Superoxide dismutase 3 (SOD3)

Superoxide dismutase 3 (SOD3) is a copper- and zinc-containing secreted antioxidant enzyme predominantly localized in the extracellular matrix and on cell surfaces, with minor presence in plasma and extracellular fluids[3][4][5][6]. It catalyzes the rapid conversion of superoxide anions, toxic byproducts of aerobic metabolism and inflammation, into less reactive hydrogen peroxide and oxygen[2][4][9]. SOD3 thereby maintains extracellular redox balance, protects tissue structures (e.g., collagen, hyaluronan, heparan sulfate) from oxidative fragmentation, and serves as a front-line defense against environmental and metabolic oxidative stress[8]. SOD3 expression and activity are regulated by copper availability and signaling pathways (including Atox1), and its deficiency or dysfunction has been linked to various diseases such as chronic obstructive pulmonary disease (COPD), cardiovascular disease, inflammatory and autoimmune disorders, and cancer[3][8][9]. SOD3 also exhibits immunomodulatory and anti-inflammatory functions by limiting activation and differentiation of immune cells (such as dendritic cells and T cells) and suppressing pro-inflammatory cytokine release[3]. Genetic variants of SOD3 can influence disease susceptibility, particularly in pulmonary and vascular contexts[8]. Although no approved drugs directly target SOD3, it is under investigation as a therapeutic and biomarker target in diseases associated with oxidative tissue injury.

Other names

Extracellular superoxide dismutaseEC-SODSOD3 (gene/protein symbol)

Enzymatic conversion (dismutation) of superoxide anion (O_2^-) into hydrogen peroxide (H_2O_2) and molecular oxygen (O_2), reducing oxidative stress in extracellular spaces[2][6][9]. - Indirect modulation of inflammatory and immune signaling by decreasing extracellular ROS[3][5].