PROPROTEIN PROCESSING ACTIVITY AND CLEAVAGE SITE SELECTIVITY OF THE KEX2-LIKE ENDOPROTEASE PACE4

被引：40
作者：
CREEMERS, JWM
KORMELINK, PJG
ROEBROEK, AJM
NAKAYAMA, K
VANDEVEN, WJM
机构：
[1] UNIV TSUKUBA,INST BIOL SCI,TSUKUBA,IBARAKI 305,JAPAN
[2] UNIV TSUKUBA,CTR GENE EXPT,TSUKUBA,IBARAKI 305,JAPAN
来源：
FEBS LETTERS | 1993年 / 336卷 / 01期
关键词：
PROPROTEIN CLEAVAGE; PACE4; VON WILLEBRAND FACTOR;
D O I：
10.1016/0014-5793(93)81610-C
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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 Ked-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.
引用
收藏
页码：65 / 69
页数：5
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