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Posttranslational processing of hepcidin in human hepatocytes is mediated by the prohormone convertase furin.

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Valore, Erika V., Ganz, Tomas·2008·Blood Cells Molecules and Diseases

DOI 10.1016/j.bcmd.2007.07.009PMC PMC2211381

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Abstract

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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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)
DOI: 10.1016/j.bcmd.2007.07.009
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
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
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 › Materials Science › Metals and Alloys › 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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Posttranslational processing of hepcidin in human hepatocytes is mediated by the prohormone convertase furin.

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