Department of Neuroscience, Mayo Clinic Jacksonville, Jacksonville, Florida, United States of America.
PLoS One. 2013 Jul 26;8(7):e69864. doi: 10.1371/journal.pone.0069864. Print 2013.
Tar DNA binding protein 43 (TDP-43) is the major component of pathological deposits in frontotemporal lobar degeneration with TDP-43 inclusions (FTLD-TDP) and in amyotrophic lateral sclerosis (ALS). It has been reported that TDP-43 transgenic mouse models expressing human TDP-43 wild-type or ALS-associated mutations recapitulate certain ALS and FTLD pathological phenotypes. Of note, expression of human TDP-43 (hTDP-43) reduces the levels of mouse Tdp-43 (mTdp-43). However, it remained unclear whether the mechanisms through which TDP-43 induces ALS or FTLD-like pathologies resulted from a reduction in mTdp-43, an increase in hTDP-43, or a combination of both. In elucidating the role of mTdp-43 and hTDP-43 in hTDP-43 transgenic mice, we observed that reduction of mTdp-43 in non-transgenic mice by intraventricular brain injection of AAV1-shTardbp leads to a dramatic increase in the levels of splicing variants of mouse sortilin 1 and translin. However, the levels of these two abnormal splicing variants are not increased in hTDP-43 transgenic mice despite significant downregulation of mTdp-43 in these mice. Moreover, further downregulation of mTdp-43 in hTDP-43 hemizygous mice, which are asymptomatic, to the levels equivalent to that of mTdp-43 in hTDP-43 homozygous mice does not induce the pathological phenotypes observed in the homozygous mice. Lastly, the number of dendritic spines and the RNA levels of TDP-43 RNA targets critical for synapse formation and function are significantly decreased in symptomatic homozygous mice. Together, our findings indicate that mTdp-43 downregulation does not lead to a loss of function mechanism or account for the pathological phenotypes observed in hTDP-43 homozygous mice because hTDP-43 compensates for the reduction, and associated functions of mTdp-43. Rather, expression of hTDP-43 beyond a certain threshold leads to abnormal metabolism of TDP-43 RNA targets critical for neuronal structure and function, which might be responsible for the ALS or FTLD-like pathologies observed in homozygous hTDP-43 transgenic mice.
TDP-43 是额颞叶变性伴 TDP-43 包涵体(FTLD-TDP)和肌萎缩性侧索硬化症(ALS)的主要病变沉积成分。据报道,表达人 TDP-43 野生型或 ALS 相关突变的 TDP-43 转基因小鼠模型可再现某些 ALS 和 FTLD 病理表型。值得注意的是,人 TDP-43(hTDP-43)的表达降低了鼠 Tdp-43(mTdp-43)的水平。然而,TDP-43 诱导 ALS 或 FTLD 样病变的机制是否是由于 mTdp-43 的减少、hTDP-43 的增加,还是两者的结合,目前尚不清楚。在阐明 mTdp-43 和 hTDP-43 在 hTDP-43 转基因小鼠中的作用时,我们观察到,通过脑室脑内注射 AAV1-shTardbp 降低非转基因小鼠中的 mTdp-43 水平会导致小鼠 sortilin 1 和 translin 的剪接变体水平显著增加。然而,尽管这些小鼠中 mTdp-43 显著下调,但这些异常剪接变体的水平并未增加。此外,尽管 hTDP-43 半合子小鼠无症状,但进一步下调 mTdp-43 至与 hTDP-43 纯合子小鼠中 mTdp-43 水平相当,也不会诱导纯合子小鼠中观察到的病理表型。最后,在有症状的纯合子小鼠中,树突棘的数量和对突触形成和功能至关重要的 TDP-43 RNA 靶标的 RNA 水平显著降低。综上所述,我们的研究结果表明,mTdp-43 的下调不会导致功能丧失机制或解释 hTDP-43 纯合子小鼠中观察到的病理表型,因为 hTDP-43 可以补偿 mTdp-43 的减少及其相关功能。相反,表达超过一定阈值的 hTDP-43 会导致对神经元结构和功能至关重要的 TDP-43 RNA 靶标的异常代谢,这可能是导致纯合子 hTDP-43 转基因小鼠中观察到的 ALS 或 FTLD 样病变的原因。