Piccardo P, Dagenais A, Cuello A C, St-Pierre S, Nalbantoglu J
Department of Pharmacology and Therapeutics, McGill University, Montreal, Quebec, Canada.
Histochemistry. 1993 May;99(5):347-53. doi: 10.1007/BF00717046.
The Alzheimer's disease amyloid precursor protein (APP) consists of several isoforms, which are extensively post-translationally modified and processed. A monoclonal antibody, MAbE1, was raised against a synthetic peptide from an extracellular domain that is common to all isoforms of APP. Immunoblots and immunolocalization studies on cells of neuronal and other origins demonstrated that this antibody recognized a subclass of APP isoforms when compared to a monoclonal antibody raised against a bacterial fusion protein of APP, MAb22C11. Prominent protein bands of 71 kDa and 120 kDa were only detected on immunoblots of cell lysates and no immunoreactivity was observed in protein samples obtained from cell conditioned media. Immunofluorescence labelling with MAbE1 revealed predominantly perinuclear staining of cells of neuronal and glial origin. The data suggest that this monoclonal antibody detects distinct conformational isoforms of APP present in intracellular compartments.
阿尔茨海默病淀粉样前体蛋白（APP）由几种亚型组成，这些亚型经过广泛的翻译后修饰和加工。一种单克隆抗体MAbE1是针对APP所有亚型共有的细胞外结构域的合成肽产生的。对神经元和其他来源细胞的免疫印迹和免疫定位研究表明，与针对APP细菌融合蛋白产生的单克隆抗体MAb22C11相比，该抗体识别APP亚型的一个亚类。仅在细胞裂解物的免疫印迹上检测到71 kDa和120 kDa的显著蛋白条带，而在从细胞条件培养基获得的蛋白质样品中未观察到免疫反应性。用MAbE1进行的免疫荧光标记显示，神经元和胶质细胞来源的细胞主要呈核周染色。数据表明，这种单克隆抗体可检测细胞内区室中存在的APP不同构象亚型。
