.1097/00001574-200103000-00014 · Cited by 27
Wang, Q., Ji, J., Hao, S., Zhang, M., Li, K., & Qiao, T. (2016) · Journal of Atherosclerosis and Thrombosis · doi:10.5551/jat.32292 · Cited by 29
Conservation in the Iron Responsive Element Family
Volz, K. W. (2021) · Genes · doi:10.3390/genes12091365 · Cited by 26
Dong, X., Gao, W., KONG, W.-N., XIE, H.-L., PENG, Y., Shao, T.-M., Yu, W., & Xi-qing, C. (2015) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2015.2234 · Cited by 26
Ferroportin and Erythroid Cells: An Update
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Hałoń, M., Kaczor, J. J., Ziółkowski, W., Flis, D. J., Borkowska, A., Popowska, U., Nyka, W. M., Woźniak, M., & Antosiewicz, J. (2014) · Free Radical Research · doi:10.3109/10715762.2014.955484 · Cited by 26
Schroeter, J. D., Dorman, D. C., Yoon, M., Nong, A., Taylor, M. D., Andersen, M. E., & M.A., H. J. C. I. (2012) · Toxicological Sciences · doi:10.1093/toxsci/kfs212 · Cited by 26
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Dzikaite, V., Holmström, P., Stål, P., Eckes, K., Hagen, K., Eggertsen, G., Gåfvels, M., Melefors, Ö., & Hultcrantz, R. (2006) · Journal of Hepatology · doi:10.1016/j.jhep.2005.07.028 · Cited by 26
Branisso, P. P. F. (2018) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/t.5.2018.tde-23102018-125025 · Cited by 26
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Farajdokht, F., Soleimani, M., Mehrpouya, S., Barati, M., & Nahavandi, A. (2015) · Neuroscience Letters · doi:10.1016/j.neulet.2015.01.008 · Cited by 26
Chen, X., Ma, X., Yang, C.-W., Jiang, S., Huang, L.-B., Li, Y., Zhang, F., Jiao, N., & Yang, W. (2022) · Frontiers in Veterinary Science · doi:10.3389/fvets.2022.903615 · Cited by 25
Huang, M. L. H., Austin, C., Sari, M., Rahmanto, Y. S., Ponka, P., Vyoral, D., & Richardson, D. R. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.471573 · Cited by 25
Starzyński, R. R., Canonne‐Hergaux, F., Willemetz, A., Gralak, M. A., Woliński, J., Styś, A., Olszak, J., & Lipiński, P. (2009) · Biochemical Journal · doi:10.1042/bj20082137 · Cited by 25
Zhuo, Z., Fang, S., Hu, Q., Huang, D., & Feng, J. (2016) · Scientific Reports · doi:10.1038/srep37923 · Cited by 25
Speletas, M. G., Kioumi, A., Loules, G., Hytiroglou, P., Tsitouridis, J., Christakis, J. I., & Germenis, A. E. (2007) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2007.09.011 · Cited by 25
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Hirsh, M., Konijn, A. M., & Iancu, T. C. (2002) · Journal of Hepatology · doi:10.1016/s0168-8278(01)00221-5 · Cited by 25
Strategy and tactics in the evolution of iron acquisition
Kaplan, J. (2002) · Seminars in Hematology · doi:10.1053/shem.2002.35631 · Cited by 25
Chiabrando, D., Fiorito, V., Marro, S., Silengo, L., Altruda, F., & Tolosano, E. (2013) · Blood Cells, Molecules, and Diseases · doi:10.1016/j.bcmd.2012.08.002 · Cited by 24
Kelleher, T., Ryan, E., Barrett, S., Sweeney, M., Byrnes, V, O’Keane, C., & Crowe, J. (2004) · Gut · doi:10.1136/gut.2003.033811 · Cited by 24
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Alves, F. M., Kysenius, K., Caldow, M. K., Hardee, J. P., Chung, J. D., Trieu, J., Hare, D. J., Crouch, P. J., Ayton, S., Bush, A. I., et al. (2022) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12950 · Cited by 25
Jenkitkasemwong, S., Broderius, M. A., Nam, H., Prohaska, J. R., & Knutson, M. D. (2010) · Journal of Nutrition · doi:10.3945/jn.109.117077 · Cited by 24
