Hamazaki H
Department of Biology, Kitasato University School of Medicine, Kanagawa, Japan.
FEBS Lett. 1996 Nov 4;396(2-3):139-42. doi: 10.1016/0014-5793(96)01087-3.
The cerebral deposition of 39-42 residue amyloid beta-protein (Abeta) is a histopathological characteristic of Alzheimer's disease. The present study is aimed at finding proteinases responsible for the intracellular clearance of Abeta. The Abeta-degrading proteinase was purified from rat brain. Amino-terminal sequence analysis indicated the Abeta-degrading proteinase was cathepsin D. Purified cathepsin D hydrolyzed Abeta between Phe19 and Phe20. Cathepsin D is likely to be involved in the intracellular clearance of aggregatable Abeta, since Abeta fragments with Phe20 at the amino-terminus have been reported to be secreted from several lines of cultured cells.
由39 - 42个氨基酸残基组成的β-淀粉样蛋白（Aβ）在大脑中的沉积是阿尔茨海默病的组织病理学特征。本研究旨在寻找负责细胞内清除Aβ的蛋白酶。从大鼠脑中纯化出了降解Aβ的蛋白酶。氨基末端序列分析表明，降解Aβ的蛋白酶是组织蛋白酶D。纯化的组织蛋白酶D在苯丙氨酸19和苯丙氨酸20之间水解Aβ。组织蛋白酶D可能参与了可聚集Aβ的细胞内清除，因为据报道，氨基末端带有苯丙氨酸20的Aβ片段可从多种培养细胞系中分泌出来。
