Premium
Lipid and Protein Alterations of Spinal Cord and Cord Myelin of Multiple Sclerosis
Author(s) -
Yu Robert K.,
Ueno Kunihiro,
Glaser Gilbert H.,
Tourtellotte Wallace W.
Publication year - 1982
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.1471-4159.1982.tb03968.x
Subject(s) - myelin , spinal cord , proteolipid protein 1 , white matter , chemistry , multiple sclerosis , phospholipid , biochemistry , cerebroside , myelin basic protein , central nervous system , endocrinology , biology , immunology , medicine , membrane , magnetic resonance imaging , radiology , neuroscience
A comprehensive study was carried out to clarify the chemical compositions of spinal cord, cord myelin, and myelin subfractions of multiple sclerosis (MS). The protein compositions of normal‐appearing cerebral white matter and cerebral plaque and periplaque tissues were also analyzed for comparison. MS whole cord samples were found to contain higher amounts of water compared with normal samples. The total lipid contents were below normal. Among the individual lipids, cholesterol content remained unchanged, whereas cholesteryl esters appeared increased in MS cords. The acidic phospholipid concentrations were found to be lower than normal. Glycolipids, such as cerebrosides G M4 , G M1 , and G D1b , which are abundant in myelin, were all decreased. However, the concentrations of G M3 and G D3 , which are more characteristic of reactive astrocytes, were highly elevated. The total protein content of MS cord samples was decreased, and the decrease was attributable to the loss of myelin proteins as evidenced by the low recovery of myelin. The concentrations of myelin‐specific proteins, such as proteolipid protein and myelin basic protein, were significantly reduced. Other changes in the protein compositions included the accretion of two low molecular weight proteins of approximately 11,000 and 12,000, and the appearance of a periodic acid‐Schiff‐positive protein with the same electrophoretic mobility as the P 0 protein. Analysis of the isolated myelin indicated that it had a grossly normal protein composition. However, the two low molecular weight proteins and the P 0 protein appeared to be enriched in an upper‐phase cord subtraction. We attribute the appearance of the two low molecular weight proteins to the breakdown of proteolipid protein and/or myelin basic protein as a result of demyelination, and the appearance of P 0 to the involvement of PNS myelin. The latter finding provides the first biochemical evidence that in MS cord, remyelination can be achieved in part by invading Schwann cells and/or by the small number of Schwann cells that may be present in the cord.