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Synuclein最初是作为一种突触前蛋白于1988年由Maroteaux等从太平洋电鲟鱼的带电器官中分离得到的,由于它同时分布于神经元的突触前终末和细胞核,因此被称为共核蛋白;免疫组织化学结果显示其分布于突触和核膜,故又命名为突触核蛋白。人类突触核蛋白存在3种结构类型,α、β和γ。α和β-突触核蛋白与神经系统变性疾病有关;γ-突触核蛋白与乳腺癌及信号传导通路的调控有关。1993年Ueda等在人类阿尔茨海默病(Alzheimerdisease,AD)淀粉样斑块中的非Aβ蛋白成分中分离到一种新的蛋白,命名为非Aβ蛋白成分,后来证实非Aβ蛋白的前体蛋白就是α-突触核蛋白(α-synuclein,α-syn)。
Synuclein was originally isolated as a presynaptic protein from the electropositive organs of Pacific Electro sturgeon by Maroteaux et al. In 1988 and is known as a co-presynaptic terminal and nucleus of neurons Nucleoprotein; immunohistochemistry results show that it is distributed in the synapse and nuclear membrane, it is also named as synuclein. There are three structural types of human synuclein, α, β and γ. Alpha and beta-synuclein are associated with degenerative diseases of the nervous system; gamma-synuclein is involved in the regulation of breast cancer and signaling pathways. In 1993, Ueda et al. Isolated a new protein from the non-Aβ protein in amyloid plaques of human Alzheimer disease (AD) and named it a non-Aβ protein component. Later, it was confirmed that non-Aβ protein precursor Protein is α-synuclein (α-syn).