Procathepsin L degrades extracellular matrix proteins in the presence of glycosaminoglycans in vitro
Procathepsin L degrades extracellular matrix proteins in the presence of glycosaminoglycans in vitro
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DOI：
10.1006/bbrc.1995.2820
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发表时间：
1995-12-14
影响因子：
3.1
通讯作者：
Kominami, E
中科院分区：
文献类型：
--
作者：
Ishidoh, K;Kominami, E
在生理性糖胺聚糖、硫酸乙酰肝素、硫酸软骨素等的表面加工组织蛋白原L，以及葡聚糖衍生物进行了研究。所有的糖胺聚糖和右旋糖酐衍生物，包括右旋糖酐T-500和DEAE右旋糖酐在这项研究中检查加快了不同的时间courses.Further，我们研究是否前组织蛋白酶L的蛋白质底物的表面材料的存在或不存在的转化为加工的组织蛋白酶L。层粘连蛋白降解的前组织蛋白酶L本身和31-kDa的处理形式的存在下，具有相同的配置文件的表面材料，相比之下，纤连蛋白被消化的前组织蛋白酶L没有处理的表面材料的存在下。加工形式的纤连蛋白的蛋白水解谱不同于前组织蛋白酶L的蛋白水解谱。这是第一个证据表明，半胱氨酸蛋白酶的预制蛋白质底物。(C)出版社：Academic Press
The processing of procathepsin L on the surfaces of physiological glycosaminoglycans, heparan sulfate, chondroitin sulfate, etc., as well as dextran derivatives were studied. All glycosaminoglycans and dextran derivatives including dextran T-500 and DEAE dextran examined in this study accelerated the conversion of procathepsin L to processed cathepsin L in vitro with different time courses.Further, we examined whether procathepsin L digests protein substrates in the presence or absence of the surface materials. Laminin was degraded by both procathepsin L itself and the 31-kDa processed form in the presence of surface materials with the same profiles, In contrast, fibronectin was digested by procathepsin L without processing in the presence of surface materials. The proteolytic profiles of fibronectin by the processed form differed from those by procathepsin L. This is the first evidence that the preform of a cysteine proteinase proteolyzes protein substrates. (C) 1995 Academic Press, Inc.