Superoxide dismutase 3 (SOD3) (SOD3)

Superoxide dismutase 3 (SOD3), also known as extracellular superoxide dismutase, is a secreted antioxidant enzyme that plays a critical role in maintaining redox homeostasis within the extracellular matrix and vascular space. It specifically catalyzes the conversion of superoxide radicals into hydrogen peroxide and molecular oxygen, serving as a primary defense against oxidative stress-induced damage to lipids, proteins, and DNA. Beyond its catalytic activity, SOD3 binds to extracellular matrix components like collagen and heparin, positioning it to protect nitric oxide from superoxide-mediated inactivation, which is vital for maintaining endothelial function and vascular tone. In various diseases, including cardiovascular disorders, chronic obstructive pulmonary disease (COPD), and certain cancers, SOD3 expression is often significantly downregulated, leading to pathological oxidative stress. Therapeutic strategies utilizing mRNA-directed protein expression aim to restore SOD3 levels by delivering synthetic mRNA to cells, which then produce and secrete the functional enzyme to mitigate tissue damage and inflammation.

Other names

Extracellular superoxide dismutaseEC-SODecSODSuperoxide dismutase [Cu-Zn] 3

mRNA-directed protein expression involves the delivery of synthetic mRNA encoding the SOD3 protein into target cells, which then translate and secrete functional SOD3 into the extracellular space. Once secreted, SOD3 catalyzes the dismutation of superoxide radicals into oxygen and hydrogen peroxide, thereby reducing oxidative stress and preventing the inactivation of nitric oxide.