Hepcidin and iron homeostasis
Open accessAbstract
Despite fluctuations in dietary iron intake and intermittent losses through bleeding, the plasma iron concentrations in humans remain stable at 10-30 μM. While most of the iron entering blood plasma comes from recycling, appropriate amount of iron is absorbed from the diet to compensate for losses and maintain nontoxic amounts in stores. Plasma iron concentration and iron distribution are similarly regulated in laboratory rodents. The hepatic peptide hepcidin was identified as the systemic iron-regulatory hormone. In the efferent arc, hepcidin regulates intestinal iron absorption, plasma iron concentrations, and tissue iron distribution by inducing degradation of its receptor, the cellular iron exporter ferroportin. Ferroportin exports iron into plasma from absorptive enterocytes, from macrophages that recycle the iron of senescent erythrocytes, and from hepatocytes that store iron. In the more complex and less well understood afferent arc, hepatic hepcidin synthesis is transcriptionally regulated by extracellular and intracellular iron concentrations through a molecular complex of bone morphogenetic protein receptors and their iron-specific ligands, modulators and iron sensors. Through as yet undefined pathways, hepcidin is also homeostatically regulated by the iron requirements of erythroid precursors for hemoglobin synthesis. In accordance with the role of hepcidin-mediated iron redistribution in host defense, hepcidin production is regulated by inflammation as well. Increased hepcidin concentrations in plasma are pathogenic in iron-restrictive anemias including anemias associated with inflammation, chronic kidney disease and some cancers. Hepcidin deficiency causes iron overload in hereditary hemochromatosis and ineffective erythropoiesis. Hepcidin, ferroportin and their regulators represent potential targets for the diagnosis and treatment of iron disorders and anemias. This article is part of a Special Issue entitled: Cell Biology of Metals.
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Haem-bound iron is released from erythrocytes within macrophages by haem oxygenase (HO-1) and is further transported to the bone marrow for erythropoiesis via transferrin.
“Haem-bound iron is released from erythrocytes within macrophages by haem oxygenase (HO-1) and is further transported to the bone marrow for erythropoiesis via transferrin (Ganz and Nemeth, 2012).”
From Iron at the Centre of Candida albicans Interactions (2018) · cites this paper as Ganz and Nemeth, 2012
Section 2.1 says macrophages degrade old erythrocytes, return their iron to plasma transferrin, and that transferrin-bound iron is mostly destined for erythrocyte production in the bone marrow. Section 4.6 mentions heme degradation in macrophages and heme oxygenase-1, but does not state that HO-1 releases the iron from heme. That specific enzymatic step is not supported by our copy. (LLM, conf=0.86)
Experimental — accuracy not yet measuredDaily iron uptake from diet via duodenal enterocytes is minimal (1-2 mg per day) compared to daily iron requirements, especially for hemoglobin synthesis, which requires approximately 20−25 mg iron.
“Daily iron uptake from diet via duodenal enterocytes is minimal (1–2 mg per day) compared to daily iron requirements, especially for hemoglobin synthesis, which requires approximately 20−25 mg iron (Ganz and Nemeth, 2012).”
From Iron at the Centre of Candida albicans Interactions (2018) · cites this paper as Ganz and Nemeth, 2012
Hepcidin is a liver-derived hormone that regulates introduction of iron into plasma from three major sources: iron stored within hepatocytes, absorbed iron in the duodenal enterocytes, and iron recycled from macrophages.
“Hepcidin is a liver-derived hormone that regulates introduction of iron into plasma from three major sources: iron stored within hepatocytes, absorbed iron in the duodenal enterocytes and iron recycled from macrophages (Ganz and Nemeth, 2012; Pantopoulos et al., 2012).”
From Iron at the Centre of Candida albicans Interactions (2018) · cites this paper as Ganz and Nemeth, 2012
Hepcidin regulates cellular iron efflux via degradation of ferroportin 1, which induces cellular iron retention in macrophages and reduces duodenal iron absorption.
“Hepcidin regulates cellular iron efflux via degradation of the sole cellular iron exporter ferroportin 1 (FPN1), which induces cellular iron retention in macrophages and reduces duodenal iron absorption [5, 6].”
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- Authors
- Ganz, T., & Nemeth, E.
- Affiliations
- University of California, Los Angeles (US)
- Corresponding author
- Ganz, Tomas
- Venue
- Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
- Publisher
- Elsevier BV
- Published
- 2012-09
- Volume
- 1823
- Issue
- 9
- Pages
- 1434-1443
- ISSN
- 0167-4889 (ISSN-L)
- PMC
- PMC4048856
- OpenAlex
- W2028034405
- Cited by
- 1,282
- References
- 102
- Citations by year
- 2026: 86 · 2025: 72 · 2024: 70 · 2023: 88 · 2022: 103 · 2021: 120 · 2020: 111 · 2019: 103 · 2018: 113 · 2017: 76 · 2016: 88 · 2015: 78 · 2014: 88 · 2013: 66 · 2012: 18
- FWCI
- 12.66
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Biochimica et Biophysica Acta (BBA) - Molecular Cell Research (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK065029, R01DK082717)
- Topics
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Health Sciences › Medicine › Pulmonary and Respiratory Medicine › Ferroptosis and cancer prognosis
- Life Sciences › Neuroscience › Neurology › Neurological diseases and metabolism
- Keywords
- hepcidin, iron homeostasis, ferroportin, iron absorption, inflammation, iron overload, hereditary hemochromatosis, chronic kidney disease, BMP signaling, iron recycling
- MeSH terms
- Iron Deficiencies, Ferroportin, Animals, Cations, Divalent, Erythropoiesis, Homeostasis, Humans, Iron, Liver, Anemia, Iron-Deficiency, Iron Overload, Hepatocytes, Antimicrobial Cationic Peptides, Cation Transport Proteins, Bone Morphogenetic Protein Receptors, Hepcidins
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