Cathepsin B: an alternative protease for the generation of an aggrecan 'metalloproteinase' cleavage neoepitope

被引:82
作者
Mort, JS
Magny, MC
Lee, ER
机构
[1] Shriners Hosp Crippled Children, Joint Dis Lab, Montreal, PQ H3G 1A6, Canada
[2] McGill Univ, Dept Surg, Montreal, PQ H3G 1A6, Canada
[3] Shriners Hosp Crippled Children, Electron Microscopy Unit, Montreal, PQ H3G 1A6, Canada
关键词
D O I
10.1042/bj3350491
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
Previously, only matrix metalloproteinases were believed capable of cleaving the cartilage proteoglycan, aggrecan, between Asn(341) and Phe(342), to yield a small G1 fragment terminating in the residues VDIPEN. We show that the combined endo- and exopeptidase activities of the cysteine protease, cathepsin B, also generate this epitope, suggesting that it should no longer be considered as an exclusive marker of metalloproteinase activity.
引用
收藏
页码:491 / 494
页数:4
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