病理/ Pathology

机制/ Mechanism

淀粉样变性/

Amyloidosis

1. 淀粉样蛋白是不溶性纤维蛋白，具有特定的结构特征，包括富含β-折叠的二级结构。/ Amyloids are insoluble fibrous proteins that have specific structural characteristics, including a β-sheet-rich secondary structure.

2. 大多数常见的神经退行性疾病表现出淀粉样蛋白异常。/ Most common neurodegenerative diseases exhibit amyloid protein abnormalities.

3. 淀粉样蛋白聚集物可以在神经元和神经胶质细胞质内发现， 淀粉样蛋白的细胞外沉积物可以在脑实质中发现为斑块。/ Amyloid aggregate deposits can be found within the cytoplasm of neurons and glia. Extracellular deposits of amyloid can be found in the brain parenchyma as plaques.

Tau蛋白病变/ Tauopathies

1. Tau是与微管相关的磷蛋白，在轴突中含量丰富，参与促进微管的聚合和稳定。/ Tau is a microtubule-associated phosphoprotein abundant in axons involved in promoting polymerization and stabilization of microtubules.

2. 已观察到翻译后修饰错误导致Tau积累。/ Post-translational modification errors have been observed to drive Tau accumulation.

3. 已经发现tau蛋白（MAPT）基因发生突变，这种突变与额颞痴呆和帕金森氏症状有关。/ Mutations have been discovered in the gene for tau protein (MAPT) which is associated with frontotemporal dementia and Parkinson’s like symptoms.

突触核蛋白病/ Synucleopathies

1. α-突触核蛋白可能在突触小泡运输中起作用。/ α-synuclein may play a role in synaptic vesicle trafficking.

2. 以神经元和神经胶质细胞（主要是少突胶质细胞）内突触前蛋白的聚集为特征。/ Characterised by the aggregation of the presynaptic protein within neurons and glia (mostly oligodendroglia).

3. 在家族性帕金森氏病中已观察到SNCA的α-突触核蛋白基因突变， α-突触核蛋白也被确定为路易小体的主要成分。/ Mutations in the gene for α-synuclein, SNCA, have been observed in familial Parkinson’s disease. α-synuclein has also been determined to be the major constituent of Lewy bodies.