免疫细胞化学证据表明β-蛋白前体是阿尔茨海默病神经原纤维缠结的一个组成部分。
Immunocytochemical evidence that the beta-protein precursor is an integral component of neurofibrillary tangles of Alzheimer's disease.
作者信息
Perry G, Richey P L, Siedlak S L, Smith M A, Mulvihill P, DeWitt D A, Barnett J, Greenberg B D, Kalaria R N
机构信息
Division of Neuropathology, Case Western Reserve University, Cleveland, Ohio 44106-4907.
出版信息
Am J Pathol. 1993 Dec;143(6):1586-93.
Abstract
Amyloid beta (A beta) immunoreactivity has been demonstrated in all extracellular neurofibrillary tangles (E-NFT) and most intraneuronal neurofibrillary tangles (I-NFT). We undertook this immunocytochemical study to understand the relationship between A beta immunoreactivity localized in NFT and beta-protein precursor (beta PP). We found epitopes of amino-, mid-, and carboxyl-terminal domains of beta PP in I-NFT and the majority of E-NFT. NFT retained beta PP after ionic detergent extraction, demonstrating that beta PP is an integral component of NFT. Finding beta PP in regions of A beta immunoreactivity raises the possibility that beta PP or its fragments associate with amyloid, and that the stability of A beta is responsible for its dominance in amyloid deposits.
摘要
在所有细胞外神经原纤维缠结（E-NFT）和大多数神经元内神经原纤维缠结（I-NFT）中均已证实存在β淀粉样蛋白（Aβ）免疫反应性。我们进行了这项免疫细胞化学研究，以了解定位于NFT中的Aβ免疫反应性与β蛋白前体（βPP）之间的关系。我们在I-NFT和大多数E-NFT中发现了βPP氨基末端、中间区域和羧基末端结构域的表位。经离子去污剂提取后，NFT仍保留βPP，表明βPP是NFT的一个组成部分。在Aβ免疫反应性区域发现βPP增加了βPP或其片段与淀粉样蛋白相关的可能性，并且Aβ的稳定性是其在淀粉样沉积物中占主导地位的原因。
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