帕金森病(Parkinsondisease,PD)是第二常见的神经变性疾病。其主要临床特征是静止性震颤、肌强直、运动减少和姿势平衡障碍等;主要病理改变是中脑黑质多巴胺能神经元进行性变性坏死,残存神经元中Lewy小体形成。5-10%帕金森病患者有家族史。虽然,大部分帕金森病病例为散发型,但阐明家族性帕金森病的分子机理对于整个帕金森病发病机制的研究有着重大的意义。本文就目前已经明确的帕金森病相关蛋白的作用机理作一综述。一、α-synucleinSCNA(PAPK1)是第一个被发现的与常染色体显性遗传帕金森病有关的基因,其编码蛋白α-synuclein。α-synuelein是一种高度保守的蛋白质,高度耐热,为小分子酸性蛋白质,含有140个氨基酸。α-synuclein的序列可以分为三个结构域高度保守的氨基端包含11个氨基酸不完全的6拷贝重复,中间部分是被称为非口-淀粉样蛋白(NAC)的疏水结构域,羧基端没有固定的结构原件。α-synuclein在中枢神经系统内(特别是突触前膜)丰富表达,定位于核周。它是一种可溶的,天然伸展的蛋 Parkinson’s disease (PD) is the second most common neurodegenerative disease. The main clinical features are quiescence tremor, muscle rigidity, decreased motion and posture balance disorders; the main pathological changes are the degeneration and necrosis of dopaminergic neurons in the substantia nigra and the formation of Lewy bodies in the remnant neurons. 5-10% of patients with Parkinson’s disease have a family history. Although the majority of Parkinson’s disease cases are sporadic, elucidation of the molecular mechanism of familial Parkinson’s disease is of great importance to the study of the pathogenesis of Parkinson’s disease as a whole. In this paper, the mechanism of action of Parkinson’s disease-related proteins has been clarified so far. First, α-synucleinSCNA (PAPK1) is the first discovered gene associated with autosomal dominant inherited Parkinson’s disease, which encodes the protein α-synuclein. Alpha-synuelein is a highly conserved protein that is highly thermostable and is a small molecule acidic protein that contains 140 amino acids. The sequence of α-synuclein can be divided into three domains. The highly conserved amino terminus contains 11 amino acid imperfect copies of 6 copies. The middle part is the hydrophobic domain known as non-lipo-amyloid (NAC) No fixed structure of the original. α-synuclein is abundantly expressed in the central nervous system (especially the presynaptic membrane) and localized in the perinuclear area. It is a soluble, naturally stretched egg