Conserved fatty acid composition of proteolipid protein during brain development and in myelin subfractions.

Myelin proteolipid protein (PLP) is modified after translation by the attachment of long-chain fatty acids to several cysteine residues. In this study, the amount and pattern of fatty acids covalently bound to rat PLP were determined during brain development and in myelin subfractions. For this purpose, PLP was isolated by gel-filtration chromatography in organic solvents, subjected to alkaline methanolysis, and the released fatty acid methyl esters were analyzed by gas-liquid chromatography. At all ages examined, PLP had the same amount of covalently-bound fatty acids (3-4% w/w) and palmitate, oleate and stearate were always the major acyl chains. In contrast to myelin lipids, the fatty acid composition of PLP showed only minor changes between 15-days and 90-days of age. The amount and pattern of fatty acids bound to PLP prepared from three myelin subfractions were also indistinguishable. The conservation of a characteristic PLP-fatty acid make-up during brain development and in various myelin compartments suggests that this post-translational modification is essential for the normal functioning of the protein.