Department of Neurology, Chiba East National Hospital, 673 Nitona, Chuo Ward, Chiba, Chiba 260-8712, Japan.
J Neurol Neurosurg Psychiatry. 2013 Jul;84(7):784-95. doi: 10.1136/jnnp-2012-303144. Epub 2012 Oct 20.
Based on the amyloid hypothesis, controlling β-amyloid protein (Aβ) accumulation is supposed to suppress downstream pathological events, tau accumulation, neurodegeneration and cognitive decline. However, in recent clinical trials, Aβ removal or reducing Aβ production has shown limited efficacy. Moreover, while active immunisation with Aβ resulted in the clearance of Aβ, it did not prevent tau pathology or neurodegeneration. This prompts the concern that it might be too late to employ Aβ targeting therapies once tau mediated neurodegeneration has occurred. Therefore, it is timely and very important to develop tau directed therapies. The pathomechanisms of tau mediated neurodegeneration are unclear but hyperphosphorylation, oligomerisation, fibrillisation and propagation of tau pathology have been proposed as the likely pathological processes that induce loss of function or gain of toxic function of tau, causing neurodegeneration. Here we review the strategies for tau directed treatments based on recent progress in research on tau and our understanding of the pathomechanisms of tau mediated neurodegeneration.
基于淀粉样蛋白假说,控制β-淀粉样蛋白(Aβ)的积累被认为可以抑制下游的病理事件、tau 蛋白的积累、神经退行性变和认知能力下降。然而,最近的临床试验表明,Aβ 的清除或减少 Aβ 的产生效果有限。此外,虽然用 Aβ 进行主动免疫可以清除 Aβ,但并不能预防 tau 病理或神经退行性变。这引发了人们的担忧,一旦 tau 介导的神经退行性变发生,使用 Aβ 靶向治疗可能为时已晚。因此,开发靶向 tau 的治疗方法是及时和非常重要的。tau 介导的神经退行性变的发病机制尚不清楚,但 tau 蛋白的过度磷酸化、寡聚化、纤维形成和病理传播被认为是导致 tau 蛋白功能丧失或获得毒性功能的可能病理过程,从而导致神经退行性变。在这里,我们根据 tau 研究的最新进展以及我们对 tau 介导的神经退行性变发病机制的理解,综述了靶向 tau 的治疗策略。