Host: The Japanese Society of Toxicology
Amyotrophic lateral sclerosis (ALS) is a motor neuron disease with muscle atrophy and respiratory failure. Superoxide dismutase-1 (SOD1) is deposited as aggregates in motor neurons and glial cells of ALS. While natively folded SOD1 binds Cu/Zn that confer structural stability to the protein, SOD1 aggregates do not contain these metals. Thus, dissociation of Cu/Zn ions from SOD1 is required for its aggregation. Metallothionein-I (MT-I) is a Cu/Zn binding protein involved in the homeostasis of these ions. We hypothesize that MT-I has the potential to inhibit pathological conversion of SOD1 into aggregation. In this symposium, we will talk about that MT-I inhibits SOD1 aggregation at molecular and cellular levels.
