New biochemical insights to unravel the pathogenesis of Alzheimer's lesions.
New biochemical insights to unravel the pathogenesis of Alzheimer's lesions.
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揭示阿尔茨海默病病变发病机制的新生化见解。
DOI：
10.1017/s0317167100032558
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发表时间：
1991
期刊：
影响因子：
--
通讯作者：
Ball,MJ
中科院分区：
文献类型：
--
作者：
Roher,AE;Palmer,KC;Capodilupo,J;Wakade,AR;Ball,MJ
从阿尔茨海默氏病脑中纯化淀粉样斑块核心蛋白（APCP），使其完全同质，并以高产率进行化学分离和表征其组分。APCP主要由β-淀粉样蛋白（βA）和各种糖蛋白（占20%）组成，这些糖蛋白富含与N-和O-连接的淀粉酶相容的碳水化合物。当加入到交感神经元和感觉神经元的组织培养物中时，APCP和βA抑制神经炎发芽，这是一种低剂量的可逆现象。这两种物质的高浓度杀死培养中的神经元。APCP的毒性明显高于βA，提示微量组分可能在增加βA毒性中起重要作用。如果观察到的APCP在原位的毒性作用发生在体内AD的过程中，那么这些细胞外蛋白的积累可能是主要负责在这种神经病理学中观察到的一些神经元死亡。
Purification of amyloid plaque core proteins (APCP) from Alzheimer's disease brains to complete homogeneity and in high yield permitted its chemical fractionation and characterization of its components. APCP is mainly made of β-amyloid (βA) and an assortment of glycoproteins (accounting for 20%) rich in carbohydrates compatible with N-and O-linked saccharides. When added to tissue culture of sympathetic and sensory neurons APCP and βA inhibited neuritic sprouting, a reversible phenomenon at low doses. Higher concentrations of both substances kill the neurons in culture. APCP is significantly more toxic than βA, suggesting the minor components may play an important role in increasing the toxicity of βA. If the observed toxic effects of APCP in situ are occurring in vivo during the course of AD, then the accumulation of these extracellular proteins could be largely responsible for some of the neuronal death observed in this neuropathology.