The suppressor of cytokine signaling (SOCS) family members are negative regulators of cytokine signal transduction that inhibit the Jak/Stat pathway. The SOCS family consists of at least 8 members including the originally identified cytokine-inducible SH2-containing protein (CIS1), as well as SOCS1-7. Each SOCS family member contains a central SH2 domain and a conserved carboxy-terminal motif designated as the SOCS box. These proteins are important regulators of cytokine signaling, proliferation, differentiation, and immune responses. Low levels of SOCS3 are observed in lung, spleen, and thymus and, like other SOCS family members, its expression is rapidly induced by a number of factors including interleukins, EPO, IFN-γ, CSF, and TNF-α. SOCS3 uses its SH2 domain to bind activated Jaks and their cognate receptors to provide negative feedback inhibition. In addition to the initially described inducers of SOCS3 expression, subsequent studies have described SOCS3-mediated negative feedback inhibition for leptin, GH, chemokine receptors, insulin, and certain pathogens. SOCS3 deletion results in embryonic lethality with placental insufficiency. SOCS3 signaling has been linked pathologically to allergic responses, inflammatory disease, endotoxic shock, wound repair, and obesity.
Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
The protein encoded by this gene binds copper and zinc ions and is one of two isozymes responsible for destroying free superoxide radicals inThe body.The encoded isozyme is a soluble cytoplasmic protein, acting as a homodimer to convert naturally-occuring but harmful superoxide radicals to molecular oxygen and hydrogen peroxide.The other isozyme is a mitochondrial protein. Mutations in this gene have been implicated as causes of familial amyotrophic lateral sclerosis. Rare transcript variants have been reported for this gene.
The protein encoded by this gene binds copper and zinc ions and is one of two isozymes responsible for destroying free superoxide radicals in the body. The encoded isozyme is a soluble cytoplasmic protein, acting as a homodimer to convert naturally-occuring but harmful superoxide radicals to molecular oxygen and hydrogen peroxide. The other isozyme is a mitochondrial protein. Mutations in this gene have been implicated as causes of familial amyotrophic lateral sclerosis. Rare transcript variants have been reported for this gene.
Manganese superoxide dismutase (MnSOD), also named as SOD2, is a mitochondrial detoxification enzyme that catalyzes the conversion of superoxide to hydrogen peroxide. Hydrogen peroxide is then decomposed to water by catalase, glutathione peroxidase, or peroxiredoxins. MnSOD and other enzymes involved in antioxidant defense protect cells from reactive oxygen species (ROS). Calorie restriction leads to SIRT3-mediated deacetylation of MnSOD and the subsequent increase of its antioxidant activity. MnSOD also plays an essential role in mediating the protective effect of mTOR inhibition to reduce epithelial stem cell senescence.
Superoxide Dismutases (SODs), originally identified as Indophenoloxidases (IPOs), are enzymes that catalyze the conversion of naturally-occuring but harmful superoxide radicals into molecular oxygen and hydrogen peroxide. Superoxide Dismutases 2 (SOD2), also known as Manganese (Mn) SOD, mitochondrial SOD, and IPO-B, is an intramitochondrial 22 kDa homotetramer. Each SOD2 monomer binds one Mn2+ ion. Three isozymes of SOD have been identified and are functionally related but have very modest sequence homology. SOD2 shares only 23% and 17% sequence identity with SOD1 and SOD3, respectively. SOD2 is, however, well conserved from species to species and shares 90% and 87% homology with mouse and rat SOD2, respectively. Oxidative stress has been implicated in many diseases and the chief source of reactive oxygen species within the cell is the mitochondrion. SOD2 is a free radical scavenging enzyme that protects against damage from superoxide produced as a byproduct of oxidative phosphorylation. SOD2 is required for normal biologic function of tissues by maintaining the integrity of mitochondrial enzymes susceptible to inactivation by superoxide. Mutations in this gene have been associated with idiopathic cardiomyopathy (IDC), premature aging, sporadic motor neuron disease, and cancer.
This gene is a member of the iron/manganese superoxide dismutase family. It encodes a mitochondrial protein that forms a homotetramer and binds one manganese ion per subunit. This protein binds to the superoxide byproducts of oxidative phosphorylation and converts them to hydrogen peroxide and diatomic oxygen. Mutations in this gene have been associated with idiopathic cardiomyopathy (IDC), premature aging, sporadic motor neuron disease, and cancer. Alternative splicing of this gene results in multiple transcript variants. A related pseudogene has been identified on chromosome 1.
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