Clark I A, Vissel B
Biomedical Sciences and Biochemistry, Research School of Biology, Australian National University, Canberra, ACT, Australia.
Neurodegeneration Research Group, Garvan Institute, Sydney, NSW, Australia.
Br J Pharmacol. 2015 Aug;172(15):3714-27. doi: 10.1111/bph.13181. Epub 2015 Jun 29.
This review concerns how the primary inflammation preceding the generation of certain key damage-associated molecular patterns (DAMPs) arises in Alzheimer's disease (AD). In doing so, it places soluble amyloid β (Aβ), a protein hitherto considered as a primary initiator of AD, in a novel perspective. We note here that increased soluble Aβ is one of the proinflammatory cytokine-induced DAMPs recognized by at least one of the toll-like receptors on and in various cell types. Moreover, Aβ is best regarded as belonging to a class of DAMPs, as do the S100 proteins and HMBG1, that further exacerbate production of these same proinflammatory cytokines, which are already enhanced, and induces them further. Moreover, variation in levels of other DAMPs of this same class in AD may explain why normal elderly patients can exhibit high Aβ plaque levels, and why removing Aβ or its plaque does not retard disease progression. It may also explain why mouse transgenic models, having been designed to generate high Aβ, can be treated successfully by this approach.
本综述关注在阿尔茨海默病(AD)中,某些关键的损伤相关分子模式(DAMP)产生之前的原发性炎症是如何出现的。在此过程中,它将可溶性淀粉样β蛋白(Aβ)——一种迄今为止被视为AD主要启动因子的蛋白质——置于一个全新的视角。我们在此指出,可溶性Aβ增加是促炎细胞因子诱导的DAMP之一,可被多种细胞类型表面和内部的至少一种Toll样受体识别。此外,Aβ与S100蛋白和高迁移率族蛋白B1(HMBG1)一样,最好被视为一类DAMP,它们会进一步加剧这些已经增强的促炎细胞因子的产生,并进一步诱导它们。此外,AD中同一类别的其他DAMP水平的变化可能解释为什么正常老年患者会出现高Aβ斑块水平,以及为什么去除Aβ或其斑块并不能延缓疾病进展。这也可能解释为什么设计用于产生高Aβ的小鼠转基因模型可以通过这种方法成功治疗。