α-synuclein overexpression promotes aggregation of mutant huntingtin
α-synuclein overexpression promotes aggregation of mutant huntingtin
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DOI：
10.1042/0264-6021:3460577
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发表时间：
2000-03-15
影响因子：
4.1
通讯作者：
Rubinsztein, DC
中科院分区：
文献类型：
--
作者：
Furlong, RA;Narain, Y;Rubinsztein, DC
蛋白质聚集是亨廷顿病和帕金森病的神经病理学特征。具有72个CAG重复序列的突变亨廷顿蛋白外显子1与增强型绿色荧光蛋白（EGFP）融合，在PC 12细胞中形成高荧光包涵体。在用EGFP-亨廷顿蛋白（CAG）（72）和α-突触核蛋白（帕金森病聚集体的主要成分）共转染的细胞中，包涵体形成增强。然而，α-突触核蛋白本身不形成聚集体，也不出现在体外亨廷顿蛋白包涵体中。
Protein aggregates are a neuropathological feature of Huntington's disease and Parkinson's disease. Mutant huntingtin exon 1 with 72 CAG repeats fused to enhanced green fluorescent protein (EGFP) forms hyperfluorescent inclusions in PC12 cells. Inclusion formation is enhanced in cells co-transfected with EGFP-huntingtin-(CAG)(72) and alpha-synuclein, a major component of Parkinson's disease aggregates. However, alpha-synuclein does not form aggregates by itself, nor does it appear in huntingtin inclusions in vitro.