Department of Biochemistry and Molecular Biology, Louisiana State University Health Sciences Center, Shreveport, LA 71130, USA.
Biochem Biophys Res Commun. 2013 Aug 23;438(2):452-6. doi: 10.1016/j.bbrc.2013.07.100. Epub 2013 Jul 31.
Using a yeast model of Parkinson's disease, we found that alpha-synuclein (αS) binds to lipid droplets in lipid-loaded, wild-type yeast cells but not to lipid droplets in lipid-loaded, peroxisome-deficient cells (pex3Δ). Our analysis revealed that pex3Δ cells have both fewer lipid droplets and smaller lipid droplets than wild-type cells, and that the acyl chains of the phospholipids on the surface of the lipid droplets from pex3Δ cells are on average shorter (C16) than those (C18) on the surface of lipid droplets from wild-type cells. We propose that the shift to shorter (C18→C16) acyl chains contributes to the reduced binding of αS to lipid droplets in pex3Δ cells.
利用帕金森病的酵母模型,我们发现α-突触核蛋白(αS)与载脂的野生型酵母细胞中的脂滴结合,但不与载脂的过氧化物酶体缺陷型细胞(pex3Δ)中的脂滴结合。我们的分析表明,pex3Δ细胞中的脂滴数量少于野生型细胞,且pex3Δ细胞中的脂滴表面的磷脂酰基链的平均长度(C16)也短于野生型细胞(C18)。我们提出,向较短的(C18→C16)酰基链的转变有助于减少αS与pex3Δ细胞中脂滴的结合。