Abstract
Myelin proteolipid protein (PLP) is one of the most abundant proteins in myelin of the central nervous system (CNS), and together with myelin basic protein (MBP), constitutes 80% of the myelin membrane proteins of the CNS. It is called “proteolipid” because of its unusual property to dissolve in organic solvents (5). There is another less abundant proteolipid, DM20, which shows immunological cross-reactivity with the major proteolipid protein (13). Most investigators have obtained molecular weights of 24,000–26,000 for PLP by SDS-PAGE, and approximately 5,000 less than PLP for DM20 (13). Lipids are covalently attached to PLP via an 0-ester linkage (28). Because amino acid and nucleotide sequences of PLP are remarkably well conserved among mouse, rat, cow, and human (4, 6, 8, 9, 14, 16, 20, 21, 25) and because severe dysmyelination is observed in the animals whose PLP-synthesis are affected (7), PLP is thought to play a crucial role in myelination in the CNS; probably by promoting the apposition of extracellular surfaces of the myelin lamellae.
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