The DOI matches its Crossref record; 218 of the 218 references it cites were found in a registry or an index.
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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In the citing paper
“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
Citations
Cites
Targeting Hypoxia-Inducible Factors for the Treatment of Anemia in Chronic Kidney Disease Patients
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Hepcidin Regulates Cellular Iron Efflux by Binding to Ferroportin and Inducing Its Internalization
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Cloning and characterization of a mammalian proton-coupled metal-ion transporter
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The ferritins: molecular properties, iron storage function and cellular regulation
Harrison, P. M., & Arosio, P. (1996) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(96)00022-9 · Cited by 2,667
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
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Positional cloning of zebrafish ferroportin1 identifies a conserved vertebrate iron exporter
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Dysmetabolic Hyperferritinemia: All Iron Overload Is Not Hemochromatosis
Makker, J. S., Hanif, A., Bajantri, B., & Chilimuri, S. S. (2015) · Case Reports in Gastroenterology · doi:10.1159/000373883 · Cited by 1,353
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
Research works printed but not linked: 1
- MacGillivray RTA, Mason AB (2001) Transferrins. In: Templeton DM (ed) Molecular and cellular iron transport. Marcel Dekker, New York, pp 41–69
Cited by
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The Metabolic Underpinnings of Ferroptosis
Zheng, J., & Conrad, M. (2020) · Cell Metabolism · doi:10.1016/j.cmet.2020.10.011 · Cited by 1,368
Current understanding of iron homeostasis
Anderson, G. J., & Frazer, D. M. (2017) · The American Journal of Clinical Nutrition · doi:10.3945/ajcn.117.155804 · Cited by 688
Self-citationNon-transferrin bound iron: a key role in iron overload and iron toxicity
Brissot, P., Ropert, M., Le Lan, C., & Loréal, O. (2012) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2011.07.014 · Cited by 654
Iron deficiency: an ominous sign in patients with systolic chronic heart failure
Jankowska, E. A., Rozentryt, P., Witkowska, A., Nowak, J., Hartmann, O., Ponikowska, B., Borodulin-Nadzieja, L., Banasiak, W., Polonski, L., Filippatos, G., et al. (2010) · European Heart Journal · doi:10.1093/eurheartj/ehq158 · Cited by 652
Dental Enamel Formation and Implications for Oral Health and Disease
Lacruz, R. S., Habelitz, S., Wright, J. T., & Paine, M. L. (2017) · Physiological Reviews · doi:10.1152/physrev.00030.2016 · Cited by 650
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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