Sequestration of amyloid beta-peptide.
Sequestration of amyloid beta-peptide.
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淀粉样β-肽的隔离。
DOI：
10.1111/j.1749-6632.1993.tb23042.x
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发表时间：
1993
影响因子：
5.2
通讯作者：
Strittmatter,WJ
中科院分区：
文献类型：
--
作者：
Goldgaber,D;Schwarzman,AI;Bhasin,R;Gregori,L;Schmechel,D;Saunders,AM;Roses,AD;Strittmatter,WJ
淀粉样蛋白β-蛋白，或β/A4，是一种4kodalton的多肽，在阿尔茨海默病(AD)、唐氏综合征(DS)和遗传性脑出血伴淀粉样变性-荷兰型(HCHWA-D)患者的大脑和软脑膜中形成难溶的淀粉样蛋白沉积。β/A4肽是一种大跨膜糖蛋白(APP)的衍生物，存在于细胞外空间，即AD患者和非AD患者的脑脊液和血清中，以及多种不同细胞培养的条件培养液中。1正常情况下产生的淀粉样蛋白β肽在患者体内形成细胞外聚集体的机制尚不清楚。一种可能的解释是β/A4肽的去除机制失败，该机制阻止这种高聚集的肽形成细胞外淀粉样蛋白沉积。
Amyloid β‐protein, or β/A4, is a 4‐kilodalton peptide that forms poorly soluble extracellular depositions of amyloid in brains and leptomeninges of patients with Alzheimer's disease (AD), Down's syndrome (DS), and hereditary cerebral hemorrhage with amyloidosis‐Dutch type (HCHWA‐D). β/A4 peptide is a derivative of a large transmembrane glycoprotein (APP) and is found in the extracellular space,i.e., in the cerebrospinal fluid and serum of individuals with and without AD and in the conditioned media of many different cells grown in culture.1The mechanism by which normally produced amyloid β peptide forms extracellular aggregates in patients is unknown. One possible explanation is a failure of a mechanism for removal of the β/A4 peptide that prevents this highly aggregating peptide from forming extracellular amyloid depositions.