Superoxide dismutases: Dual roles in controlling ROS damage and regulating ROS signaling
By Ying Wang, Robyn Branicky, Alycia Noë, S. Hekimi. Journal of Cell Biology, 2018
1,862 citations recorded by the source corpus.
Superoxide dismutases (SODs) are universal enzymes of organisms that live in the presence of oxygen. They catalyze the conversion of superoxide into oxygen and hydrogen peroxide. Superoxide anions are the intended product of dedicated signaling enzymes as well as the byproduct of several metabolic processes including mitochondrial respiration. Through their activity, SOD enzymes control the levels of a variety of reactive oxygen species (ROS) and reactive nitrogen species, thus both limiting the potential toxicity of these molecules and controlling broad aspects of cellular life that are regulated by their signaling functions. All aerobic organisms have multiple SOD proteins targeted to different cellular and subcellular locations, reflecting the slow diffusion and multiple sources of their substrate superoxide. This compartmentalization also points to the need for fine local control of ROS signaling and to the possibility for ROS to signal between compartments. In this review, we discuss studies in model organisms and humans, which reveal the dual roles of SOD enzymes in controlling damage and regulating signaling.
Subfields: Molecular Biology
View Paper: https://www.semanticscholar.org/paper/c7133623a6747b39d7168082b52efc79c75f1ef5
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Citations in the corpus
- Oxidative Stress in Human Pathology and Aging: Molecular Mechanisms and Perspectives (2022, background): “In biological systems and in medicine, H2O2 is used as anti-infective agent, such as for the cleaning of wounds, due to its strong oxidative potential to kill microorganisms and cells [38,48].”
- The Chemistry of Reactive Oxygen Species (ROS) Revisited: Outlining Their Role in Biological Macromolecules (DNA, Lipids and Proteins) and Induced Pathologies (2021, background): “Some mutations that increase ROS production ultimately induce oxidative damage to the mitochondrial matrix, inhibiting proteins such as Sirtuin3 (antioxidant and anti-tumour protein) [31] and reducing other redundant antioxidant defences, such as SOD2 [32].”
- Glutathione metabolism in cancer progression and treatment resistance (2018, background): “Enzymatic antioxidant responses include increased abundance of superoxide dismutase or catalase (Sies, 1993; Ighodaro and Akinloye, 2017; Wang et al., 2018).”
- Reactive Oxygen Species-Induced Lipid Peroxidation in Apoptosis, Autophagy, and Ferroptosis (2019, background): “SOD can catalyze the conversion of superoxide into oxygen and hydrogen peroxide [12].”