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Gene Section
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FURIN (furin (paired basic amino acid cleaving
enzyme))
Abdel-Majid Khatib, Fatma Sfaxi
University Bordeaux 1, INSERM U1029, Avenue des Facultes, Batiment B2, Talence 33405, France (AMK,
FS)
Published in Atlas Database: April 2012
Online updated version : http://AtlasGeneticsOncology.org/Genes/FURINID40646ch15q26.html
DOI: 10.4267/2042/47533
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 2.0 France Licence.
© 2012 Atlas of Genetics and Cytogenetics in Oncology and Haematology
This protein is produced as a 104 kDa zymogen that is
converted into a 98 kDa mature following autocatalytic
cleavage at two sites.
The cleavages occur during enzyme progression from
the endoplasmic reticulum to the trans golgi network
(TGN).
Identity
Other names: FUR, PACE, PCSK3, SPC1
HGNC (Hugo): FURIN
Location: 15q26.1
DNA/RNA
Expression
Description
Expression of Furin in different tissues was localized
by northern blot, in situ hybridization and
histochemistry.
These analyses demonstrated that Furin is ubiquitously
expressed.
However, high expression of Furin was found in liver
and spleen.
This gene can be found on chromosome 15 at location:
89212826-89227692.
Transcription
The DNA sequence contains 16 exons and the
transcript length: 4244 bps translated to a 794 residues
protein.
Localisation
Protein
Furin cycle between the cell surface and the TGN.
Description
Function
Furin is a member of the family of subtilisin/kexin-like
proprotein convertases (PCs) that process protein at
basic residues.
Furin is involved in the activation of precursor proteins
by cleavage on a single or paired basic residue.
Atlas Genet Cytogenet Oncol Haematol. 2012; 16(9)
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FURIN (furin (paired basic amino acid cleaving enzyme))
Khatib AM, Sfaxi F
Precursors are usually cleaved at the general motif
(K/R)-(X)n-(K/R)↓, where n= 0, 2, 4 or 6. Furin
substrates include growth factors and their receptors
(such as pro-TGFb, pro-IGF-1, 2, pro-PDGF-A, B,
insulin-R, IGF1-R, R-PTPm, Notch), neurotrophins
(pro-NGF, -BDNF,- NT3), prohormones (pro-PTH,
pro-endothelin, proparathyroid hormone), blood
coagulation factors (pro-Von Willebrand Factor, proFactor VII, pro-Factor IX, pro-Factor X), integrins (α3,
α6, αv, α5 and α4 chains) and various
metalloendopeptidases
(stromelysin-3,
ADAM,
ADAMTS, MT1-MMP). The activation of these
substrates by Furin, implicated directly the latter to cell
proliferation, survival, migration, invasion and
homeostasis.
cell lines as well as ovarian epithelial cancer specimens
revealed that Furin is only expressed in cancer cell
lines especially in primary tumors from patients whose
life expectancy don't exceed five years.
Oral tongue squamous cell carcinoma
Note
The Furin expression was found to be correlated with
the grade of oral tongue squamous carcinoma. The
highest Furin expression was found in the most
aggressive line of squamous cell carcinoma (SCC) and
the least Furin expression in the less aggressive line.
Breast cancer
Note
Furin was shown to be overexpressed in breast cancer
cell lines and breast tumor tissues.
Homology
The Furin catalytic domain has a high percentage of
homology with those of the other PCs which range
from 70% (between PACE4 and Furin) to 54%
(between PC2 and Furin).
Viral infections
Note
By activating various viral envelope glycoproteins,
Furin is involved in numerous viral infections. These
include HIV-gp160, RSV-Pr95env, NDV-F, Influenza
haemagglutinin-HA, CMV-gB, SFV-p62.
Implicated in
Cancer
Bacterial infections
Note
To date Furin is expressed in all tissues and cell lines
examined so far but at very low levels as compared to
tumor cells and tissues. Inhibition of Furin activity or
expression in tumor cells reduced dramatically their
malignant
phenotype
(proliferation,
invasion,
migration...) and their ability to induce tumor growth.
Note
The involvement of Furin in bacterial infections was
suggested by its capacity to activate the various classes
of bacterial toxins such as the Diphteria toxin,
Pseudomonas Aerugenosa exotoxin A, Botulinum
neurotoxin, Bordetella dermonecrotic toxin, Anthrax
and aerolysin.
Head and neck squamous cell
carcinomas (HNSCCs)
Neurodegenerative pathology
Note
Furin can activate the α and β-secretase which are
implicated in the cleavage of amyloid-β the principal
component of senile plaques.
Note
While Furin expression is undetectable in non
metastasing head and neck squamous cell carcinomas
its overexpressed in more aggressive lines.
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FURIN (furin (paired basic amino acid cleaving enzyme))
Khatib AM, Sfaxi F
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Atlas Genet Cytogenet Oncol Haematol. 2012; 16(9)
This article should be referenced as such:
Khatib AM, Sfaxi F. FURIN (furin (paired basic amino acid
cleaving enzyme)). Atlas Genet Cytogenet Oncol Haematol.
2012; 16(9):639-643.
643