Johnstone E M, Oltersdorf T, Bales K R, Chaney M O, Santerre R F, Little S P
Lilly Research Laboratories, A Division of Eli Lilly and Company Lilly Corporate Center, Indianapolis, IN 46285-0424.
Neurosci Lett. 1994 Oct 24;180(2):151-4. doi: 10.1016/0304-3940(94)90509-6.
The expression of the carboxyl-terminal 100 (C-100) residues of the amyloid precursor protein (APP) may provide a model for studying the processing of APP to the 42-43 residue beta-amyloid peptide (beta A4) implicated in Alzheimer's disease. Expression of human C-100 in mammalian cells reportedly causes 'toxicity' and amyloid-like fibrils. We have expressed the C-100 fragment in human embryonic kidney cells (293 cells) in a transient assay and compared it to the expression of transfected wild type and mutant (Swedish familial Alzheimer's disease) full length APP. Products were characterized by Western blot analysis using antibodies to the carboxyl-terminal region of APP.
淀粉样前体蛋白（APP）羧基末端100个（C-100）残基的表达可能为研究APP加工成与阿尔茨海默病相关的42 - 43个残基的β-淀粉样肽（βA4）提供一个模型。据报道，人C-100在哺乳动物细胞中的表达会导致“毒性”和淀粉样纤维。我们在瞬时分析中于人类胚胎肾细胞（293细胞）中表达了C-100片段，并将其与转染的野生型和突变型（瑞典家族性阿尔茨海默病）全长APP的表达进行了比较。使用针对APP羧基末端区域的抗体通过蛋白质免疫印迹分析对产物进行了表征。
