Cited by 317Iron Metabolism and DisordersFerroptosis and cancer prognosisTrace Elements in Health

Mammalian iron transport

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Anderson, Gregory Jon, Vulpe, Christopher D.·2009·Cellular and Molecular Life Sciences

Abstract

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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Crossref · 10.1007/s00018-009-0051-1

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219 of 219 references verified0 citation errors · 0 not checkable

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  • During periods of high iron requirement, such as iron deficiency or pregnancy, hepcidin levels are reduced to increase duodenal iron absorption and release from macrophages.

    “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

  • 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.

    “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

  • Transferrin-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.

    “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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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
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
Locations
  • Cellular and Molecular Life Sciences (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
  • Health Sciences › Medicine › Pulmonary and Respiratory Medicine › 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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