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Motor neuron degeneration in mice that express a human Cu/Zn superoxide dismutase mutation. Science 264: 1772–5 (1994)
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BibTeX
@MISC{Gurney94motorneuron,
author = {Mark E. Gurney and Haifeng Pu and Arlene Y. Chiu and Mauro C. Dal Canto and Cynthia Y. Polchow and Denise D. Alex and Jan Caliendo and Afif Hentati and Young W. Kwon and Han-xiang Deng and Wenje Chen and Ping Zhai and Robert L. Sufit and Teepu Siddique and M. E. Gurney and H. Pu and D. D. Alex and Y. W. Kwon and A. Y. Chiu},
title = {Motor neuron degeneration in mice that express a human Cu/Zn superoxide dismutase mutation. Science 264: 1772–5},
year = {1994}
}
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Abstract
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. Amyotrophic lateral sclerosis occurs in both sporadic and familial forms and results from the degeneration of motor neurons in the cortex, brainstem, and spinal cord. The disease typically begins in adults as an asymmetric weakness in two or more limbs and then progresses to complete paralysis (1). Familial ALS is inherited as an auto-
Keyphrases
spinal cord familial al motor neuron little effect high level human cu zn superoxide dismutase transgenic mouse amyotrophic lateral sclerosis familial form familial amyotrophic lateral sclerosis asymmetric weakness human sod gain-of-function mutation enzyme activity-caused motor neuron disease sod contribute motor neuron loss
