Kitazume Shinobu, Saido Takaomi C, Hashimoto Yasuhiro
Glyco-chain Functions Laboratory, Frontier Research System and Laboratory for Proteolytic Neuroscience, Brain Science Institute, RIKEN, 2-1 Hirosawa, Wako-shi, Saitama 351-0198, Japan.
Glycoconj J. 2004;20(1):59-62. doi: 10.1023/B:GLYC.0000016743.25495.45.
Alzheimer's beta-secretase (BACE1) is a membrane-bound protease that cleaves the amyloid precursor protein (APP) in the trans-Golgi network, an initial step in the pathogenesis of Alzheimer's disease. Although BACE1 is distributed among various tissues including brain, its physiological substrate other than APP have not been identified. We have recently found that when BACE1 was overexpressed in COS cells together with alpha2,6-sialyltransferase (ST6Gal I), the secretion of ST6Gal I markedly increased, suggesting that BACE1 cleaves ST6Gal I as a physiological substrate. Thus BACE1 is the first identified protease that is responsible for the cleavage and secretion of glycosyltransferases.
阿尔茨海默病β-分泌酶(BACE1)是一种膜结合蛋白酶,可在反式高尔基体网络中切割淀粉样前体蛋白(APP),这是阿尔茨海默病发病机制的起始步骤。尽管BACE1分布于包括脑在内的各种组织中,但其除APP之外的生理底物尚未被鉴定。我们最近发现,当BACE1与α2,6-唾液酸转移酶(ST6Gal I)在COS细胞中共同过表达时,ST6Gal I的分泌显著增加,这表明BACE1将ST6Gal I作为生理底物进行切割。因此,BACE1是首个被鉴定出的负责糖基转移酶切割和分泌的蛋白酶。