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Furin-mediated release of soluble hemojuvelin: a new link between hypoxia and iron homeostasis
Open accessAbstract
The liver peptide hepcidin regulates iron absorption and recycling. Hemojuvelin (HJV) has a key role in hepcidin regulation, and its inactivation causes severe iron overload both in humans and in mice. Membrane HJV (m-HJV) acts as a coreceptor for bone morphogenetic proteins (BMPs), whereas soluble HJV (s-HJV) may down-regulate hepcidin in a competitive way interfering with BMP signaling. s-HJV is decreased by iron in vitro and increased by iron deficiency in vivo. However, the mechanisms regulating the 2 HJV isoforms remain unclear. Here we show that s-HJV originates from a furin cleavage at position 332-335. s-HJV is reduced in the cleavage mutant R335Q as well as in cells treated with a furin inhibitor, and increased in cells overexpressing exogenous furin, but not in cells overexpressing an inactive furin variant. Furin is up-regulated by iron deficiency and hypoxia in association with the stabilization of HIF-1alpha. Increased s-HJV in response to HIF-1alpha occurs during differentiation of murine muscle cells expressing endogenous Hjv. Our data are relevant to the mechanisms that relate iron metabolism to the hypoxic response. The release of s-HJV might be a tissue-specific mechanism, signaling the local iron requests of hypoxic skeletal muscles independently of the oxygen status of the liver.
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“In hypoxia hepcidin is also suppressed in vitro by soluble hemojuvelin, released by furin,53 an effect unclear in vivo, and by platelet-derived growth factor-BB in volunteers exposed to hypoxia.54”
From Iron metabolism and iron disorders revisited in the hepcidin era (2020) · cites this paper as [53]
In the citing paper
“Recent in vivo studies have shown that HIF induces furin, a proprotein convertase that cleaves HJV and generates a soluble form of HJV, which suppresses hepcidin by antagonizing BMP6 signaling.”
From Regulation of erythropoiesis by hypoxia-inducible factors (2013) · cites this paper as [203]
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Hanudel, M. R., & Salusky, I. B. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-818036-5.00006-9
Impact of the UPR on the expression of relevant genes for cellular iron metabolism
Oliveira, S. J. (2011)
Metadata
- Authors
- Silvestri, L., Pagani, A., & Camaschella, C.
- Affiliations
- Vita-Salute San Raffaele University (IT)
- Venue
- Blood
- Publisher
- American Society of Hematology
- Published
- 2008-01-15
- Volume
- 111
- Issue
- 2
- Pages
- 924-931
- ISSN
- 0006-4971 (ISSN-L)
- 1528-0020
- OpenAlex
- W2005438156
- Cited by
- 311
- References
- 36
- Citations by year
- 2026: 1 · 2025: 4 · 2024: 11 · 2023: 3 · 2022: 10 · 2021: 18 · 2020: 12 · 2019: 16 · 2018: 16 · 2017: 16 · 2016: 13 · 2015: 17 · 2014: 16 · 2013: 27 · 2012: 20
- FWCI
- 17.97
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Blood (publishedVersion)
- PubMed (publishedVersion)
- INFM-OAR (INFN Catania) (submittedVersion, other-oa)
- 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
- hemojuvelin, furin, proteolytic cleavage, hypoxia, iron homeostasis, hepcidin, HIF-1α, iron deficiency, BMP signaling, skeletal muscle, myogenesis, iron overload
- MeSH terms
- Hemochromatosis Protein, Iron Deficiencies, Animals, Cell Differentiation, HeLa Cells, Homeostasis, Humans, Iron, Liver, Membrane Proteins, Organ Specificity, Oxygen, Signal Transduction, Down-Regulation, Cell Hypoxia, Muscle, Skeletal, Iron Overload, Bone Morphogenetic Proteins, Amino Acid Substitution, Protein Isoforms, Mutation, Missense, Antimicrobial Cationic Peptides, Muscle Cells, Furin, Mice, Hypoxia-Inducible Factor 1, alpha Subunit, GPI-Linked Proteins, Hepcidins
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