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组织蛋白酶B:一种用于产生聚集蛋白聚糖“金属蛋白酶”裂解新表位的替代蛋白酶。

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

作者信息

Mort J S, Magny M C, Lee E R

机构信息

Joint Diseases Laboratory, Shriners Hospital for Children and Department of Surgery, McGill University, 1529 Cedar Avenue, Montreal, Quebec, Canada H3G 1A6.

出版信息

Biochem J. 1998 Nov 1;335 ( Pt 3)(Pt 3):491-4. doi: 10.1042/bj3350491.

Abstract

Previously, only matrix metalloproteinases were believed capable of cleaving the cartilage proteoglycan, aggrecan, between Asn341 and Phe342, 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.

摘要

以前,人们认为只有基质金属蛋白酶能够在天冬酰胺341和苯丙氨酸342之间切割软骨蛋白聚糖(聚集蛋白聚糖),从而产生一个以VDIPEN残基结尾的小G1片段。我们发现,半胱氨酸蛋白酶组织蛋白酶B的内切酶和外切酶联合活性也能产生这一表位,这表明它不应再被视为金属蛋白酶活性的唯一标志物。

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本文引用的文献

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Crystallization of rat procathepsin B.大鼠组织蛋白酶B前体的结晶
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Cathepsin B.组织蛋白酶B
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