Trypsin interaction with the senile plaques of Alzheimer disease is mediated by beta-protein precursor.
Trypsin interaction with the senile plaques of Alzheimer disease is mediated by beta-protein precursor.
复制标题
胰蛋白酶与阿尔茨海默病老年斑的相互作用是由β-蛋白前体介导的。
DOI：
10.1007/bf02815090
复制
发表时间：
1996
期刊：
影响因子：
--
通讯作者：
Perry,G
中科院分区：
文献类型：
--
作者：
Smith,MA;Dunbar,CE;Miller,EJ;Perry,G
In this study we demonstrate byin situbinding that trypsin interacts with the senile plaques found in Alzheimer disease. Characterization of various potential trypsin binding proteins shows that trypsin binding is mediated by β-protein precursor (βPP)—the progenitor of amyloid-β in senile plaques. Using specific antisera against various proteins to sterically block trypsin blocking, we found that only those antibodies raised against proteins or peptides containing the Kunitz protease inhibitor domain were able to abolish binding. By analogy with other protease/inhibitor interactions, we speculate that the binding of trypsin to βPP could involve concomitant βPP cleavage. Therefore, βPP in protecting against potentially damaging proteolysis could simultaneously liberate βPP fragments or intermediate precursors of amyloid-β deposits.
