Superoxide dismutase (SOD), catalase, and glutathione peroxidase are necessary for preventing the intracellular accumulation of reactive oxygen species. Three forms of SOD include the cytosolic Cu/Zn2+ SOD, the extracelluar Cu/Zn[2+] SOD, and the mitochondrial manganese (Mn) superoxide dismutase (MnSOD). In the mitochondria, MnSOD catalyzes the dismutation of two superoxide radicals, producing H2O2 and oxygen. Following protein synthesis, MnSOD is post-transcriptionally modified for transport from the cytosol into the mitochondria. In rat hepatocytes, H2O2 exposure induces MnSOD expression, while in rat lung, exposure to smoke induces expression in bronchial epithelial cells. In addition, MnSOD expression is required for PC12 cell resistance to nitric oxide (NO) toxicity and for nNOS neuron resistance to NMDA-induced NO toxicity. Superoxide radical anions may induce transcriptional activation of the MnSOD gene through PKC phosphorylation and activation of a CREB-1/ATF-1-like factor. Thus, MnSOD removal of reactive oxygen species created by exposure to toxic stimuli is thought to be critical for the survival of a variety of cell types.
This antibody is routinely tested by western blot analysis. Other applications were tested at BD Biosciences Pharmingen during antibody development only or reported in the literature.