Krüger R, Müller T, Riess O
Department of Neurology, St. Josef-Hospital, Ruhr-University, Bochum, Federal Republic of Germany.
J Neural Transm (Vienna). 2000;107(1):31-40. doi: 10.1007/s007020050002.
A major step in the elucidation of the pathogenesis of neurodegenerative disorders was the identification of a mutation in the alpha-synuclein gene in autosomal dominant Parkinson's disease (PD). Alpha-synuclein is the main component of Lewy bodies (LB), the neuropathological hallmark of PD. Moreover, a fragment of alpha-synuclein (NAC) is the second major component of amyloid plaques in Alzheimer's disease (AD). Recent studies of other neurodegenerative disorders such as dementia with LB (DLB), multiple system atrophy (MSA) and amyotrophic lateral sclerosis (ALS) also revealed intracellular accumulations of alpha-synuclein in affected brain regions. This may indicate that these disorders partially share common pathogenic mechanisms. Recent data provide first insights into the physiological function of alpha-synuclein and support the concept of an essential role of alpha-synuclein in neurodegeneration. Increasing knowledge on the pathogenic molecular mechanisms of neurodegeneration and of the pathophysiological function of alpha-synuclein in particular may influence future development of therapeutic strategies in neurodegenerative disorders.
阐明神经退行性疾病发病机制的一个重要进展是在常染色体显性帕金森病(PD)中发现了α-突触核蛋白基因的突变。α-突触核蛋白是路易小体(LB)的主要成分,而路易小体是帕金森病的神经病理学标志。此外,α-突触核蛋白的一个片段(NAC)是阿尔茨海默病(AD)中淀粉样斑块的第二主要成分。最近对其他神经退行性疾病的研究,如路易小体痴呆(DLB)、多系统萎缩(MSA)和肌萎缩侧索硬化症(ALS),也揭示了受影响脑区中α-突触核蛋白的细胞内积聚。这可能表明这些疾病部分共享共同的致病机制。最近的数据首次揭示了α-突触核蛋白的生理功能,并支持α-突触核蛋白在神经退行性变中起重要作用的概念。对神经退行性变致病分子机制的了解不断增加,尤其是对α-突触核蛋白病理生理功能的了解,可能会影响神经退行性疾病治疗策略的未来发展。