Bergmann, O. M., Mathahs, M. M., Broadhurst, K. A., Weydert, J. A., Wilkinson, N. W., Howe, J. R., Han, O., Schmidt, W. N., & Brown, K. E. (2008) · Laboratory Investigation · doi:10.1038/labinvest.2008.95 · Cited by 25
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Ma, J., Zhang, F., Zhou, G., Bao, Y.-X., Shen, Y., & Qian, Z. (2018) · Neurochemical Research · doi:10.1007/s11064-018-2577-9 · Cited by 23
Gaurav, R., Mikuls, T. R., Thiele, G. M., Nelson, A. J., Niu, M., Guda, C., Eudy, J. D., Barry, A., Wyatt, T. A., Romberger, D. J., et al. (2021) · PLoS ONE · doi:10.1371/journal.pone.0240707 · Cited by 24
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Qian, Z., Li, W., & Guo, Q. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.101961 · Cited by 22
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Tapryal, N., Vishnu Vivek, G., & Mukhopadhyay, C. K. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.592519 · Cited by 22
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Molecular Mechanisms of Intestinal Iron Transport
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Shahandeh, A., Bui, B. V., Finkelstein, D. I., & Nguyen, C. T. O. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.794809 · Cited by 21
Mylvaganam, S., & Freeman, S. A. (2023) · Immunological Reviews · doi:10.1111/imr.13260 · Cited by 23
Wang, Y., Protchenko, O. V., Huber, K. D., Shakoury‐Elizeh, M., Ghosh, M. C., & Philpott, C. C. (2023) · Blood · doi:10.1182/blood.2023020504 · Cited by 22
Balušíková, K., Neubauerová, J., Dostalikova‐Cimburova, M., Horák, J., & Kovár̆, J. (2008) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-008-9926-y · Cited by 20
Song, G., Jiang, Q., Xu, T., Liu, Y., Xu, Z., & Guo, Z. (2013) · FEBS Journal · doi:10.1111/febs.12192 · Cited by 20
Manganese transport and toxicity in polarized WIF-B hepatocytes
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Metadata
- Authors
- Abboud, S., & Haile, D. J.
- Affiliations
- The University of Texas at San Antonio Health Science Center (US)
- Corresponding author
- Haile, David J.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2000-06
- Volume
- 275
- Issue
- 26
- Pages
- 19906-19912
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2063617352
- Cited by
- 1,267
- References
- 14
- Citations by year
- 2026: 9 · 2025: 20 · 2024: 26 · 2023: 25 · 2022: 34 · 2021: 47 · 2020: 52 · 2019: 25 · 2018: 48 · 2017: 36 · 2016: 51 · 2015: 39 · 2014: 65 · 2013: 51 · 2012: 49
- FWCI
- 34.94
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r01dk053079-02)
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK-53079, R03DK96009)
- 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
- DMT1, iron homeostasis, duodenal epithelium, reticuloendothelial system, liver, iron deficiency, basolateral membrane, gene expression regulation
- MeSH terms
- Iron Deficiencies, Ferroportin, Amino Acid Sequence, Animals, Base Sequence, Carrier Proteins, Cloning, Molecular, Duodenum, Embryo, Mammalian, Ferritins, Humans, Iron, Liver, Mice, Inbred C57BL, Molecular Sequence Data, Plasmids, Sequence Homology, Nucleic Acid, Tissue Distribution, Transfection, Blotting, Western, Down-Regulation, Sequence Homology, Amino Acid, DNA, Complementary, Fluorescent Antibody Technique, Indirect, COS Cells, Cation Transport Proteins, Mice
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