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α-突触核蛋白是一种在中枢神经系统突触前表达的可溶性蛋白,具有调节膜稳定性和神经可塑性等生理功能。近来研究发现,α-突触核蛋白基因突变及其结构和功能障碍与包括帕金森病在内的多种神经变性疾病的病理机制密切相关。环境或基因因素均可引发α-突触核蛋白的错误折叠,从而启动一系列级联反应,最终导致多巴胺能系统损伤。深入了解α-突触核蛋白的生物特性及其毒性机制是揭示帕金森病发病并制定相应防治策略的关键。
Alpha-synuclein is a soluble protein expressed presynaptically in the central nervous system and possesses physiological functions such as membrane stability and neuroplasticity. Recent studies have found that α-synuclein gene mutations and their structural and functional disorders are closely related to the pathological mechanisms of various neurodegenerative diseases, including Parkinson’s disease. Both environmental and genetic factors trigger the misfolding of α-synuclein, initiating a series of cascades that eventually lead to dopaminergic system damage. In-depth understanding of the biological characteristics of α-synuclein and its toxicity mechanism is to reveal the key to the development of Parkinson’s disease and to develop appropriate prevention and treatment strategies.