Soluble derivatives of the beta amyloid protein precursor of Alzheimer's disease are labeled by antisera to the beta amyloid protein.
Soluble derivatives of the beta amyloid protein precursor of Alzheimer's disease are labeled by antisera to the beta amyloid protein.
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阿尔茨海默病的β淀粉样蛋白前体的可溶性衍生物被β淀粉样蛋白的抗血清标记。
DOI：
10.1016/0006-291x(89)91052-8
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发表时间：
1989
影响因子：
3.1
通讯作者：
Younkin,SG
中科院分区：
文献类型：
--
作者：
Palmert,MR;Siedlak,SL;Podlisny,MB;Greenberg,B;Shelton,ER;Chan,HW;Usiak,M;Selkoe,DJ;Perry,G;Younkin,SG
阿尔茨海默病（AD）中沉积的淀粉样蛋白主要由39-42个残基的多肽（βAP）组成，所述β AP衍生自较大的β淀粉样蛋白前体（βAPP）。在以前的研究中，我们和其他人鉴定了βAPP的全长膜相关形式，并表明这些形式被加工成缺乏全长形式羧基末端的可溶性衍生物。在这份报告中，我们证明了在人脑脊液中发现的βAPP的可溶性β 125和β 105 kDa形式被几种不同的βAP抗血清特异性标记。这一发现表明，这两种可溶性衍生物都含有全部或部分βAP序列，这表明这些形式中的一种或两种可能是AD中沉积的淀粉样蛋白的直接前体。
The amyloid deposited in Alzheimer's disease (AD) is composed primarily of a 39–42 residue polypeptide (βAP) that is derived from a larger β amyloid protein precursor (βAPP). In previous studies, we and others identified full-length, membrane-associated forms of the βAPP and showed that these forms are processed into soluble derivatives that lack the carboxyl-terminus of the full-length forms. In this report, we demonstrate that the soluble ∼125 and ∼105 kDa forms of the βAPP found in human cerebrospinal fluid are specifically labeled by several different antisera to the βAP. This finding indicates that both soluble derivatives contain all or part of the βAP sequence, and it suggests that one or both of these forms may be the immediate precursor of the amyloid deposited in AD.