Hogg Marion C, Mitchem Mollie R, König Hans-Georg, Prehn Jochen H M
Centre for the Study of Neurological Disorders, Royal College of Surgeons In Ireland, St. Stephen's Green, Dublin 2, Ireland; Department of Physiology and Medical Physics, Royal College of Surgeons In Ireland, St. Stephen's Green, Dublin 2, Ireland.
Centre for the Study of Neurological Disorders, Royal College of Surgeons In Ireland, St. Stephen's Green, Dublin 2, Ireland; Department of Physiology and Medical Physics, Royal College of Surgeons In Ireland, St. Stephen's Green, Dublin 2, Ireland.
Biochim Biophys Acta. 2016 Jun;1862(6):1063-73. doi: 10.1016/j.bbadis.2016.03.006. Epub 2016 Mar 11.
In amyotrophic lateral sclerosis (ALS), it has been suggested that the process of neurodegeneration starts at the neuromuscular junction and is propagated back along axons towards motor neurons. Caspase-dependent pathways are well established as a cause of motor neuron death, and recent work in other disease models indicated a role for caspase 6 in axonal degeneration. Therefore we hypothesised that caspase 6 may be involved in motor neuron death in ALS. To investigate the role of caspase 6 in ALS we profiled protein levels of caspase-6 throughout disease progression in the ALS mouse model SOD1(G93A); this did not reveal differences in caspase 6 levels during disease. To investigate the role of caspase 6 further we generated a colony with SOD1(G93A) transgenic mice lacking caspase 6. Analysis of the transgenic SOD1(G93A); Casp6(-/-) revealed an exacerbated phenotype with motor dysfunction occurring earlier and a significantly shortened lifespan when compared to transgenic SOD1(G93A); Casp6(+/+) mice. Immunofluorescence analysis of the neuromuscular junction revealed no obvious difference between caspase 6(+/+) and caspase 6(-/-) in non-transgenic mice, while the SOD1(G93A) transgenic mice showed severe degeneration compared to non-transgenic mice in both genotypes. Our data indicate that caspase-6 does not exacerbate ALS pathogenesis, but may have a protective role.
在肌萎缩侧索硬化症(ALS)中,有人提出神经退行性变过程始于神经肌肉接头,并沿轴突逆向传播至运动神经元。半胱天冬酶依赖性途径已被确认为运动神经元死亡的一个原因,最近在其他疾病模型中的研究表明半胱天冬酶6在轴突变性中起作用。因此,我们推测半胱天冬酶6可能参与ALS中运动神经元的死亡。为了研究半胱天冬酶6在ALS中的作用,我们在ALS小鼠模型SOD1(G93A)的整个疾病进展过程中分析了半胱天冬酶-6的蛋白水平;这并未揭示疾病期间半胱天冬酶6水平的差异。为了进一步研究半胱天冬酶6的作用,我们培育了一群缺乏半胱天冬酶6的SOD1(G93A)转基因小鼠。对转基因SOD1(G93A);Casp6(-/-)的分析显示,与转基因SOD1(G93A);Casp6(+/+)小鼠相比,其表型加重,运动功能障碍出现得更早,寿命显著缩短。神经肌肉接头的免疫荧光分析显示,在非转基因小鼠中,半胱天冬酶6(+/+)和半胱天冬酶6(-/-)之间没有明显差异,而在两种基因型中,SOD1(G93A)转基因小鼠与非转基因小鼠相比均表现出严重的变性。我们的数据表明,半胱天冬酶-6不会加剧ALS的发病机制,反而可能具有保护作用。