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Hypoxia-inducible factor regulates hepcidin via erythropoietin-induced erythropoiesis
Open accessAbstract
Iron demand in bone marrow increases when erythropoiesis is stimulated by hypoxia via increased erythropoietin (EPO) synthesis in kidney and liver. Hepcidin, a small polypeptide produced by hepatocytes, plays a central role in regulating iron uptake by promoting internalization and degradation of ferroportin, the only known cellular iron exporter. Hypoxia suppresses hepcidin, thereby enhancing intestinal iron uptake and release from internal stores. While HIF, a central mediator of cellular adaptation to hypoxia, directly regulates renal and hepatic EPO synthesis under hypoxia, the molecular basis of hypoxia/HIF-mediated hepcidin suppression in the liver remains unclear. Here, we used a genetic approach to disengage HIF activation from EPO synthesis and found that HIF-mediated suppression of the hepcidin gene (Hamp1) required EPO induction. EPO induction was associated with increased erythropoietic activity and elevated serum levels of growth differentiation factor 15. When erythropoiesis was inhibited pharmacologically, Hamp1 was no longer suppressed despite profound elevations in serum EPO, indicating that EPO by itself is not directly involved in Hamp1 regulation. Taken together, we provide in vivo evidence that Hamp1 suppression by the HIF pathway occurs indirectly through stimulation of EPO-induced erythropoiesis.
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In the citing paper
“studies in humans receiving recombinant EPO have not yet shown a significant inverse relationship between serum hepcidin and GDF15 levels”
From Regulation of erythropoiesis by hypoxia-inducible factors (2013) · cites this paper as [208]
In the citing paper
“Hepcidin suppression under conditions of hypoxia and hepatic HIF activation was dependent on erythropoietic activity in the bone marrow.”
From Regulation of erythropoiesis by hypoxia-inducible factors (2013) · cites this paper as [208]
In the citing paper
“We found that recombinant murine GDF15 suppressed hepcidin in Hep3B cells at a concentration of 750 pg/ml.”
From Regulation of erythropoiesis by hypoxia-inducible factors (2013) · cites this paper as [208]
In the citing paper
“found that hypoxia/HIF-mediated suppression of hepcidin required EPO.”
From Regulation of erythropoiesis by hypoxia-inducible factors (2013) · cites this paper as [208]
In the citing paper
“However, we determined that the induction of EPO synthesis alone was not sufficient to suppress hepcidin in this model.”
From Regulation of erythropoiesis by hypoxia-inducible factors (2013) · cites this paper as [208]
In the citing paper
“The latter, however, is most likely a reflection of increased erythropoietic activity.”
From Regulation of erythropoiesis by hypoxia-inducible factors (2013) · cites this paper as [208]
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Citations
Cites
Oxygen sensing by metazoans: the central role of the HIF hydroxylase pathway.
Kaelin, W. G., & Ratcliffe, P. J. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.04.009 · Cited by 3,251 · cited 6×
“The activity of HIF is controlled by O 2 -, iron, and ascorbate-dependent dioxygenases, also known as prolyl-hydroxy-lase domain–containing proteins 1–3 (PHD1–3), which use 2-oxo-glutarate as substrate for the hydroxylation of specific proline residues in HIF-α .”
InfluentialSimplified mammalian DNA isolation procedure
Laird, P. W., Zijderveld, A., Linders, K., Rudnicki, M. A., Jaenisch, R., & Berns, A. J. M. (1991) · Nucleic Acids Research · doi:10.1093/nar/19.15.4293 · Cited by 1,497
Nicolas, G., Chauvet, C., Viatte, L., Danan, J. L., Bigard, X., Devaux, I., Beaumont, C., Kahn, A., & Vaulont, S. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0215686 · Cited by 1,214
Bone morphogenetic protein signaling by hemojuvelin regulates hepcidin expression
Babitt, J. L., Huang, F. W., Wrighting, D. M., Xia, Y., Sidis, Y., Samad, T. A., Campagna, J. A., Chung, R. T., Schneyer, A. L., Woolf, C. J., et al. (2006) · Nature Genetics · doi:10.1038/ng1777 · Cited by 1,026 · cited 1×
“…transferrin receptor 1 (TRFC) and transferrin receptor 2 (TFR2) (2, 11, 12), or hemojuvelin (HJV), which acts as a coreceptor for bone morphogenetic protein 6 (BMP6), increases hepcidin expression in a mothers against decapen-taplegic homolog–dependent (SMAD-dependent) fashion (13–15).”
