Yanagisawa K, Ihara Y, Miyatake T
Department of Neurology, School of Medicine, Tokyo Medical and Dental University, Japan.
Neurosci Lett. 1992 Sep 14;144(1-2):43-5. doi: 10.1016/0304-3940(92)90711-f.
To determine whether the secretory pathway of beta/A4 amyloid protein precursor (APP) was altered in familial Alzheimer's disease (FAD) with a mutation of Val717 to Ile, cerebrospinal fluid was studied by Western blotting. The ratio of the density of the bands labeled with the antibody against the amino-terminal part of beta/A4 protein to that with the antibody against amino-terminal part of beta/A4 protein to that with the antibody against amino-terminal part of APP was not decreased. The present result suggests that the secretory pathway is not altered by the mutation in such a way that amyloidogenic full-length beta/A4 protein is generated.
为了确定伴有缬氨酸717突变为异亮氨酸的家族性阿尔茨海默病（FAD）中β/A4淀粉样蛋白前体（APP）的分泌途径是否改变，通过蛋白质免疫印迹法对脑脊液进行了研究。用针对β/A4蛋白氨基末端部分的抗体标记的条带密度与用针对APP氨基末端部分的抗体标记的条带密度之比并未降低。目前的结果表明，该突变并未以产生淀粉样变性全长β/A4蛋白的方式改变分泌途径。
