The multifaceted proprotein convertases: their unique, redundant, complementary, and opposite functions.
Montréal, Canada. In J Biol Chem, 2013
The secretory proprotein convertase (PC) family comprises nine members: PC1/3, PC2, furin, PC4, PC5/6, PACE4, PC7, SKI-1/S1P, and PCSK9.
The biology and therapeutic targeting of the proprotein convertases.
Montréal, Canada. In Nat Rev Drug Discov, 2012
Seven of these (proprotein convertase 1 (PC1), PC2, furin, PC4, PC5, paired basic amino acid cleaving enzyme 4 (PACE4) and PC7) activate cellular and pathogenic precursor proteins by cleavage at single or paired basic residues, whereas subtilisin kexin isozyme 1 (SKI-1) and proprotein convertase subtilisin kexin 9 (PCSK9) regulate cholesterol and/or lipid homeostasis via cleavage at non-basic residues or through induced degradation of receptors.
What lies ahead for the proprotein convertases?
Montréal, Canada. In Ann N Y Acad Sci, 2011
Limited proteolysis of secretory proteins is performed by one or more of the nine-membered proprotein convertase (PC) family: PC1/3, PC2, furin, PC4, PC5/6, PACE4, PC7, SKI-1/S1P, and PCSK9.
The proprotein convertases, 20 years later.
Montréal, Canada. In Methods Mol Biol, 2010
The family of PCs comprises nine members, PC1/3, PC2, furin, PC4, PC5/6, PACE4, PC7, SKI-1/S1P, and PCSK9 (Fig. 3.1).