Stevens Neuroimaging and Informatics Institute, Keck School of Medicine, University of Southern California, Los Angeles, CA 90033, USA.
Centre for Medical Image Computing, Department of Medical Physics and Biomedical Engineering, University College London, London WC1V 6LJ, UK.
Brain. 2023 Dec 1;146(12):4935-4948. doi: 10.1093/brain/awad232.
Amyloid-β is thought to facilitate the spread of tau throughout the neocortex in Alzheimer's disease, though how this occurs is not well understood. This is because of the spatial discordance between amyloid-β, which accumulates in the neocortex, and tau, which accumulates in the medial temporal lobe during ageing. There is evidence that in some cases amyloid-β-independent tau spreads beyond the medial temporal lobe where it may interact with neocortical amyloid-β. This suggests that there may be multiple distinct spatiotemporal subtypes of Alzheimer's-related protein aggregation, with potentially different demographic and genetic risk profiles. We investigated this hypothesis, applying data-driven disease progression subtyping models to post-mortem neuropathology and in vivo PET-based measures from two large observational studies: the Alzheimer's Disease Neuroimaging Initiative (ADNI) and the Religious Orders Study and Rush Memory and Aging Project (ROSMAP). We consistently identified 'amyloid-first' and 'tau-first' subtypes using cross-sectional information from both studies. In the amyloid-first subtype, extensive neocortical amyloid-β precedes the spread of tau beyond the medial temporal lobe, while in the tau-first subtype, mild tau accumulates in medial temporal and neocortical areas prior to interacting with amyloid-β. As expected, we found a higher prevalence of the amyloid-first subtype among apolipoprotein E (APOE) ε4 allele carriers while the tau-first subtype was more common among APOE ε4 non-carriers. Within tau-first APOE ε4 carriers, we found an increased rate of amyloid-β accumulation (via longitudinal amyloid PET), suggesting that this rare group may belong within the Alzheimer's disease continuum. We also found that tau-first APOE ε4 carriers had several fewer years of education than other groups, suggesting a role for modifiable risk factors in facilitating amyloid-β-independent tau. Tau-first APOE ε4 non-carriers, in contrast, recapitulated many of the features of primary age-related tauopathy. The rate of longitudinal amyloid-β and tau accumulation (both measured via PET) within this group did not differ from normal ageing, supporting the distinction of primary age-related tauopathy from Alzheimer's disease. We also found reduced longitudinal subtype consistency within tau-first APOE ε4 non-carriers, suggesting additional heterogeneity within this group. Our findings support the idea that amyloid-β and tau may begin as independent processes in spatially disconnected regions, with widespread neocortical tau resulting from the local interaction of amyloid-β and tau. The site of this interaction may be subtype-dependent: medial temporal lobe in amyloid-first, neocortex in tau-first. These insights into the dynamics of amyloid-β and tau may inform research and clinical trials that target these pathologies.
淀粉样蛋白-β 被认为有助于在阿尔茨海默病的新皮质中扩散 tau,尽管其具体机制尚不清楚。这是因为淀粉样蛋白-β 在新皮质中积累,而 tau 在衰老过程中在颞叶内侧部积累,两者的空间分布不同。有证据表明,在某些情况下,淀粉样蛋白-β 独立的 tau 会扩散到颞叶内侧部以外的区域,在那里它可能与新皮质中的淀粉样蛋白-β 相互作用。这表明可能存在多种不同的与阿尔茨海默病相关的蛋白聚集的时空亚型,具有潜在不同的人口统计学和遗传风险特征。我们通过应用数据驱动的疾病进展亚型模型,对来自两项大型观察性研究(阿尔茨海默病神经影像学倡议[ADNI]和宗教秩序研究和拉什记忆与衰老项目[ROSMAP])的死后神经病理学和体内正电子发射断层扫描(PET)基于测量数据进行了研究。我们使用两项研究的横断面信息一致地识别出“淀粉样蛋白-β 优先”和“tau 优先”两种亚型。在淀粉样蛋白-β 优先亚型中,广泛的新皮质淀粉样蛋白-β 先于 tau 扩散到颞叶内侧部之外,而在 tau 优先亚型中,轻度 tau 会在颞叶内侧和新皮质区域积累,然后再与淀粉样蛋白-β 相互作用。正如预期的那样,我们发现载脂蛋白 E(APOE)ε4 等位基因携带者中“淀粉样蛋白-β 优先”亚型的患病率更高,而 APOE ε4 非携带者中“tau 优先”亚型更为常见。在 tau 优先的 APOE ε4 携带者中,我们发现淀粉样蛋白-β 的积累速度增加(通过纵向淀粉样蛋白 PET),这表明这个罕见的群体可能属于阿尔茨海默病连续体。我们还发现,tau 优先的 APOE ε4 携带者的受教育年限比其他群体少几年,这表明可改变的风险因素在促进淀粉样蛋白-β 独立的 tau 中起作用。相比之下,tau 优先的 APOE ε4 非携带者再现了许多原发性年龄相关性 tau 病的特征。该组中通过 PET 测量的纵向淀粉样蛋白-β 和 tau 积累率(均通过 PET 测量)与正常衰老没有差异,支持将原发性年龄相关性 tau 病与阿尔茨海默病区分开来。我们还发现,tau 优先的 APOE ε4 非携带者的纵向亚型一致性降低,这表明该组内存在额外的异质性。我们的研究结果支持这样的观点,即淀粉样蛋白-β 和 tau 可能首先在空间上不连续的区域独立发生,广泛的新皮质 tau 是由淀粉样蛋白-β 和 tau 的局部相互作用引起的。这种相互作用的部位可能取决于亚型:淀粉样蛋白-β 优先的部位是颞叶内侧,tau 优先的部位是新皮质。这些关于淀粉样蛋白-β 和 tau 动态的见解可能会为针对这些病理学的研究和临床试验提供信息。