AMYLOID PLAQUE CORE PROTEIN IN ALZHEIMER-DISEASE AND DOWN SYNDROME
AMYLOID PLAQUE CORE PROTEIN IN ALZHEIMER-DISEASE AND DOWN SYNDROME
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DOI：
10.1073/pnas.82.12.4245
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发表时间：
1985-01-01
影响因子：
11.1
通讯作者：
BEYREUTHER, K
中科院分区：
文献类型：
--
作者：
MASTERS, CL;SIMMS, G;BEYREUTHER, K
脑淀粉样蛋白，在阿尔茨海默病和唐氏综合征的老年人中形成斑块核心，被纯化和表征。该蛋白质由约40个残基（4 kDa [千道尔顿]）的多肽的多聚体聚集体组成。这种淀粉样蛋白的氨基酸组成、分子量和NH 2-末端序列几乎与阿尔茨海默病和唐氏综合征的嗜酸性血管病中沉积的淀粉样蛋白相同，但斑块核心蛋白的NH 2末端参差不齐。共有的4-kDa亚基表明斑块核心和嗜酸性血管病的淀粉样蛋白的共同来源。斑块核心的溶解性特征与羊瘙痒病感染性的某些特性之间存在表面相似性，但斑块核心与羊瘙痒病多肽之间的氨基酸序列没有相似性。
The cerebral amyloid protein that forms the plaque core in Alzheimer''s disease and in aged individuals with Down''s syndrome was purified and characterized. The protein consists of multimeric aggregates of a polypeptide of about 40 residues (4 kDa [kilodalton]). The amino acid composition, molecular mass, and NH2-terminal sequence of this amyloid protein are almost identical to those described for the amyloid deposited in the congophilic angiopathy of Alzheimer''s disease and Down''s syndrome, but the plaque core proteins have ragged NH2 termini. The shared 4-kDa subunit indicates a common origin for the amyloids of the plaque core and of the congophilic angiopathy. There are superficial resemblances between the solubility characteristics of the plaque core and some of the properties of scrapie infectivity, but there are no similarities in amino acid sequences between the plaque core and scrapie polypeptides.