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White Matter Proteins in Multiple Sclerosis
Author(s) -
Newcombe J.,
Cuzner M. L.,
Röyttä M.,
Frey H.
Publication year - 1980
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1980.tb11200.x
Subject(s) - myelin , white matter , myelin basic protein , multiple sclerosis , gliosis , glial fibrillary acidic protein , gel electrophoresis , biology , pathology , microbiology and biotechnology , chemistry , central nervous system , immunology , medicine , immunohistochemistry , endocrinology , neuroscience , magnetic resonance imaging , radiology
The SDS‐soluble membrane proteins of plaques and of macroscopically normal white matter from multiple sclerosis brain were investigated by gradient polyacrylamide gel electrophoresis (PAGE). Eleven protein bands were analyzed in detail. The extensive loss of myelin proteins in plaque samples was accompanied by changes in at least three other non‐myelin proteins, besides glial fibrillary acidic protein (GFAP), which probably reflect gliosis. Densitometric analysis of the PAGE patterns of membrane fractions from MS and control white matter revealed significant quantitative differences in a number of protein bands. A reduction in myelin basic protein (BP) was associated with an equally significant increase in a high‐molecular‐weight peptide fragment which may prove to be a breakdown product of BP. Small but highly significant differences in the Wolfgram protein and in one non‐myelin protein were also a consistent feature of the normal‐appearing white matter samples. The problem of defining normal white matter in multiple sclerosis brain is discussed in relation to the results of the present study, which suggest that one of the early events in the pathogenesis of the disease prior to frank demyelination is an alteration in the protein components of the myelin sheath and possibly of glial cells.