Soluble Aβ oligomer-induced synaptopathy: c-Jun N-terminal kinase's role

• 来源期刊: 分子细胞生物学报（英文版）
• 年，卷（期）: 2013,（4）
• 页码范围: 277-279
• 页数: 3页
• 语种: 英文
• DOI: 10.1093/jmcb/mjt015

摘要

Dear Editor, Among the neurodegenerative diseases,Alzheimer disease (AD) is the most common and severe age-related dementia for which there is currently no available treatment.Many studies support the assumption that AD is a spine pathology (Selkoe,2002;Sivanesan et al.,2013) and that soluble amyloid-β (Aβ) oligomers are causative of AD synaptopathy.Diverse lines of evidence indicate that Aβ oligomers induce formation of pore-like structures on the membrane (Arispe et al.,1993;Lashuel et al.,2002) and interfere with glutamatergic transmission.The Aβ oligomers result in a decreased number of AMPA receptors (AMPA-r) and NMDA receptors (NMDA-r),as well as PSD-95 at the postsynaptic membrane,and thus reduce the strength and plasticity of excitatory synapses (Chapman et al.,1999;Walsh et al.,2002).However,the underlying intracellular mechanisms regulating synaptic changes are only partially known.By understanding the pathophysiological mechanisms leading to synaptic dysfunction and the progression of this dysfunction,better interference in the pathogenesis of AD can be achieved.