FURIN binds furin inhibitors

Stable Identifier
R-HSA-9683546
Type
Reaction [binding]
Species
Homo sapiens
Compartment
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Furin and related proprotein convertases (PCs) cleave the multibasic motifs R-X-R/K/X-R in precursor proteins, transforming latent proproteins into biologically active proteins and peptides. Furin is present both in the intracellular secretory pathway and at the cell surface. Intracellular furin processes its multiple normal cellular targets in the Golgi and secretory vesicle compartments. Cell surface furin-mediated cleavage of coat proteins of viral pathogens including influenza A-H5N1 (bird flu), flaviviruses, and Marburg and Ebola viruses and of anthrax and botulinum toxins, enables entry into host cells to cause disease onset (Braun & Sauter 2019). Cell surface furin inhibitors capric acid, pirfenidone (Burghardt et al. 2007) and MI-1148 (Hardes et al. 2015) inhibit furin activity thereby exhibiting a protective effect against some toxins and inhibiting the spread of several pathogenic viruses (Hardes et al. 2015). Inhibitors of PCs represent a potential therapeutic anti-SARS activity (Bergeron et al. 2005, Izaguirre 2019).

Literature References
PubMed ID Title Journal Year
25974265 Novel Furin Inhibitors with Potent Anti-infectious Activity

Hardes, K, Becker, GL, Lu, Y, Dahms, SO, Köhler, S, Beyer, W, Sandvig, K, Yamamoto, H, Lindberg, I, Walz, L, von Messling, V, Than, ME, Garten, W, Steinmetzer, T

ChemMedChem 2015
17234158 Pirfenidone inhibits TGF-beta expression in malignant glioma cells

Burghardt, I, Tritschler, F, Opitz, CA, Frank, B, Weller, M, Wick, W

Biochem. Biophys. Res. Commun. 2007
15596135 Implication of proprotein convertases in the processing and spread of severe acute respiratory syndrome coronavirus

Bergeron, E, Vincent, MJ, Wickham, L, Hamelin, J, Basak, A, Nichol, ST, Chrétien, M, Seidah, NG

Biochem. Biophys. Res. Commun. 2005
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