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Elevated neutral protease activity in myelin from brains of patients with multiple sclerosis
Author(s) -
Sato Shuzo,
Quarles Richard H.,
Brady Roscoe O.,
Tourtellotte Wallace W.
Publication year - 1984
Publication title -
annals of neurology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.764
H-Index - 296
eISSN - 1531-8249
pISSN - 0364-5134
DOI - 10.1002/ana.410150310
Subject(s) - myelin , multiple sclerosis , myelin basic protein , myelin associated glycoprotein , protease , pathogenesis , glycoprotein , chemistry , myelin sheath , biochemistry , immunology , biology , enzyme , endocrinology , central nervous system
Incubation of human myelin at neutral P H resulted in the proteolytic conversion of the myelin‐associated glycoprotein to a lower molecular weight derivative (dMAG) and the degradation of basic protein. The formation of dMAG occured much more rapidly than the degradation of basic protein. The formation of dMAG and the degradation of basic protein both occured significantly more rapidly in myelin preparations purified from brains of patients with multiple sclerosis than in preparations from control brain. The results suggest that this neutral protease associated with myelin may function in the pathogenesis of demyelinating diseases such as multiple sclerosis.