Sean M. Healey & AMG Center for ALS at Mass General, Massachusetts General Hospital, Boston, Massachusetts, USA.
Department of Neurology, Massachusetts General Hospital, Harvard Medical School, Boston, Massachusetts, USA.
Brain Pathol. 2022 Mar;32(2):e13035. doi: 10.1111/bpa.13035. Epub 2021 Nov 14.
Although the molecular mechanisms underlying amyotrophic lateral sclerosis (ALS) are not yet fully understood, several studies report alterations in tau phosphorylation in both sporadic and familial ALS. Recently, we have demonstrated that phosphorylated tau at S396 (pTau-S396) is mislocalized to synapses in ALS motor cortex (mCTX) and contributes to mitochondrial dysfunction. Here, we demonstrate that while there was no overall increase in total tau, pTau-S396, and pTau-S404 in ALS post-mortem mCTX, total tau and pTau-S396 were increased in C9ORF72-ALS. Additionally, there was a significant decrease in pTau-T181 in ALS mCTX compared controls. Furthermore, we leveraged the ALS Knowledge Portal and Project MinE data sets and identified ALS-specific genetic variants across MAPT, the gene encoding tau. Lastly, assessment of cerebrospinal fluid (CSF) samples revealed a significant increase in total tau levels in bulbar-onset ALS together with a decrease in CSF pTau-T181:tau ratio in all ALS samples, as reported previously. While increases in CSF tau levels correlated with a faster disease progression as measured by the revised ALS functional rating scale (ALSFRS-R), decreases in CSF pTau-T181:tau ratio correlated with a slower disease progression, suggesting that CSF total tau and pTau-T181 ratio may serve as biomarkers of disease in ALS. Our findings highlight the potential role of pTau-T181 in ALS, as decreases in CSF pTau-T181:tau ratio may reflect the significant decrease in pTau-T181 in post-mortem mCTX. Taken together, these results indicate that tau phosphorylation is altered in ALS post-mortem mCTX as well as in CSF and, importantly, the newly described pathogenic or likely pathogenic variants identified in MAPT in this study are adjacent to T181 and S396 phosphorylation sites further highlighting the potential role of these tau functional domains in ALS.
虽然肌萎缩侧索硬化症(ALS)的分子机制尚未完全阐明,但有几项研究报告称,散发性和家族性 ALS 中 tau 的磷酸化都发生了改变。最近,我们已经证明,S396 位磷酸化的 tau(pTau-S396)在 ALS 运动皮层(mCTX)中发生了异常定位,并导致线粒体功能障碍。在这里,我们证明,尽管 ALS 死后 mCTX 中的总 tau、pTau-S396 和 pTau-S404 没有总体增加,但 C9ORF72-ALS 中的总 tau 和 pTau-S396 增加了。此外,与对照组相比,ALS mCTX 中的 pTau-T181 显著减少。此外,我们利用 ALS 知识门户和 Project MinE 数据集,在编码 tau 的基因 MAPT 上鉴定出了 ALS 特异性遗传变异。最后,对脑脊液(CSF)样本的评估显示,延髓起病 ALS 患者的 CSF 总 tau 水平显著升高,与之前报道的一样,所有 ALS 样本中的 CSF pTau-T181:tau 比值降低。虽然 CSF tau 水平的升高与修订后的 ALS 功能评定量表(ALSFRS-R)测量的疾病进展更快相关,但 CSF pTau-T181:tau 比值的降低与疾病进展更慢相关,这表明 CSF 总 tau 和 pTau-T181 比值可能作为 ALS 疾病的生物标志物。我们的研究结果强调了 pTau-T181 在 ALS 中的潜在作用,因为 CSF pTau-T181:tau 比值的降低可能反映了死后 mCTX 中 pTau-T181 的显著减少。总之,这些结果表明,tau 磷酸化在 ALS 死后 mCTX 以及 CSF 中都发生了改变,而且重要的是,在本研究中在 MAPT 中发现的新描述的致病性或可能致病性变异位于 T181 和 S396 磷酸化位点附近,进一步突出了这些 tau 功能域在 ALS 中的潜在作用。