Redox-active proteins in apoptotic and oxidative stress pathways

Redox-active proteins in apoptotic and oxidative stress pathways constitute a diverse functional group of molecules that regulate cellular thiol-disulfide balance and manage reactive oxygen species (ROS) [1]. This category includes the thioredoxin (Trx) and glutathione (GSH) systems, peroxiredoxins (Prx), and superoxide dismutases (SOD), which are critical for maintaining redox homeostasis [2]. These proteins play a dual role in disease: in cancer, they are frequently upregulated to protect tumor cells from oxidative stress-induced apoptosis, whereas their deficiency or dysfunction is linked to neurodegenerative and cardiovascular diseases [3]. Therapeutic interventions targeting these proteins often involve small-molecule inhibitors like auranofin, which targets thioredoxin reductase to induce lethal ROS accumulation in cancer cells [4]. Additionally, redox-sensitive signaling proteins such as Apoptosis signal-regulating kinase 1 (ASK1) serve as key nodes connecting oxidative stress to the apoptotic machinery [5].

Other names

Redox-sensitive proteinsAntioxidant enzymesRedox signaling moleculesThiol-disulfide oxidoreductases

Modulation of cellular redox state through the inhibition of antioxidant enzymes (e.g., Thioredoxin reductase) to promote apoptosis in cancer, or the use of ROS scavengers and mimetics to protect cells from oxidative damage in degenerative conditions [2, 4].