HIF-2α, but not HIF-1α, promotes iron absorption in mice
Open accessAbstract
HIF transcription factors (HIF-1 and HIF-2) are central mediators of cellular adaptation to hypoxia. Because the resting partial pressure of oxygen is low in the intestinal lumen, epithelial cells are believed to be mildly hypoxic. Having recently established a link between HIF and the iron-regulatory hormone hepcidin, we hypothesized that HIFs, stabilized in the hypoxic intestinal epithelium, may also play critical roles in regulating intestinal iron absorption. To explore this idea, we first established that the mouse duodenum, the site of iron absorption in the intestine, is hypoxic and generated conditional knockout mice that lacked either Hif1a or Hif2a specifically in the intestinal epithelium. Using these mice, we found that HIF-1alpha was not necessary for iron absorption, whereas HIF-2alpha played a crucial role in maintaining iron balance in the organism by directly regulating the transcription of the gene encoding divalent metal transporter 1 (DMT1), the principal intestinal iron transporter. Specific deletion of Hif2a led to a decrease in serum and liver iron levels and a marked decrease in liver hepcidin expression, indicating the involvement of an induced systemic response to counteract the iron deficiency. This finding may provide a basis for the development of new strategies, specifically in targeting HIF-2alpha, to improve iron homeostasis in patients with iron disorders.
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HIF-2α is a central non-redundant regulator of erythropoiesis by inducing kidney EPO and promoting gut iron uptake, supporting erythroid progenitor maturation and proliferation.
“HIF-2α is a central non-redundant regulator of erythropoiesis by inducing erythropoietin (EPO) production by the kidney, and promoting iron uptake in the gut, which facilitates erythroid progenitor maturation and proliferation [21].”
From The HIF Axes in Cancer - Angiogenesis, Metabolism and Immune-Modulation (2025) · cites this paper as [21]
The Abstract reports that intestinal HIF-2α is crucial for iron absorption in mice, and the Introduction describes HIF-2α as important in adult erythropoiesis and dominant in regulating EPO expression. The Results report increased kidney EPO after intestinal Hif2a deletion, but do not establish that HIF-2α induces kidney EPO. The copy also does not address erythroid progenitor maturation or proliferation. (LLM, conf=0.88)
Experimental — accuracy not yet measuredAnaerobic glycolysis is predominantly controlled by HIF-1, whereas EPO synthesis and iron metabolism are HIF-2-regulated processes.
“For example, anaerobic glycolysis appears to be predominantly controlled by HIF-1, 68 whereas EPO synthesis and iron metabolism have emerged as HIF-2-regulated processes. 24, 69–73”
From Regulation of erythropoiesis by hypoxia-inducible factors (2013) · cites this paper as [73]
HIF-2 directly regulates DMT1 and duodenal cytochrome b (DCYTB).
“it furthermore plays a critical role in iron uptake and utilization as it directly regulates DMT1 and duodenal cytochrome b (DCYTB)”
From Regulation of erythropoiesis by hypoxia-inducible factors (2013) · cites this paper as [73]
HIF-2 is the key regulator of renal and hepatic EPO production.
“HIF-2 has not only emerged as the key regulator of renal and hepatic EPO production”
From Regulation of erythropoiesis by hypoxia-inducible factors (2013) · cites this paper as [73]
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Chiabrando, D., Fiorito, V., Marro, S., Silengo, L., Altruda, F., & Tolosano, E. (2013) · Blood Cells, Molecules, and Diseases · doi:10.1016/j.bcmd.2012.08.002 · Cited by 24 · see citing works
Investigating the real role of HIF-1 and HIF-2 in iron recycling by macrophages
Mathieu, J. R. R., Heinis, M., Zumerle, S., Delga, S., Le Bon, A., & Peyssonnaux, C. (2014) · Haematologica · doi:10.3324/haematol.2013.102319 · Cited by 22 · see citing works
Self-citationProlyl hydroxylase domain-2 (PHD2) inhibition may be a better therapeutic strategy in renal anemia
Soni, H. (2014) · Medical Hypotheses · doi:10.1016/j.mehy.2014.02.008 · Cited by 21 · see citing works
- Authors
- Mastrogiannaki, M., Matak, P., Keith, B., Simon, M. C., Vaulont, S., & Peyssonnaux, C.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- Abramson Cancer Center (US)
- Corresponding author
- Peyssonnaux, Carole
- Venue
- Journal of Clinical Investigation
- Published
- 2009-05-01
- Volume
- 119
- Issue
- 5
- Pages
- 1159-1166
- ISSN
- 0021-9738 (ISSN-L)
- PMC
- PMC2673882
- OpenAlex
- W2147160899
- Cited by
- 502
- References
- 38
- Citations by year
- 2026: 19 · 2025: 25 · 2024: 25 · 2023: 17 · 2022: 33 · 2021: 18 · 2020: 38 · 2019: 12 · 2018: 26 · 2017: 23 · 2016: 22 · 2015: 30 · 2014: 30 · 2013: 52 · 2012: 38
- FWCI
- 28.77
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Clinical Investigation (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Institut National de la Santé et de la Recherche Médicale
- Topics
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Health Sciences › Medicine › Hematology › Erythropoietin and Anemia Treatment
- Health Sciences › Medicine › Pulmonary and Respiratory Medicine › Ferroptosis and cancer prognosis
- Keywords
- HIF-2α, HIF-1α, intestinal iron absorption, iron homeostasis, hepcidin, DMT1, duodenum, conditional knockout mice, iron deficiency
- MeSH terms
- Iron Deficiencies, Ferroportin, Endothelial PAS Domain-Containing Protein 1, Solute Carrier Family 11, Member 2, Animals, Duodenum, Erythrocytes, Gene Expression Regulation, Hemoglobins, Humans, Intestinal Absorption, Iron, Liver, Mice, Inbred C57BL, Mice, Transgenic, Promoter Regions, Genetic, Protein Binding, Transcriptional Activation, Cell Hypoxia, Gene Expression, Caco-2 Cells, Response Elements, Antimicrobial Cationic Peptides, Cation Transport Proteins, Cytochromes b, Mice, Basic Helix-Loop-Helix Proteins, Hypoxia-Inducible Factor 1, alpha Subunit, Hepcidins
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