Department Medical Biotechnologies and Translational Medicine, Università of Milano, Via F.lli Cervi, 93, 20090 Segrate (MI), Italy.
Department of Molecular Biochemistry and Pharmacology, Istituto di Ricerche Farmacologiche Mario Negri IRCCS, Via Mario Negri, 2, 20156 Milano, Italy.
Int J Mol Sci. 2020 Nov 5;21(21):8295. doi: 10.3390/ijms21218295.
The physiological and pathological roles of nascent amyloid beta (Aβ) monomers are still debated in the literature. Their involvement in the pathological route of Alzheimer's Disease (AD) is currently considered to be the most relevant, triggered by their aggregation into structured oligomers, a toxic species. Recently, it has been suggested that nascent Aβ, out of the amyloidogenic pathway, plays a physiological and protective role, especially in the brain. In this emerging perspective, the study presented in this paper investigated whether the organization of model membranes is affected by contact with Aβ in the nascent state, as monomers. The outcome is that, notably, the rules of engagement and the resulting structural outcome are dictated by the composition and properties of the membrane, rather than by the Aβ variant. Interestingly, Aβ monomers are observed to favor the tightening of adjacent complex membranes, thereby affecting a basic structural event for cell-cell adhesion and cell motility.
在文献中，新生淀粉样β（Aβ）单体的生理和病理作用仍存在争议。目前认为，它们在阿尔茨海默病（AD）的病理途径中最为相关，由其聚集形成结构寡聚体，这是一种有毒物质。最近，有研究表明，新生 Aβ 脱离淀粉样蛋白生成途径，发挥着生理和保护作用，尤其是在大脑中。在这种新出现的观点中，本文研究了与处于新生状态的 Aβ单体接触是否会影响模型膜的组织，结果表明，值得注意的是，结合的规则和产生的结构结果取决于膜的组成和性质，而不是 Aβ 变体。有趣的是，观察到 Aβ 单体有利于使相邻的复合膜收紧，从而影响细胞-细胞黏附和细胞迁移的基本结构事件。
