Article
Copper-binding-site-null SOD1 causes ALS in transgenic mice: aggregates of non-native SOD1 delineate a common feature.
Human molecular genetics - 1 Nov 2003
Wang Jiou, Slunt Hilda, Gonzales Victoria, Fromholt David, Coonfield Michael, Copeland Neal G, Jenkins Nancy A, Borchelt David R
Abstract excerpt
Cu/Zn superoxide dismutase (SOD1), a crucial cellular antioxidant, can in certain settings mediate toxic chemistry through its Cu cofactor. Whether this latter property explains why mutations in SOD1 cause FALS has been debated. Here, we demonstrate motor neuron disease in transgenic mice expressing a SOD1 variant that mutates the four histidine residues that coordinately bind Cu. In-depth analyses of this new...
Topics
- Amyotrophic Lateral Sclerosis
- Animals
- Axons
- Binding Sites
- Cells, Cultured
- Copper
- Histidine
- Humans
- Intermediate Filament Proteins
- Intracellular Signaling Peptides and Proteins
- Mice
- Mice, Transgenic
- Motor Neurons