Creemers J W, Groot Kormelink P J, Roebroek A J, Nakayama K, Van de Ven W J
Laboratory for Molecular Oncology, University of Leuven, Belgium.
FEBS Lett. 1993 Dec 20;336(1):65-9. doi: 10.1016/0014-5793(93)81610-c.
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.
测定了类Kex2的哺乳动物内切蛋白酶PACE4的前体蛋白加工活性及其对含碱性氨基酸残基位点的切割选择性。利用基于重组痘苗病毒的表达系统，PACE4在猪肾PK(15)细胞中表达，并且与另外两种类Kex2内切蛋白酶弗林蛋白酶和PC6A一样，能够正确加工血管性血友病因子前体（pro-vWF）。此外，使用vWF切割位点突变体vWFR-1G、vWFK-2A和vWFR-4A作为底物，将PACE4的切割位点选择性特征与弗林蛋白酶和PC6A的进行了比较。PACE4和PC6A的切割位点选择性似乎相似，但与弗林蛋白酶不同。
