Adams, David S.
UMass Medical Center, Worcester, MA
Amyotrophic lateral sclerosis (ALS) is a fatal neurodegenerative disorder that causes motor neuron degeneration, skeletal muscle atrophy, paralysis and ultimately death. Mutations in the Cu, Zn superoxide dismutase (SOD1) gene causes a subset of this disease. Mutated human SOD1 transgenic mice develop clinical and pathological symptoms similar to those in human ALS. In these mouse models, mitochondrial dysfunction is primarily seen in central nervous system (CNS) tissues. Previous studies have shown that degenerated mitochondria may trigger the onset of ALS. In order to determine why CNS mitochondria are susceptible to this damage, mitochondrial proteins found in tissues of mice were purified with blue native polyacrylamide gel electrophoresis (BN-PAGE), and identified using Coomassie blue staining. These proteins were compared among the different tissues. To date, three proteins have been found to differ among brain, lung and liver tissues. These proteins may interact differently with toxic mutant proteins, resulting in cell-specific mitochondrial vulnerability. Determining the sequence of these proteins could help determine their function and may lead to a better understanding of the mitochondrial degeneration mechanism.
Worcester Polytechnic Institute
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Biology and Biotechnology