肌萎缩侧索硬化
运动神经元
超氧化物歧化酶
SOD1
脊髓
发病机制
突变
转基因小鼠
神经元
转基因
生物
酶
化学
内分泌学
内科学
医学
基因
生物化学
神经科学
疾病
免疫学
作者
Mark E. Gurney,Haifeng Pu,Arlene Y. Chiu,Mauro C. Dal Canto,Cynthia Y. Polchow,Denise D. Alexander,Janice Caliendo,Afif Hentati,Young W. Kwon,Han Xiang Deng,Wenje Chen,Ping Zhai,Robert Sufit,Teepu Siddique
出处
期刊:Science
[American Association for the Advancement of Science (AAAS)]
日期:1994-06-17
卷期号:264 (5166): 1772-1775
被引量:3772
标识
DOI:10.1126/science.8209258
摘要
Mutations of human Cu,Zn superoxide dismutase (SOD) are found in about 20 percent of patients with familial amyotrophic lateral sclerosis (ALS). Expression of high levels of human SOD containing a substitution of glycine to alanine at position 93--a change that has little effect on enzyme activity--caused motor neuron disease in transgenic mice. The mice became paralyzed in one or more limbs as a result of motor neuron loss from the spinal cord and died by 5 to 6 months of age. The results show that dominant, gain-of-function mutations in SOD contribute to the pathogenesis of familial ALS.
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