Zheng Bo-Wen, Yang Li, Dai Xue-Ling, Jiang Zhao-Feng, Huang Han-Chang
a Beijing Key Laboratory of Bioactive Substances and Functional Foods , Beijing Union University , Beijing , P.R. China.
b College of Applied Sciences and Humanities of Beijing Union University , Beijing , P.R. China.
Neurol Res. 2016 Feb;38(2):177-86. doi: 10.1080/01616412.2015.1133485. Epub 2016 Mar 14.
Alzheimer disease (AD), a central nervous system degenerative disease, is characterized by abnormal deposition of amyloid-β peptide (Aβ), neurofibrillary tangles formed by hyperphosphorylated tau and synaptic loss. It is widely accepted that Aβ is the chief culprit of AD. Aβ peptide is the cleavage product of amyloid-β precursor protein (APP). Recently, more attention has been paid to O-linked β-N-acetylglucosaminylation (O-GlcNAcylation) modification of protein. O-GlcNAcylation plays a significant role in hippocampal synaptic function. Abated O-GlcNAcylation might be a modulator in progression of AD through regulating activity of pertinent enzymes and factors. Evidence suggests that enhanced O-GlcNAcylation interacts with tau phosphorylation and prevents brain from tau and Aβ-induced impairment. Here, we review the roles of O-GlcNAcylation in APP cleavage, tau phosphorylation and hippocampal synapses function.
阿尔茨海默病（AD）是一种中枢神经系统退行性疾病，其特征是β淀粉样肽（Aβ）异常沉积、由过度磷酸化的tau形成的神经原纤维缠结以及突触丧失。人们普遍认为Aβ是AD的主要元凶。Aβ肽是淀粉样β前体蛋白（APP）的裂解产物。最近，蛋白质的O-连接β-N-乙酰葡糖胺化（O-GlcNAcylation）修饰受到了更多关注。O-GlcNAcylation在海马突触功能中起重要作用。O-GlcNAcylation减弱可能通过调节相关酶和因子的活性而成为AD进展的调节因子。有证据表明，增强的O-GlcNAcylation与tau磷酸化相互作用，并防止大脑受到tau和Aβ诱导的损伤。在此，我们综述O-GlcNAcylation在APP裂解、tau磷酸化和海马突触功能中的作用。
