Munro Kathryn M, Nash Amelia, Pigoni Martina, Lichtenthaler Stefan F, Gunnersen Jenny M
Department of Anatomy and Neuroscience, School of Biomedical Sciences, The University of Melbourne, Parkville, Melbourne, Australia.
Deutsches Zentrum für Neurodegenerative Erkrankungen (DZNE), Munich, Germany.
J Mol Neurosci. 2016 Nov;60(3):305-315. doi: 10.1007/s12031-016-0800-1. Epub 2016 Jul 25.
Inhibition of the protease β-site amyloid precursor protein-cleaving enzyme 1 (BACE1) is a promising treatment strategy for Alzheimer's disease, and a number of BACE inhibitors are currently progressing through clinical trials. The strategy aims to decrease production of amyloid-β (Aβ) peptide from the amyloid precursor protein (APP), thus reducing or preventing Aβ toxicity. Over the last decade, it has become clear that BACE1 proteolytically cleaves a number of substrates in addition to APP. These substrates are not known to be involved in the pathogenesis of Alzheimer's disease but have other roles in the developing and/or mature central nervous system. Consequently, BACE inhibition and knockout in mice results in synaptic and other neuronal dysfunctions and the key substrates responsible for these deficits are still being elucidated. Of the BACE1 substrates that have been validated to date, a number may contribute to the synaptic deficits seen with BACE blockade, including neuregulin 1, close homologue of L1 and seizure-related gene 6. It is important to understand the impact that BACE blockade may have on these substrates and other proteins detected in substrate screens and, if necessary, develop substrate-selective BACE inhibitors.
抑制蛋白酶β-分泌酶1(BACE1)是治疗阿尔茨海默病的一种很有前景的策略,目前有多种BACE抑制剂正处于临床试验阶段。该策略旨在减少淀粉样前体蛋白(APP)生成β淀粉样蛋白(Aβ)肽,从而降低或预防Aβ毒性。在过去十年中,已经明确BACE1除了切割APP外,还能蛋白水解切割多种底物。这些底物并不参与阿尔茨海默病的发病机制,但在发育中和/或成熟的中枢神经系统中具有其他作用。因此,小鼠体内BACE的抑制和基因敲除会导致突触及其他神经元功能障碍,而导致这些缺陷的关键底物仍在研究中。在迄今已得到验证的BACE1底物中,有一些可能导致BACE阻断后出现的突触缺陷,包括神经调节蛋白1、L1紧密同源物和癫痫相关基因6。了解BACE阻断对这些底物以及在底物筛选中检测到的其他蛋白质可能产生的影响,并在必要时开发底物选择性BACE抑制剂,这很重要。