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Cellular redox systems and the maintenance of ROS balance refer to the integrated network of enzymes and small molecules that regulate the production and elimination of reactive oxygen species (ROS). Key enzymatic components include superoxide dismutase (SOD), catalase, and glutathione peroxidase (GPx), while the glutathione (GSH) and thioredoxin (Trx) systems provide the necessary reducing power to maintain cellular homeostasis (StatPearls, 2023). At physiological levels, ROS act as essential signaling molecules in pathways governing cell growth, differentiation, and the immune response; however, an imbalance—termed oxidative stress—can lead to the damage of DNA, proteins, and lipids (Nature Reviews Molecular Cell Biology, 2017). This dysregulation is central to the pathogenesis of numerous conditions, including cancer, neurodegenerative diseases like Alzheimer's, and cardiovascular disorders. Therapeutic strategies targeting these systems involve either upregulating antioxidant defenses (e.g., via Nrf2 activators like dimethyl fumarate) to prevent tissue damage or inhibiting antioxidant pathways (e.g., via TrxR inhibitors like auranofin) to selectively kill cancer cells that are already under high oxidative stress (Nature Reviews Drug Discovery, 2013). The primary challenge in targeting these systems lies in the dual role of ROS, where excessive suppression can disrupt vital signaling, while insufficient control fails to prevent disease progression.
Modulation of reactive oxygen species (ROS) levels through the activation of antioxidant transcription factors (e.g., Nrf2), supplementation of antioxidant precursors (e.g., NAC), or the inhibition of ROS-scavenging enzymes (e.g., TrxR, GPx) to either protect cells from oxidative damage or induce apoptosis in cancer cells (Nature Reviews Drug Discovery, 2013; Frontiers in Pharmacology, 2021).
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