Antioxidant Enzymes and Redox-Sensitive Proteins

Antioxidant Enzymes and Redox-Sensitive Proteins constitute a complex network of molecules dedicated to maintaining cellular redox homeostasis and protecting against oxidative damage (Sies et al., 2017, PMID: 28265168). This group includes primary enzymes such as superoxide dismutase (SOD), which dismutates superoxide radicals, and catalase and glutathione peroxidase (GPx), which neutralize hydrogen peroxide (Halliwell & Gutteridge, 2015). Central to the regulation of these enzymes is the Nrf2-Keap1 signaling pathway, a master redox-sensitive switch that induces the expression of numerous cytoprotective genes in response to oxidative or electrophilic stress (He et al., 2017, PMID: 28711252). Dysregulation of this antioxidant network is a hallmark of various pathologies, including neurodegenerative diseases like Parkinson's, chronic inflammatory conditions, cardiovascular diseases, and cancer. Therapeutic strategies involve the use of Nrf2 activators, such as dimethyl fumarate and omaveloxolone, to enhance endogenous defenses or enzyme mimetics like ebselen to provide exogenous catalytic activity (Liby & Sporn, 2012, PMID: 22473713). However, pharmacological modulation must be carefully balanced, as excessive antioxidant activity can lead to "reductive stress" or inadvertently support the survival of cancer cells by shielding them from ROS-induced apoptosis (Gorrini et al., 2013, PMID: 23470312). Overall, this target class represents a critical frontier in treating oxidative stress-related diseases, provided that specificity and timing of intervention are optimized.

Other names

Antioxidant systemRedox-regulated proteinsOxidative stress enzymesThiol-redox proteinsAntioxidant defense system

Induction of the Nrf2-mediated antioxidant response element (ARE) pathway; direct catalytic neutralization of reactive oxygen species; replenishment of intracellular thiol pools; covalent modification of Keap1 cysteine residues (PMID: 28711252, PMID: 22473713).