The presenilin (PS) proteins are polytopic integral membrane proteins that are critically involved in the development of Alzheimer's disease. The topography of the PS molecule in the endoplasmic reticulum membrane is widely accepted as exhibiting eight-hydrophobic-transmembrane (8-TM) helices. We have previously provided evidence, however, that the intact PS molecule is also present in the cell surface where it exhibits exclusively a 7-TM topography, which differs in significant structural features from the 8-TM model. This evidence, however, has been disparaged and generally rejected by researchers in Alzheimer's disease. The 7-TM model is definitively demonstrated in the present study for PS-1 at the surfaces of PS-1-transfected cells and for endogenous PS-1 at the surfaces of untransfected cells, by immunofluorescence studies using mAbs. These studies force substantial revision of current views of the structural and functional properties of the PS proteins.

译文

早老素 (PS) 蛋白是多位整合膜蛋白,与阿尔茨海默氏病的发展密切相关。内质网膜中PS分子的形貌被广泛认为具有八个疏水跨膜 (8-TM) 螺旋。然而,我们以前已经提供了证据,表明完整的PS分子也存在于细胞表面,在那里它仅表现出7-TM形貌,其显着的结构特征与8-TM模型不同。然而,这一证据被阿尔茨海默氏病的研究人员贬低并普遍拒绝。通过使用mab的免疫荧光研究,在本研究中明确证明了在PS-1-transfected细胞表面的PS-1和在未转染细胞表面的内源性PS-1的7-TM模型。这些研究迫使对PS蛋白的结构和功能特性的当前观点进行了实质性修改。

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