Reactive oxygen species and protein disulfides (ROS/Protein disulfides)

Reactive oxygen species (ROS) and protein disulfides are central components of cellular redox biology, acting as both signaling molecules and mediators of oxidative damage. ROS, such as superoxide and hydrogen peroxide, are produced during mitochondrial respiration and by enzymes like NADPH oxidases; they regulate various pathways including cell proliferation and immune responses (PMID: 21233337). Protein disulfides are formed through the oxidation of cysteine residues, a process often facilitated by ROS or enzymes like protein disulfide-isomerase (PDI), and are essential for proper protein folding and structural stability (PMID: 15103334). However, an imbalance between ROS production and antioxidant defenses leads to oxidative stress, resulting in aberrant protein disulfide formation and cellular dysfunction associated with cancer, neurodegeneration, and cardiovascular disease (PMID: 25236395, PMID: 16430502). Therapeutic interventions include ROS scavengers like N-acetylcysteine and edaravone, as well as inhibitors of redox-active enzymes, aimed at restoring homeostasis or selectively inducing oxidative stress in tumor cells (DrugBank DB01151, PMID: 28249518).

Other names

Oxidative stress mediatorsRedox signaling moleculesProtein thiol-disulfide exchange systemReactive oxygen speciesProtein disulfides

Direct scavenging of reactive oxygen species, inhibition of ROS-producing enzymes (e.g., NADPH oxidase), or modulation of enzymes involved in thiol-disulfide exchange such as protein disulfide-isomerase (PDI) and thioredoxin (PMID: 28249518, DrugBank DB01151).