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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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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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