Characterization of Myelin-Associated Glycoprotein (MAG) Proteolysis in the Human Central Nervous System

被引：0
作者：
Jeffrey W. Stebbins
Howard Jaffe
Johanna R. Möller
机构：
[1] Demyelinating Disorders Unit,
[2] LMCN,undefined
[3] NINDS,undefined
[4] LNC-NINDS Protein/Peptide Sequencing Facility,undefined
[5] NIH,undefined
来源：
Neurochemical Research | 1998年 / 23卷
关键词：
Myelin; protease; demyelination; multiple sclerosis;
D O I：
暂无
中图分类号：
学科分类号：
摘要：
Purified human central nervous system myelin contains an endogenous cysteine protease which degrades the 100-kDa myelin-associated glycoprotein into a slightly smaller 90-kDa derivative called dMAG, and which has been implicated in demyelinating diseases. The native proteolytic site in human MAG was determined in order to characterize this cysteine protease in humans further. This was accomplished by identifying the carboxy-terminus of purified dMAG. The results of these experiments, in conjunction with peptidolysis assays of myelin, demonstrated that the enzyme which proteolyses MAG is extracellular and has cathepsin L-like specificity. Furthermore, it was shown that this cathepsin L-like activity potentially was regulated by the endogenous extracellular inhibitor cystatin C.
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页码：1005 / 1010
页数：5
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