Popescu Anca, Lippa Carol F, Lee Virginia M-Y, Trojanowski John Q
Department of Neurology, Drexel University College of Medicine, 3300 Henry Avenue, Philadelphia, PA 19129, USA.
Arch Neurol. 2004 Dec;61(12):1915-9. doi: 10.1001/archneur.61.12.1915.
Increased attention has been given to alpha-synuclein aggregation in nonsynucleinopathies because alpha-synuclein-containing Lewy bodies (LBs) influence symptoms. However, the spectrum of disorders in which secondary inclusions are likely to occur has not been defined. Amygdala neurons commonly develop large numbers of secondary LBs, making it a practical region for studying this phenomenon.
To characterize the spectrum of diseases associated with LB formation in the amygdala of neurodegenerative disease and control cases.
An autopsy series of 101 neurodegenerative disease and 34 aged control cases. Using immunohistochemistry studies, we examined the amygdala for alpha-synuclein aggregates.
Lewy bodies were often abundant in classic Pick disease, argyrophilic grain disease, Alzheimer disease, and dementia with LBs but not in cases with amygdala degeneration lacking tau-based inclusions, control cases, preclinical disease carriers, or degenerative diseases lacking pathologic involvement of the amygdala. The exposed alpha-synuclein epitopes were similar in all cases containing LBs.
Abnormal alpha-synuclein aggregation in the amygdala is disease selective, but not restricted to disorders of alpha-synuclein and beta-amyloid. Our data are compatible with the notion that tau aggregates predispose neurons to develop secondary LBs.
由于含α-突触核蛋白的路易小体（LB）会影响症状，因此非突触核蛋白病中α-突触核蛋白聚集受到了更多关注。然而，可能出现继发性包涵体的疾病谱尚未明确。杏仁核神经元通常会形成大量继发性路易小体，使其成为研究这一现象的理想区域。
明确神经退行性疾病及对照病例杏仁核中与路易小体形成相关的疾病谱。
对101例神经退行性疾病尸检系列及34例老年对照病例进行研究。通过免疫组织化学研究，检测杏仁核中α-突触核蛋白聚集情况。
在经典匹克病、嗜银颗粒病、阿尔茨海默病及路易小体痴呆病例中，路易小体通常较多，但在缺乏基于tau蛋白的包涵体的杏仁核变性病例、对照病例、临床前疾病携带者或无杏仁核病理改变的退行性疾病病例中则不然。在所有含路易小体的病例中，暴露的α-突触核蛋白表位相似。
杏仁核中异常的α-突触核蛋白聚集具有疾病选择性，但不仅限于α-突触核蛋白和β-淀粉样蛋白相关疾病。我们的数据支持tau蛋白聚集使神经元易形成继发性路易小体这一观点。
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