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Cited by 234Iron Metabolism and DisordersNeurological diseases and metabolismIron and Steelmaking Processes

The DOI matches its Crossref record; 31 of the 32 references it cites were found in a registry or an index.

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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Metadata

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
Licence
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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