O'Farrell C, Murphy D D, Petrucelli L, Singleton A B, Hussey J, Farrer M, Hardy J, Dickson D W, Cookson M R
Neurogenetics Laboratory, Mayo Clinic Jacksonville, Jacksonville, FL 32224, USA.
Brain Res Mol Brain Res. 2001 Dec 16;97(1):94-102. doi: 10.1016/s0169-328x(01)00292-3.
The discovery of mutations in the gene for alpha-synuclein in familial Parkinson's disease (PD) has led to an increased interest in this pre-synaptic protein. Synphilin-1, a potential synuclein-binding protein, was cloned using yeast two-hybrid assays. The function of synphilin-1 is currently unknown, although it has been reported to be present along with alpha-synuclein in Lewy bodies in PD. In the present study, we monitored synphilin-1 aggregation directly using fusion proteins of synphilin-1 and green fluorescent protein (EGFP). Transfection of synphilin-EGFP fusion proteins formed cytoplasmic inclusions in HEK293 cells. Although these inclusions overlapped with the distribution of alpha-synuclein, they were unlike Lewy bodies in that they were not eosinophilic, and instead were membrane-bound, lipid-rich cytoplasmic inclusions.
家族性帕金森病（PD）中α-突触核蛋白基因突变的发现，引发了人们对这种突触前蛋白越来越浓厚的兴趣。通过酵母双杂交试验克隆出了一种潜在的突触核蛋白结合蛋白——Synphilin-1。尽管据报道在帕金森病的路易小体中Synphilin-1与α-突触核蛋白同时存在，但其功能目前尚不清楚。在本研究中，我们使用Synphilin-1与绿色荧光蛋白（EGFP）的融合蛋白直接监测Synphilin-1的聚集情况。Synphilin-EGFP融合蛋白转染后在HEK293细胞中形成细胞质包涵体。尽管这些包涵体与α-突触核蛋白的分布重叠，但它们与路易小体不同，因为它们不是嗜酸性的，而是膜结合的、富含脂质的细胞质包涵体。
