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帕金森病(PD)的主要病理改变为黑质多巴胺神经元变性和Lewy体形成。纤维化积聚的α-共核蛋白(ASN)是Lewy体的主要组成成分。研究证实ASN寡聚体具神经毒性,ASN异常积聚被认为在PD发病机制中发挥了关键作用。ASN的基因突变、过度表达、异常修饰或清除减少都可能引起其异常积聚。异常积聚的ASN通过刺激免疫反应、诱导多巴胺神经元凋亡、降低自噬作用、破坏高尔基体组成等途径导致多巴胺神经元变性。本文针对α-共核蛋白异常积聚的具体机制及其在帕金森病发病过程中的作用作一综述。
The major pathological changes in Parkinson’s disease (PD) are degeneration of substantia nigra dopamine neurons and formation of Lewy bodies. The fibrotic accumulation of α-synuclein (ASN) is a major component of Lewy bodies. Studies have demonstrated neuronal toxicity of ASN oligomers, and abnormal accumulation of ASN is thought to play a key role in the pathogenesis of PD. ASN gene mutations, overexpression, abnormal modification or clearance reduction may cause its abnormal accumulation. Abnormal accumulation of ASN leads to degeneration of dopaminergic neurons by stimulating the immune response, inducing apoptosis of dopamine neurons, reducing autophagy, and damaging Golgi apparatus. In this paper, the specific mechanism of α-synuclein abnormal accumulation and its role in the pathogenesis of Parkinson’s disease are reviewed.