Ironing out Ferroportin
Open accessAbstract
Maintaining physiologic iron concentrations in tissues is critical for metabolism and host defense. Iron absorption in the duodenum, recycling of iron from senescent erythrocytes, and iron mobilization from storage in macrophages and hepatocytes constitute the major iron flows into plasma for distribution to tissues, predominantly for erythropoiesis. All iron transfer to plasma occurs through the iron exporter ferroportin. The concentration of functional membrane-associated ferroportin is controlled by its ligand, the iron-regulatory hormone hepcidin, and fine-tuned by regulatory mechanisms serving iron homeostasis, oxygen utilization, host defense, and erythropoiesis. Fundamental questions about the structure and biology of ferroportin remain to be answered.
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Aberrant ferroportin activity can lead to diseases of iron overload, like hemochromatosis, or iron limitation anemias.
“Aberrant ferroportin activity can lead to diseases of iron overload, like hemochromatosis, or iron limitation anemias 2 .”
From Structure of hepcidin-bound ferroportin reveals iron homeostatic mechanisms (2020) · cites this paper as [2]
The section on genetic disorders of ferroportin reports that gain-of-function mutations cause iron overload resembling classical hemochromatosis. It also reports iron restriction and hypochromic erythrocytes in a mouse model with a ferroportin mutation, but does not establish iron-limitation anemia as a disease caused by aberrant ferroportin activity; it says patients with loss-of-function mutations generally avoid systemic iron deficiency unless phlebotomized. Page numbers are unavailable in our copy. (LLM, conf=0.83)
Experimental — accuracy not yet measuredIn mammals, iron levels are regulated by hepcidin acting on ferroportin, the only known iron efflux transporter.
“In mammals, iron levels are regulated by the action of hepcidin, a peptide hormone, on ferroportin (FPN), the only known iron efflux transporter 2-4 (Fig. 1a).”
From Structure of hepcidin-bound ferroportin reveals iron homeostatic mechanisms (2020) · cites this paper as [2]
The cryo-EM density map of FPN enabled building of an atomic model of FPN regions important for iron transport and hepcidin binding and a portion of ICL3 important in hepcidin-induced FPN internalization.
“The cryo-EM density map of FPN enabled building of an atomic model of FPN regions important for iron transport and hepcidin binding 2,7 , and a portion of the intracellular loop 3 (ICL3) important in hepcidin-induced FPN internalization 8-10 (Extended Data Fig. 5).”
From Structure of hepcidin-bound ferroportin reveals iron homeostatic mechanisms (2020) · cites this paper as [2]
FPN abundance is controlled at transcriptional, posttranscriptional, and posttranslational stages.
“The expression of FPN is tightly regulated at the transcriptional, posttranscriptional, and posttranslational levels.8”
From RNF217 regulates iron homeostasis through its E3 ubiquitin ligase activity by modulating ferroportin degradation (2021) · cites this paper as [8]
In duodenal enterocytes, Fpn transcription is regulated by iron and hypoxia to increase dietary iron absorption during iron deficiency and anemia.
“In duodenal enterocytes, transcription of the Fpn gene, which encodes ferroportin, is regulated by iron and hypoxia to increase the absorption of dietary iron during iron deficiency and anemia.8,54”
From RNF217 regulates iron homeostasis through its E3 ubiquitin ligase activity by modulating ferroportin degradation (2021) · cites this paper as [8]
FPN expression is tightly controlled at transcriptional and/or translational levels, allowing diverse physiological effects to influence FPN activity at its various sites.
“Taken together, these data support that FPN expression is tightly controlled at both transcriptional and/or the translational levels,8,68,69 which allow multiple and diverse physiological effects to influence FPN activity at its various sites of expression.”
From RNF217 regulates iron homeostasis through its E3 ubiquitin ligase activity by modulating ferroportin degradation (2021) · cites this paper as [8]
On average, humans ingest 20-25 mg of iron per day, the majority of which is inorganic iron (85%-90%), followed by haem-bound iron (10%-15%).
“On average, humans ingest 20–25 mg of iron/day, the majority of which is inorganic iron (85%–90%), followed by haem‐bound iron (10%–15%).”
From The battle for iron in enteric infections (2020) · cites this paper as [9]
In mammals, excretion of iron is not extensively regulated; instead, iron homeostasis is achieved mainly by regulating intestinal absorption in the duodenum, and possibly in the colon to some extent.
“In mammals, excretion of iron is not extensively regulated; instead, iron homeostasis is achieved mainly by regulating intestinal absorption in the duodenum, 9 and possibly in the colon to some extent. 10”
From The battle for iron in enteric infections (2020) · cites this paper as [9]
Only about 1 mg of iron is absorbed per day, because of both poor iron bioavailability and tightly regulated iron homeostasis.
“However, only ~ 1 mg iron is absorbed per day, because of both poor iron bioavailability and tightly regulated iron homeostasis. 9 , 11”
From The battle for iron in enteric infections (2020) · cites this paper as [9]
In conditions of iron accumulation, HAMP production is stimulated, and iron is subsequently trapped within enterocytes and macrophages, respectively inhibiting iron export to circulation or preventing recycling of iron derived from red blood cells.
“In conditions of iron accumulation, the production of HAMP is stimulated, and, as a result, iron is subsequently trapped within enterocytes and macrophages, respectively inhibiting iron export to circulation or preventing recycling of iron derived from red blood cells. 9”
From The battle for iron in enteric infections (2020) · cites this paper as [9]
Hepcidin limits iron fluxes to the bloodstream by promoting degradation of the iron exporter ferroportin in target cells.
“The iron regulatory hormone hepcidin limits iron fluxes to the bloodstream by promoting degradation of the iron exporter ferroportin in target cells.”
From Pharmacological Targeting of the Hepcidin/Ferroportin Axis (2016) · cites this paper as Drakesmith et al., 2015
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“However, the degree and duration of hypoferremia caused by this inflammatory suppression of Fpn1 mRNA are relatively minor in the absence of hepcidin, as evidenced by the small effects on circulating iron after infection with extracellular bacteria in hepcidin knockout mice (Arezes et al., 2015).”
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- Authors
- Drakesmith, H., Nemeth, E., & Ganz, T.
- Affiliations
- University of Oxford (GB)
- University of California, Los Angeles (US)
- Corresponding author
- Ganz, Tomas
- Venue
- Cell Metabolism
- Publisher
- Elsevier BV
- Published
- 2015-11
- Volume
- 22
- Issue
- 5
- Pages
- 777-787
- ISSN
- 1550-4131 (ISSN-L)
- PMC
- PMC4635047
- OpenAlex
- W2174098335
- Cited by
- 638
- References
- 110
- Citations by year
- 2026: 35 · 2025: 64 · 2024: 68 · 2023: 76 · 2022: 75 · 2021: 67 · 2020: 86 · 2019: 52 · 2018: 54 · 2017: 33 · 2016: 24 · 2015: 1 · 2012: 1
- FWCI
- 5.59
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell Metabolism (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- Funders
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK065029, R01DK090554, R01DK107309)
- 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
- ferroportin, hepcidin, iron homeostasis, iron absorption, erythropoiesis, iron recycling, iron storage, iron export, membrane protein structure, host defense, oxygen utilization
- MeSH terms
- Ferroportin, Animals, Erythrocytes, Erythropoiesis, Homeostasis, Humans, Iron, Macrophages, Hepatocytes, Cation Transport Proteins, Hepcidins
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