Fatty acid composition of myelin proteolipid protein during vertebrate evolution

被引:8
作者
Bizzozero, OA
Lees, MB
机构
[1] EK Shriver Ctr, Div Biomed Sci, Waltham, MA 02452 USA
[2] Univ New Mexico, Ctr Hlth Sci, Dept Cell Biol & Physiol, Albuquerque, NM 87131 USA
[3] Harvard Univ, Sch Med, Dept Neurol, Boston, MA 02114 USA
[4] Massachusetts Gen Hosp, Boston, MA 02114 USA
关键词
proteolipid protein; myelin; protein acylation; evolution; fatty acids;
D O I
10.1023/A:1022518206037
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The hydrophobic myelin proteolipid protein (PLP) contains covalently bound long-chain fatty acids which are attached to intracellular cysteine residues via thioester linkages. To gain insight into the role of acylation in the structure and function of myelin PLP, the amount and pattern of acyl groups attached to the protein during vertebrate evolution was determined. PLP isolated from brain myelin of amphibians, reptiles, birds and several mammals was subjected to alkaline methanolysis and the released methyl esters were analyzed by gas-liquid chromatography. In all species studied, PLP contained approximately the same amount of covalently bound fatty acids (3% w/w), and palmitic, palmitoleic, oleic and stearic acids were always the major acyl groups. Although the relative proportions of these fatty acids changed during evolution, the changes did not necessarily follow the variations in the acyl chain composition of the myelin free fatty acid pool, suggesting fatty acid specificity. The phylogenetic conservation of acylation suggests that this post-translational modification is critical for PLP function.
引用
收藏
页码:269 / 274
页数:6
相关论文
共 41 条