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

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Abstract

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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Authors and Affiliations

  1. Demyelinating Disorders Unit, LMCN, NINDS, USA

    Jeffrey W. Stebbins & Johanna R. Möller

  2. LNC-NINDS Protein/Peptide Sequencing Facility, NIH, 9000 Rockville Pike, Bethesda, MD, 20892

    Howard Jaffe

  3. Bethesda, MD, 20892-4440

    Jeffrey W. Stebbins

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  1. Jeffrey W. Stebbins
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  2. Howard Jaffe
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  3. Johanna R. Möller
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Stebbins, J.W., Jaffe, H. & Möller, J.R. Characterization of Myelin-Associated Glycoprotein (MAG) Proteolysis in the Human Central Nervous System. Neurochem Res 23, 1005–1010 (1998). https://doi.org/10.1023/A:1021092624046

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