UBIQUITIN IS DETECTED IN NEUROFIBRILLARY TANGLES AND SENILE PLAQUE NEURITES OF ALZHEIMER-DISEASE BRAINS
UBIQUITIN IS DETECTED IN NEUROFIBRILLARY TANGLES AND SENILE PLAQUE NEURITES OF ALZHEIMER-DISEASE BRAINS
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DOI：
10.1073/pnas.84.9.3033
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发表时间：
1987-05-01
影响因子：
11.1
通讯作者：
CHAU, V
中科院分区：
文献类型：
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作者：
PERRY, G;FRIEDMAN, R;CHAU, V
用针对泛素的亲和纯化抗体对阿尔茨海默病脑组织中与老年斑（SP）相关的神经原纤维缠结（NFT）和神经突进行了特异性免疫染色。此外，在含有NFT和SP的大脑区域中发现的一类神经突也被特异性染色。泛素抗血清对tau蛋白、神经丝蛋白和高分子量微管相关蛋白（MAPs）的交叉反应性被排除在外，原因是：(i)泛素抗血清在免疫印迹实验中无法染色这些蛋白；（ii） tau、神经丝和MAP制剂在与泛素抗血清一起预孵育时，无法抑制观察到的选择性神经纤维染色。我们的结果与泛素与NFT和SP的不溶性神经原纤维物质共价相关的建议一致。我们提出泛素药物降解途径可能对去除阿尔茨海默病大脑中的这些纤维结构无效。
Neurofibrillary tangles (NFT) and neurites associated with senile plaques (SP) in Alzheimer disease-affected brain tissues were specifically immunostained with affinity-purified antibody preparations directed against ubiquitin. In addition, a class of neurites seen in brain regions containing NFT and SP were also specifically stained. Cross-reactivity of the ubiquitin antisera for tau protein, neurofilament proteins, and high molecular weight microtubule-associated proteins (MAPs) were ruled out by (i) the inability of the ubiquitin antisera to stain these proteins in immunoblotting experiments and (ii) the inability of tau, neurofilament, and MAP preparations, when preincubated with the ubiquitin antisera, to inhibit the selective neurofibrillar staining observed. Our results are consistent with the suggestion that ubiquitin is covalently associated with the insoluble neurofibrillary material of NFT and SP. We propose that the ubiquitin-medicated degradative pathway may be ineffective in removing these fibrillar structures in Alzheimer disease brain.