SOD1 & SOD2

Superoxide Dismutase Enzymes are present in practically all cells and in extracellular fluids. The SODs are considered free radical scavengers, preventing oxidative damage and thus are considered important to delay the aging process. Genetic polymorphism in SOD enzymes and their altered expressions and activities are associated with oxidative DNA damage and an increased cancer risk. (Khan MA, Tania M, Zhang D, Chen H. Antioxidant enzymes and cancer. Chin J Cancer Res 22(2);87-92. 2010)

SOD enzymes contain metal cofactors which can be copper, zinc, manganese or iron. Deficiency in any of these metals will lower certain SOD levels and function.

SOD-Gene defects have been associated with diseases such as Amyotrophic lateral sclerosis (ALS) (Banzi et al. SOD1 and amyotrophic lateral sclerosis: mutation and oligomerization. PLoS 3/-/2008. NCBI; Furukawa Y et al. Complete loss of post-translational modifications triggers fibrillar aggregation of SOD1 in familial form of ALS. J. Biol. Chem. 283/35/2008)

Superoxide Dismutase 1 (SOD1) or CuSOD

SOD1 is also called the copper/zinc superoxide dismutase or CuZnSOD. It is present in the cytosol, the nucleus and the mitochondria. Its primary function is to act as an antioxidant enzyme, lowering the steady-state concentration of superoxide. High concentrations are found in liver, brain and testes, but also in red blood cells, pancreas and the lung. Inactivity of an SOD enzyme disturbs the cell metabolism.

A copper or zinc deficiency reduces the function and activity of the SOD1 enzyme.

Superoxide Dismutase 2 (SOD2) or MnSOD

This gene is a member of the iron/manganese superoxide dismutase family. Mutations in this gene have been associated with idiopathic cardiomyopathy, premature aging, (IDC), sporadic motor neuron disease, and cancer. (NCBI Report. SOD2 superoxide dismutase 2. upd. May 2011)