Posttranslational processing of hepcidin in human hepatocytes is mediated by the prohormone convertase furin.
Open accessAbstract
Hepcidin is encoded as an 84 amino acid prepropeptide containing a typical N-terminal 24 amino acid endoplasmic reticulum targeting signal sequence, and a 35 amino acid proregion (pro) with a consensus furin cleavage site immediately followed by the C-terminal 25 amino acid bioactive iron-regulatory hormone (mature peptide). We performed pulse-chase studies of posttranslational processing of hepcidin in human hepatoma HepG2 cells and in primary human hepatocytes induced with bone morphogenic protein (BMP-9). In some experiments, the cells were treated with the furin protease inhibitor decanoyl-Arg-Val-Lys-Arg-chloromethylketone (CMK) or furin siRNA. In the absence of furin inhibitor, hepcidin was found to be processed in less than 1 h and secreted as a 3 kDa form reactive with anti-mature but not anti-pro antibody. In the presence of furin inhibitors or furin siRNA, a 6 kDa form reactive with both anti-pro and anti-mature antibody was rapidly secreted into the medium. Processing was not affected by inhibitors of the hypoxia inducible factor (HIF) pathway, or by treatment with 30 microM holo- or apo-transferrin. In conclusion, the hepatic prohormone convertase furin mediates the posttranslational processing of hepcidin. The proteolytic cleavage of prohepcidin to hepcidin is not regulated by iron-transferrin or the HIF pathway.
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Proteolytic processing of the hepcidin prohormone is carried out by furin in a relatively unregulated manner.
“Proteolytic processing of the prohormone is carried out by furin in a relatively unregulated manner.98”
From Forging a field: the golden age of iron biology. (2008) · cites this paper as [98]
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- Authors
- Valore, E. V., & Ganz, T.
- Affiliations
- University of California, Los Angeles (US)
- Corresponding author
- Ganz, Tomas
- ORCID
- Ganz, Tomas
- Venue
- Blood Cells Molecules and Diseases
- Publisher
- Elsevier BV
- Published
- 2008-01
- Volume
- 40
- Issue
- 1
- Pages
- 132-138
- ISSN
- 1079-9796 (ISSN-L)
- PMC
- PMC2211381
- OpenAlex
- W2054421541
- Cited by
- 234
- References
- 32
- Citations by year
- 2026: 2 · 2025: 3 · 2024: 8 · 2023: 1 · 2022: 5 · 2021: 11 · 2020: 9 · 2019: 15 · 2018: 14 · 2017: 11 · 2016: 11 · 2015: 9 · 2014: 10 · 2013: 19 · 2012: 15
- FWCI
- 15.62
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Blood Cells Molecules and Diseases (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK065029)
- Topics
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Life Sciences › Neuroscience › Neurology › Neurological diseases and metabolism
- Physical Sciences › Engineering › Mechanical Engineering › Iron and Steelmaking Processes
- Keywords
- hepcidin, furin, prohormone convertases, post-translational processing, prohepcidin, hepatocytes, BMP9, iron regulation, hypoxia-inducible factor, transferrin, proteolytic cleavage, HepG2 cells
- MeSH terms
- Humans, Peptide Fragments, Protein Processing, Post-Translational, Transferrin, Hepatocytes, Antimicrobial Cationic Peptides, Proprotein Convertases, Furin, Hypoxia-Inducible Factor 1, Hepcidins
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