| Literature DB >> 8262218 |
J W Creemers1, P J Groot Kormelink, A J Roebroek, K Nakayama, W J Van de Ven.
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.Entities:
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Year: 1993 PMID: 8262218 DOI: 10.1016/0014-5793(93)81610-c
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124