High levels of GDF15 in thalassemia suppress expression of the iron regulatory protein hepcidin
Tanno, T., Bhanu, N. V., Oneal, P. A., Goh, S.-H., Staker, P., Lee, Y. T., Moroney, J. W., Reed, C. H., Luban, N. L., Wang, R.-H., et al. (2007) · Nature Medicine · doi:10.1038/nm1629 · Cited by 854
Ruzankina, Y., Pinzon‐Guzman, C., Asare, A., Ong, T., Pontano, L. L., Cotsarelis, G., Zediak, V. P., Velez, M., Bhandoola, A., & Brown, E. J. (2007) · Cell stem cell · doi:10.1016/j.stem.2007.03.002 · Cited by 803
BMP6 is a key endogenous regulator of hepcidin expression and iron metabolism
Andriopoulos Jr, B., Corradini, E., Xia, Y., Faasse, S. A., Chen, S., Grgurevic, L., Knutson, M. D., Pietrangelo, A., Vukicevic, S., Lin, H. Y., et al. (2009) · Nature Genetics · doi:10.1038/ng.335 · Cited by 769
High-resolution genome-wide mapping of HIF-binding sites by ChIP-seq
Schödel, J., Oikonomopoulos, S., Ragoussis, J., Pugh, C. W., Ratcliffe, P. J., & Mole, D. R. (2011) · Blood · doi:10.1182/blood-2010-10-314427 · Cited by 724
Regulation of iron homeostasis by the hypoxia-inducible transcription factors (HIFs)
Peyssonnaux, C., Zinkernagel, A. S., Schuepbach, R. A., Rankin, E., Vaulont, S., Haase, V. H., Nizet, V., & Johnson, R. S. (2007) · Journal of Clinical Investigation · doi:10.1172/jci31370 · Cited by 639
Self-citationForging a field: the golden age of iron biology.
Andrews, N. C. (2008) · Blood · doi:10.1182/blood-2007-12-077388 · Cited by 623
Research works printed but not linked: 2
- Tanno, 2010, Curr Opin Hematol., 17, 184
- Hickey, 2007, J Clin Invest., 12, 3879
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Ganz, T. (2013) · Physiological Reviews · doi:10.1152/physrev.00008.2013 · Cited by 1,122
Identification of erythroferrone as an erythroid regulator of iron metabolism
Kautz, L., Jung, G., Valore, E. V., Rivella, S., Nemeth, E., & Ganz, T. (2014) · Nature Genetics · doi:10.1038/ng.2996 · Cited by 1,127
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Haase, V. H. (2013) · Blood Reviews · doi:10.1016/j.blre.2012.12.003 · Cited by 787
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Self-citationZhao, N., Zhang, A., & Enns, C. A. (2013) · Journal of Clinical Investigation · doi:10.1172/jci67225 · Cited by 215
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Haase, V. H. (2021) · Kidney International Supplements · doi:10.1016/j.kisu.2020.12.002 · Cited by 200
Self-citationIron Balance and the Role of Hepcidin in Chronic Kidney Disease
Ganz, T., & Nemeth, E. (2016) · Seminars in Nephrology · doi:10.1016/j.semnephrol.2016.02.001 · Cited by 195
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Shah, Y. M., & Xie, L. (2014) · Gastroenterology · doi:10.1053/j.gastro.2013.12.031 · Cited by 187
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Self-citationIron Status and the Acute Post-Exercise Hepcidin Response in Athletes
Peeling, P., Sim, M., Badenhorst, C. E., DAWSON, B. T., Govus, A. D., Abbiss, C. R., Swinkels, D. W., & Trinder, D. (2014) · PLoS ONE · doi:10.1371/journal.pone.0093002 · Cited by 171
Marques, O., Weiß, G., & Muckenthaler, M. U. (2022) · Blood · doi:10.1182/blood.2021013472 · Cited by 176
HIF‐prolyl hydroxylases as therapeutic targets in erythropoiesis and iron metabolism
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Pasricha, S., Frazer, D. M., Bowden, D. K., & Anderson, G. J. (2013) · Blood · doi:10.1182/blood-2012-12-471441 · Cited by 156
Sugahara, M., Tanaka, T., & Nangaku, M. (2017) · Kidney International · doi:10.1016/j.kint.2017.02.035 · Cited by 151
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Sonnweber, T., Nachbaur, D., Schroll, A., Nairz, M., Seifert, M., Demetz, E., Haschka, D., Mitterstiller, A.-M., Kleinsasser, A., Burtscher, M., et al. (2014) · Gut · doi:10.1136/gutjnl-2013-305317 · Cited by 145
