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Mammalian iron transport
Open accessAbstract
Iron is essential for basic cellular processes but is toxic when present in excess. Consequently, iron transport into and out of cells is tightly regulated. Most iron is delivered to cells bound to plasma transferrin via a process that involves transferrin receptor 1, divalent metal-ion transporter 1 and several other proteins. Non-transferrin-bound iron can also be taken up efficiently by cells, although the mechanism is poorly understood. Cells can divest themselves of iron via the iron export protein ferroportin in conjunction with an iron oxidase. The linking of an oxidoreductase to a membrane permease is a common theme in membrane iron transport. At the systemic level, iron transport is regulated by the liver-derived peptide hepcidin which acts on ferroportin to control iron release to the plasma.
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“During periods of high iron requirement, such as in iron deficiency or pregnancy, its levels are reduced to increase duodenal iron absorption and release from macrophages (Anderson and Vulpe, 2009).”
From Iron at the Centre of Candida albicans Interactions (2018) · cites this paper as Anderson and Vulpe, 2009
In the citing paper
“Transferrin transfers iron to cells through transferrin receptor 1 (TfR1) found on the surface of most body cells, and via transferrin receptor 2 (TfR2) expressed mainly in hepatocytes (Anderson and Vulpe, 2009; Caza and Kronstad, 2013).”
From Iron at the Centre of Candida albicans Interactions (2018) · cites this paper as Anderson and Vulpe, 2009
In the citing paper
“Transferrin-Transferrin receptor (TfR1) interaction triggers cell-mediated endocytosis of the complex and iron bound on transferrin dissociates within endosomes at a low pH (~5.5) since apotransferrin binds iron with a higher affinity at physiological pH relative to a low pH (Bali and Aisen, 1992; Anderson and Vulpe, 2009).”
From Iron at the Centre of Candida albicans Interactions (2018) · cites this paper as Anderson and Vulpe, 2009
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Metadata
- Authors
- Anderson, G. J., & Vulpe, C. D.
- Affiliations
- QIMR Berghofer Medical Research Institute (AU)
- Corresponding author
- Anderson, Gregory Jon
- Venue
- Cellular and Molecular Life Sciences
- Published
- 2009-05-31
- Volume
- 66
- Issue
- 20
- Pages
- 3241-3261
- ISSN
- 1420-682X (ISSN-L)
- 1420-9071
- PMC
- PMC11115736
- OpenAlex
- W1981407334
- Cited by
- 317
- References
- 217
- Citations by year
- 2026: 6 · 2025: 25 · 2024: 21 · 2023: 21 · 2022: 24 · 2021: 17 · 2020: 14 · 2019: 18 · 2018: 16 · 2017: 14 · 2016: 9 · 2015: 16 · 2014: 20 · 2013: 23 · 2012: 33
- FWCI
- 3.34
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Cellular and Molecular Life Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Ferroptosis and cancer prognosis
- Health Sciences › Nursing › Nutrition and Dietetics › Trace Elements in Health
- Keywords
- iron transport, transferrin, transferrin receptor 1, DMT1, ferroportin, hepcidin, non-transferrin-bound iron, iron export, iron homeostasis, membrane transporters
- MeSH terms
- Animals, Biological Transport, Carrier Proteins, Gene Expression Regulation, Homeostasis, Iron, Macrophages, Mammals, Mitochondria, Models, Biological, Oxidoreductases, Hepatocytes, Antimicrobial Cationic Peptides, Erythroid Cells, Hepcidins
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