UMMS Affiliation

Department of Biochemistry and Molecular Pharmacology

Publication Date


Document Type



Amino Acid Substitution; Animals; Biological Markers; Disease Models, Animal; Electron Transport Complex IV; Fluorescent Antibody Technique; Humans; Immunohistochemistry; Mice; Mice, Transgenic; Microscopy, Immunoelectron; Mitochondria; Motor Neuron Disease; Motor Neurons; Mutation; Protein Subunits; Spinal Cord; Superoxide Dismutase


Life Sciences | Medicine and Health Sciences


Mutations in Cu, Zn superoxide dismutase (SOD1) cause a fraction of amyotrophic lateral sclerosis (ALS), which involves motoneuron degeneration, paralysis, and death. An acquired activity by mutant SOD1 is responsible for the cellular toxicity, but how mutant SOD1 kills motoneurons is unclear. In transgenic mouse models of ALS, mitochondrial degeneration occurs early, before disease onset, raising the question of how mutant SOD1 damages mitochondria. Here we investigate the intracellular localization of SOD1 in the CNS to determine whether SOD1 is present in mitochondria, where it could directly damage this organelle. We show that endogenous mouse SOD1, wild-type human, and mutant human SOD1 (G93A), when expressed as transgenes, are colocalized with mitochondria in spinal cord by immunofluorescence confocal microscopy. By immunoelectron microscopy, we show that SOD1 is present within mitochondria at similar concentrations as in the cytoplasm. Thus SOD1, in addition to being a cytosolic enzyme, is present inside mitochondria in the CNS.


J Neurosci. 2002 Mar 15;22(6):RC215.

Journal/Book/Conference Title

The Journal of neuroscience : the official journal of the Society for Neuroscience

Related Resources

Link to Article in PubMed

PubMed ID




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