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Shenoy, N. K., Vallumsetla, N., Rachmilewitz, E. A., Verma, A., & Ginzburg, Y. Z. (2014) · Blood · doi:10.1182/blood-2014-03-563221 · Cited by 128
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Abnormal erythropoiesis and the pathophysiology of chronic anemia
Koury, M. J. (2014) · Blood Reviews · doi:10.1016/j.blre.2014.01.002 · Cited by 98
Ariazi, J. L., Duffy, K. J., Adams, D. F., Fitch, D. M., Luo, L., Pappalardi, M. B., Biju, M. P., DiFilippo, E. H., Shaw, T., Wiggall, K., et al. (2017) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.117.242503 · Cited by 94
Zhang, J., Wang, Y., Fan, M., Guan, Y., Zhang, W., Huang, F., Zhang, Z., Li, X., Yuan, B., Liu, W., et al. (2024) · Cell Metabolism · doi:10.1016/j.cmet.2024.05.008 · Cited by 94
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Zumbrennen‐Bullough, K. B., & Babitt, J. L. (2013) · Nephrology Dialysis Transplantation · doi:10.1093/ndt/gft443 · Cited by 82
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Vyoral, D., & Petrák, J. (2016) · Pharmacological Research · doi:10.1016/j.phrs.2016.11.010 · Cited by 79
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Finberg, K. E. (2013) · Current Opinion in Hematology · doi:10.1097/moh.0b013e32835f5a47 · Cited by 72
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Tojo, Y., Sekine, H., Hirano, I., Pan, X., Souma, T., Tsujita, T., Kawaguchi, S., Takeda, N., Takeda, K., Fong, G., et al. (2015) · Molecular and Cellular Biology · doi:10.1128/mcb.00161-15 · Cited by 72
Semenza, G. L. (2022) · Annual Review of Medicine · doi:10.1146/annurev-med-042921-102602 · Cited by 74
Renal epithelium regulates erythropoiesis via HIF-dependent suppression of erythropoietin
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Self-citationKong, W.-N., Gao, G., & Chang, Y.-Z. (2014) · Cell & Bioscience · doi:10.1186/2045-3701-4-19 · Cited by 71
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Liang, R. H.-S., & Ghaffari, S. (2016) · British Journal of Haematology · doi:10.1111/bjh.14194 · Cited by 69
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“Nevertheless, the hypoxia-inducible factor may be stimulated by different signaling mechanisms [130], and potentially have an EPO-independent effect on hepcidin production [126,131].”
BackgroundTherapeutic Advances in Regulating the Hepcidin/Ferroportin Axis
Hawula, Z. J., Wallace, D. F., Subramaniam, V. N., & Rishi, G. (2019) · Pharmaceuticals · doi:10.3390/ph12040170 · Cited by 62
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Haase, V. H. (2017) · Experimental Cell Research · doi:10.1016/j.yexcr.2017.05.004 · Cited by 65
Self-citationHypoxia-inducible factor stabilizers for treating anemia of chronic kidney disease
Hasegawa, S., Tanaka, T., & Nangaku, M. (2018) · Current Opinion in Nephrology & Hypertension · doi:10.1097/mnh.0000000000000431 · Cited by 63
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Solberg, A., & Reikvam, H. (2023) · Life · doi:10.3390/life13102007 · Cited by 57
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Sonnweber, T., Pizzini, A., Tancevski, I., Löffler‐Ragg, J., & Weiß, G. (2020) · Internal and Emergency Medicine · doi:10.1007/s11739-020-02288-1 · Cited by 59
Fandrey, J., Schödel, J., Eckardt, K., Katschinski, D. M., & Wenger, R. H. (2019) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-019-02334-8 · Cited by 54
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Agarwal, A. K. (2021) · Kidney International Supplements · doi:10.1016/j.kisu.2020.12.003 · Cited by 57
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Borawski, B., & Małyszko, J. (2020) · Advances in Medical Sciences · doi:10.1016/j.advms.2020.06.004 · Cited by 54
Locatelli, F., Minutolo, R., Nicola, L. D., & Vecchio, L. D. (2022) · Drugs · doi:10.1007/s40265-022-01783-3 · Cited by 53
