Huang Bo, Wu Qinxue, Zhou Hongxia, Huang Cao, Xia Xu-Gang
Department of Pathology, Thomas Jefferson University, Philadelphia, Pennsylvania, USA.
Department of Neurology, Thomas Jefferson University, Philadelphia, Pennsylvania, USA.
J Neurochem. 2016 Oct;139(2):285-293. doi: 10.1111/jnc.13748.
Pathogenic mutation of ubiquilin 2 (UBQLN2) causes neurodegeneration in amyotrophic lateral sclerosis and frontotemporal lobar degeneration. How UBQLN2 mutations cause the diseases is not clear. While over-expression of UBQLN2 with pathogenic mutation causes neuron death in rodent models, deletion of the Ubqln2 in rats has no effect on neuronal function. Previous findings in animal models suggest that UBQLN2 mutations cause the diseases mainly through a gain rather than a loss of functions. To examine whether the toxic gain in UBQLN2 mutation is related to the enhancement of UBQLN2 functions, we created new transgenic rats over-expressing wild-type human UBQLN2. Considering that human UBQLN2 may not function properly in the rat genome, we also created transgenic rats over-expressing rat's own Ubqln2. When over-expressed in rats, both human and rat wild-type Ubqln2 caused neuronal death and spatial learning deficits, the pathologies that were indistinguishable from those observed in mutant UBQLN2 transgenic rats. Over-expressed wild-type UBQLN2 formed protein inclusions attracting the autophagy substrate sequestosome-1 and the proteasome component 26S proteasome regulatory subunit 7. These findings suggest that excess UBQLN2 is toxic rather than protective to neurons and that the enhancement of UBQLN2 functions is involved in UBQLN2 pathogenesis. Pathogenic mutation in ubiquilin 2 (UBQLN2) causes neurodegeneration in ALS and FTLD. Studies in rodent models suggest a gain of toxic function in mutant UBQLN2. We created new transgenic rats as a relevant model and examined whether enhancing wild-type UBQLN2 expression is implicated in the pathogenesis of mutant UBQLN2. We observed that over-expression of human or rat wild-type Ubqln2 caused protein aggregation and neuronal death in transgenic rats. Our findings suggest that excess UBQLN2 is toxic rather than protective to neurons and that uncontrolled enhancement of UBQLN2 function is involved in UBQLN2 pathogenesis. Read the Editorial Highlight for this article on page 159.
泛素连接酶2(UBQLN2)的致病性突变会导致肌萎缩侧索硬化症和额颞叶痴呆中的神经退行性变。UBQLN2突变如何引发这些疾病尚不清楚。虽然具有致病性突变的UBQLN2过表达会在啮齿动物模型中导致神经元死亡,但大鼠中Ubqln2的缺失对神经元功能并无影响。先前在动物模型中的研究结果表明,UBQLN2突变主要通过功能获得而非功能丧失来引发疾病。为了研究UBQLN2突变中的毒性功能获得是否与UBQLN2功能增强有关,我们构建了过表达野生型人UBQLN2的新型转基因大鼠。考虑到人类UBQLN2在大鼠基因组中可能无法正常发挥功能,我们还构建了过表达大鼠自身Ubqln2的转基因大鼠。当在大鼠中过表达时,人类和大鼠野生型Ubqln2均导致神经元死亡和空间学习缺陷,这些病理表现与在突变型UBQLN2转基因大鼠中观察到的无法区分。过表达的野生型UBQLN2形成蛋白聚集体,吸引自噬底物p62和蛋白酶体组分26S蛋白酶体调节亚基7。这些发现表明,过量的UBQLN2对神经元具有毒性而非保护作用,并且UBQLN2功能的增强参与了UBQLN2的发病机制。泛素连接酶2(UBQLN2)中的致病性突变会导致肌萎缩侧索硬化症(ALS)和额颞叶痴呆(FTLD)中的神经退行性变。啮齿动物模型研究表明突变型UBQLN2具有毒性功能获得。我们构建了新型转基因大鼠作为相关模型,并研究增强野生型UBQLN2表达是否与突变型UBQLN2的发病机制有关。我们观察到人类或大鼠野生型Ubqln2的过表达在转基因大鼠中导致蛋白聚集和神经元死亡。我们的发现表明,过量的UBQLN2对神经元具有毒性而非保护作用,并且UBQLN2功能的失控增强参与了UBQLN2的发病机制。阅读本期第159页关于本文的编辑推荐。