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Description
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.Catalytic activity: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).Subcellular location: Cytoplasm. Involvement in disease: Defects in SOD1 are the cause of amyotrophic lateral sclerosis type 1 (ALS1). ALS1 is a familial form of amyotrophic lateral sclerosis, a neurodegenerative disorder affecting upper and lower motor neurons and resulting in fatal paralysis. Sensory abnormalities are absent. Death usually occurs within 2 to 5 years. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of cases leading to familial forms. The protein (both wild-type and ALS1 variants) has a tendency to form fibrillar aggregates in the absence of the intramolecular disulfide bond or of bound zinc ions. These aggregates may have cytotoxic effects. Zinc binding promotes dimerization and stabilizes the native form. Also known as: SOD1, Superoxide dismutase 1, SODC.
Immunogen
A synthetic peptide from the internal region of human SOD1 (Superoxide dismutase 1, SODC) conjugated to an immunogenic carrier protein was used as the antigen. The antigen is homologous in rat and mouse.