Furlong R A, Narain Y, Rankin J, Wyttenbach A, Rubinsztein D C
Department of Medical Genetics, Cambridge University, Wellcome Trust Centre for the Study of Molecular Mechanisms in Disease, Cambridge Institute for Medical Research, Wellcome/MRC Building, Addenbrooke's Hospital, Hills Road, Cambridge CB2 2XY, U.K.
Biochem J. 2000 Mar 15;346 Pt 3(Pt 3):577-81.
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.
蛋白质聚集体是亨廷顿舞蹈症和帕金森病的神经病理学特征。带有72个CAG重复序列的突变型亨廷顿蛋白外显子1与增强型绿色荧光蛋白（EGFP）融合，在PC12细胞中形成高荧光包涵体。在与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-突触核蛋白自身并不形成聚集体，在体外也未出现在亨廷顿蛋白包涵体中。
