Lipofuscin and Aβ42 exhibit distinct distribution patterns in normal and Alzheimer's disease brains
Lipofuscin and Aβ42 exhibit distinct distribution patterns in normal and Alzheimer's disease brains
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DOI：
10.1016/s0304-3940(01)02444-2
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发表时间：
2002-04-19
影响因子：
2.5
通讯作者：
Andrade-Gordon, P
中科院分区：
文献类型：
--
作者：
D'Andrea, MR;Nagele, RG;Andrade-Gordon, P
我们最近的研究提供了证据，Abeta42，一个42个氨基酸的淀粉样前体蛋白片段，在脆弱的神经元中积累在细胞内。这项研究似乎表明，在阿尔茨海默病(AD)的内嗅觉皮质中，神经元溶解并形成致密核心的淀粉样斑块。以前的研究表明，细胞内的Abeta42与脂褐素在神经元中共定位，这些增加的脂褐素和Abeta42水平与AD有关。其他研究对这种关系提出了质疑，并提出，在AD和年龄匹配的对照组织中，β-淀粉样蛋白和脂褐素不是共定位的，它们的水平彼此独立。为了解决这一争议，我们使用一种新的组合免疫组织化学方法：组织化学染色方法，研究了AD脑组织中细胞内Abeta42和脂褐素的相对空间关系。我们的结果显示了Abeta42和脂褐素在神经元和淀粉样斑块中的不同和不同的定位模式。(C)2002爱思唯尔科学爱尔兰有限公司。保留所有权利。
Our recent study has provided evidence that Abeta42, a 42 amino acid fragment of the amyloid precursor protein, accumulates intracellularly in vulnerable neurons. This study appears to show that neurons lyse and form dense-core amyloid plaques in Alzheimer's disease (AD) entorhinal cortex. Previous studies have suggested that intracellular Abeta42 co-localizes with lipofuscin in neurons and those increased levels of lipofuscin and Abeta42 are associated with AD. Other studies have questioned this relationship and suggested that beta-amyloid and lipofuscin are not co-localized and that their levels are independent of one another in AD and age-matched control tissues. In an effort to resolve this controversy, we investigated the relative spatial relationship of intracellular Abeta42 and lipofuscin in AD brains tissue using a novel combined immunohistochemical:histochemical staining protocol. Our results show separate and distinct localization patterns of Abeta42 and lipofuscin in neurons and amyloid plaques. (C) 2002 Elsevier Science Ireland Ltd. All rights reserved.