Misfolded SOD1 associated with motor neuron mitochondria alters mitochondrial shape and distribution prior to clinical onset

• Published in: PloS one Vol. 6; no. 7; p. e22031
• Main Authors: Vande Velde, Christine, McDonald, Karli K, Boukhedimi, Yasmin, McAlonis-Downes, Melissa, Lobsiger, Christian S, Bel Hadj, Samar, Zandona, Andre, Julien, Jean-Pierre, Shah, Sameer B, Cleveland, Don W
• Format: Journal Article
• Language: English
• Published: United States Public Library of Science 11.07.2011; Public Library of Science (PLoS)
• Subjects: Aberration; Amyotrophic lateral sclerosis; Animals; Axon guidance; Axons; Biology; Cancer; Clustering; Cytochrome; Development and progression; Elongation; Fluorescence; Fluorescent Antibody Technique; Genetic aspects; Green fluorescent protein; Homeostasis; Immunoblotting; Medical research; Medicine; Mice; Mice, Transgenic; Mitochondria; Mitochondria - metabolism; Morphology; Motor neurons; Motor Neurons - metabolism; Multiple sclerosis; Mutation; Neurons; Neurosciences; Pathogenesis; Permeability; Physical characteristics; Protein Folding; Recruitment; Rodents; Spinal cord; Superoxide dismutase; Superoxide Dismutase - chemistry; Superoxide Dismutase - genetics; Superoxide Dismutase - metabolism; Superoxide Dismutase-1; Superoxides; La Jolla California; United States > US; California

Mutations in superoxide dismutase (SOD1) are causative for inherited amyotrophic lateral sclerosis. A proportion of SOD1 mutant protein is misfolded onto the cytoplasmic face of mitochondria in one or more spinal cord cell types. By construction of mice in which mitochondrially targeted enhanced gre...