Crowther R A, Jakes R, Spillantini M G, Goedert M
Medical Research Council, Laboratory of Molecular Biology, Cambridge, UK.
FEBS Lett. 1998 Oct 9;436(3):309-12. doi: 10.1016/s0014-5793(98)01146-6.
Recently two point mutations in the alpha-synuclein gene have been found in familial Parkinson's disease. The characteristic fibrous neuropathological lesions of Parkinson's and other neurodegenerative diseases have been shown to stain strongly with antibodies against alpha-synuclein and extracted filaments have been labelled with anti-alpha-synuclein antibodies. In view of the close involvement of alpha-synuclein filaments with pathology, it was important to establish an in vitro assembly system. We report here that C-terminally truncated recombinant alpha-synuclein readily assembles into filaments resembling those isolated from diseased brain and suggest that truncation by proteolysis may play a role in the pathological process.
最近，在家族性帕金森病中发现了α-突触核蛋白基因的两个点突变。帕金森病和其他神经退行性疾病的典型纤维状神经病理损伤已被证明能与抗α-突触核蛋白抗体强烈染色，并且提取的细丝已用抗α-突触核蛋白抗体标记。鉴于α-突触核蛋白细丝与病理学密切相关，建立体外组装系统很重要。我们在此报告，C末端截短的重组α-突触核蛋白很容易组装成类似于从患病大脑中分离出的细丝，并表明蛋白水解截短可能在病理过程中起作用。
