title: Proprotein processing activity and cleavage site selectivity of the Kex2-like endoprotease PACE4.
abstract: Proprotein processing activity of the Kex2-like mammalian endoprotease PACE4 and its cleavage selectivity for sites with basic amino acid residues were determined. Using a recombinant vaccinia virus-based expression system, PACE4 was expressed in pig kidney PK(15) cells and, like two other Kex2-like endoproteases furin and PC6A, shown to correctly process the precursor of von Willebrand factor (pro-vWF). Furthermore, characteristics of the cleavage site selectivity of PACE4 were compared to those of furin and PC6A using the vWF cleavage site mutants vWFR-1G, vWFK-2A, and vWFR-4A as substrates. Cleavage site selectivity of PACE4 and PC6A appeared to be similar but they differed from that of furin.
authors.affiliation: Laboratory for Molecular Oncology, University of Leuven, Belgium.
authors.forename: J W
authors.initials: JW
authors.lastname: Creemers
authors.forename: P J
authors.initials: PJ
authors.lastname: Groot Kormelink
authors.forename: A J
authors.initials: AJ
authors.lastname: Roebroek
authors.forename: K
authors.initials: K
authors.lastname: Nakayama
authors.forename: W J
authors.initials: WJ
authors.lastname: Van de Ven
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002478:Cells, Cultured; D045683:Furin; D006801:Humans; D051379:Mice; D008969:Molecular Sequence Data; D045702:Proprotein Convertase 5; D043484:Proprotein Convertases; D011498:Protein Precursors / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D012697:Serine Endopeptidases / Q000378:metabolism*; D013379:Substrate Specificity; D013381:Subtilisins / Q000378:metabolism; D013552:Swine; D014841:von Willebrand Factor / Q000378:metabolism
chemical_list: D011498:Protein Precursors; D014841:von Willebrand Factor; C080654:PCSK6 protein, human; C513086:Pcsk6 protein, mouse; D045702:Proprotein Convertase 5; D043484:Proprotein Convertases; D012697:Serine Endopeptidases; D013381:Subtilisins; D045683:Furin