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Oxidative stress regulatory proteins are a broad class of molecules, including enzymes and transcription factors, that maintain cellular redox balance by managing reactive oxygen species (ROS) (Ighodaro & Akinloye, 2018, PMID: 29473213). Key members include superoxide dismutase (SOD), catalase, glutathione peroxidase, and the master transcriptional regulator Nuclear factor erythroid 2-related factor 2 (Nrf2) (He et al., 2020, PMID: 32165834). These proteins protect cells from oxidative damage to DNA, proteins, and lipids, which is a primary driver of aging and chronic diseases such as Parkinson's, Alzheimer's, and atherosclerosis (Sies et al., 2017, PMID: 28851513). In drug development, these proteins are targeted either to enhance antioxidant defenses, such as with Nrf2 activators like Dimethyl fumarate for multiple sclerosis, or to inhibit them in cancer to increase oxidative stress-induced apoptosis (Sayin et al., 2014, PMID: 24478344). However, the complexity of redox signaling poses challenges, as excessive antioxidant activity can sometimes interfere with normal physiological processes or promote the survival of malignant cells (Le Gal et al., 2015, PMID: 26446958).
Activation of the Nrf2-ARE signaling pathway to induce phase II antioxidant enzymes, direct scavenging of reactive oxygen species, and enzymatic neutralization of superoxide and hydrogen peroxide (He et al., 2020, PMID: 32165834; Ighodaro & Akinloye, 2018, PMID: 29473213).
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