EVIDENCE THAT BETA-AMYLOID PROTEIN IN ALZHEIMERS-DISEASE IS NOT DERIVED BY NORMAL PROCESSING
EVIDENCE THAT BETA-AMYLOID PROTEIN IN ALZHEIMERS-DISEASE IS NOT DERIVED BY NORMAL PROCESSING
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DOI：
10.1126/science.1691865
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发表时间：
1990-04-27
期刊：
影响因子：
56.9
通讯作者：
PRICE, DL
中科院分区：
文献类型：
--
作者：
SISODIA, SS;KOO, EH;PRICE, DL
β-淀粉样蛋白（β/ A4），来源于较大的淀粉样前体蛋白（APP），是阿尔茨海默病老年斑的主要成分。APP是一种完整的膜糖蛋白，并作为羧基末端截短的分子分泌。作为膜相关事件的APP裂解发生在位于β/β细胞内的位点。A4区。这表明完整的淀粉样蛋白生成β/正常APP catalysts过程中不产生A4片段。因此，淀粉样蛋白形成中的早期事件可能涉及改变的APP加工，其导致完整的β-淀粉样蛋白的释放和随后的沉积。A4.
The .beta.-amyloid protein (.beta./A4), derived from a larger amyloid precursor protein (APP), is the principal component of senile plaques in Alzheimer''s disease. APP is an integral membrane glycoprotein and is secreted as a carboxyl-terminal truncated molecule. APP cleavage, which is a membrane-associated event, occurred at a site located within the .beta./A4 region. This suggests that an intact amyloidogenic .beta./A4 fragment is not generated during normal APP catabolism. Therefore, an early event in amyloid formation may involve altered APP processing that results in the release and subsequent deposition of intact .beta./A4.