Reactive oxygen species-generating and reactive oxygen species-modulated proteins (ROS-generating/modulated proteins)

Reactive oxygen species (ROS)-generating and ROS-modulated proteins constitute a broad functional class of molecules that govern cellular redox homeostasis. ROS-generating proteins, such as the NADPH oxidase (NOX) family, xanthine oxidase, and mitochondrial respiratory chain complexes, produce superoxide and hydrogen peroxide as primary products or metabolic byproducts (Sies & Jones, 2020). ROS-modulated proteins include redox-sensitive transcription factors like Nrf2 and NF-κB, as well as enzymes like protein tyrosine phosphatases, which contain cysteine residues susceptible to reversible oxidative modification (Holmström & Finkel, 2014). While ROS serve as vital secondary messengers in signal transduction and host defense, their excessive production or impaired scavenging leads to oxidative stress (Lambeth, 2004). This oxidative imbalance is a hallmark of various pathologies, including cancer, neurodegeneration, and cardiovascular diseases. Pharmacological intervention targeting these proteins involves either the inhibition of ROS-producing enzymes or the activation of antioxidant response pathways to mitigate tissue damage. For example, drugs like allopurinol inhibit xanthine oxidase, while bardoxolone methyl targets the Nrf2 pathway to enhance antioxidant defenses. However, therapeutic development is challenged by the need to maintain physiological ROS levels required for normal cellular functions, as complete suppression can impair innate immunity and mitogenic signaling (He et al., 2020).

Other names

Redox-sensitive proteinsROS-related proteinsOxidative stress-associated proteinsRedoxome

Inhibition of ROS-producing enzymes, scavenging of reactive species, or modulation of redox-sensitive signaling pathways to restore cellular redox balance.