Langer, A. L., & Ginzburg, Y. Z. (2017) · Hemodialysis International · doi:10.1111/hdi.12543 · Cited by 57
Cui, R., Gale, R. P., Zhu, G., Xu, Z., Qin, T., Zhang, Y., Huang, G., Li, B., Fang, L., Zhang, H., et al. (2014) · Leukemia Research · doi:10.1016/j.leukres.2014.01.016 · Cited by 52
Hypoxia-inducible factor stabilisers for the anaemia of chronic kidney disease
Natale, P., Palmer, S. C., Jauré, A., Hodson, E. M., Ruospo, M., Cooper, T. E., Hahn, D., Saglimbene, V. M., Craig, J. C., & Strippoli, G. F. (2022) · Cochrane Database of Systematic Reviews · doi:10.1002/14651858.cd013751.pub2 · Cited by 50
Yun, S., & Vincelette, N. D. (2015) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2015.02.006 · Cited by 52
Shanmugam, N. K. N., Trebicka, E., Fu, L.-L., Shi, H. N., & Cherayil, B. J. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1400278 · Cited by 49
Sugahara, M., Tanaka, T., & Nangaku, M. (2022) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2022.108272 · Cited by 53
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Galliera, E., Lombardi, G., Marazzi, M. G., Grasso, D., Vianello, E., Pozzoni, R., Banfi, G., & Romanelli, M. M. C. (2014) · Scandinavian Journal of Clinical and Laboratory Investigation · doi:10.3109/00365513.2014.905697 · Cited by 45
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Self-citationCystathionine β‐synthase is required for body iron homeostasis
Zhou, Y., Wu, X., Zhou, G., Mu, M., Zhang, F., Li, F., Qian, C., Du, F., Yung, W., Qian, Z., et al. (2017) · Hepatology · doi:10.1002/hep.29499 · Cited by 45
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Landau, D., London, L., Bandach, I., & Segev, Y. (2018) · PLoS ONE · doi:10.1371/journal.pone.0196684 · Cited by 45
Theurl, M., Nairz, M., Schroll, A., Sonnweber, T., Asshoff, M., Haschka, D., Seifert, M., Willenbacher, W., Wilflingseder, D., Posch, W., et al. (2014) · Haematologica · doi:10.3324/haematol.2013.099481 · Cited by 42
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Metadata
- Authors
- Liu, Q., Davidoff, O., Niss, K., & Haase, V. H.
- Affiliations
- Vanderbilt University (US)
- MilliporeSigma (United States) (US)
- Corresponding author
- Haase, Volker H.
- ORCID
- Haase, Volker H.
- Venue
- Journal of Clinical Investigation
- Published
- 2012-11-01
- Volume
- 122
- Issue
- 12
- Pages
- 4635-4644
- ISSN
- 0021-9738 (ISSN-L)
- PMC
- PMC3533545
- OpenAlex
- W2002549547
- Cited by
- 328
- References
- 51
- Citations by year
- 2026: 10 · 2025: 18 · 2024: 18 · 2023: 26 · 2022: 40 · 2021: 25 · 2020: 28 · 2019: 19 · 2018: 22 · 2017: 28 · 2016: 28 · 2015: 20 · 2014: 29 · 2013: 16
- FWCI
- 13.86
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Journal of Clinical Investigation (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (R01-DK080821)
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK080821, R01DK081646, P30DK020593)
- Topics
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Health Sciences › Medicine › Hematology › Erythropoietin and Anemia Treatment
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Hemoglobin structure and function
- Keywords
- hypoxia-inducible factor, hepcidin, erythropoietin, erythropoiesis, iron metabolism, ferroportin, growth differentiation factor 15, hypoxia, iron absorption, liver
- MeSH terms
- Endothelial PAS Domain-Containing Protein 1, Animals, Erythropoiesis, Erythropoietin, Gene Expression Regulation, Humans, Liver, Procollagen-Proline Dioxygenase, Gene Expression, Mice, Knockout, Hepatocytes, Antimicrobial Cationic Peptides, Cell Line, Tumor, Mice, Basic Helix-Loop-Helix Proteins, Basic Helix-Loop-Helix Transcription Factors, Von Hippel-Lindau Tumor Suppressor Protein, Hypoxia-Inducible Factor 1, alpha Subunit, Growth Differentiation Factor 15, Hepcidins, Hypoxia-Inducible Factor-Proline Dioxygenases
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