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Reactive oxygen species and neuroepithelial interactions during wound healing
Published in David M. Gardiner, Regenerative Engineering and Developmental Biology, 2017
Although low H2O2 levels are critical for specific oxidation of signaling proteins, they do not explain how only some signaling proteins are oxidized but others are not. A computational study predicted that susceptible cysteine residues must be in the vicinity of another cysteine sulfur atom, accessible to solvents, and possess a pKa less than 9.05 (Sanchez et al. 2008). Furthermore, oxidation-prone cysteine residues must be present in an active site or regulatory motif in order to change the enzymatic function of a signaling protein after reversible disulfide bond formation. Recent data show that cysteine oxidation is not a linear process, which might explain the high specificity of signaling protein activation. It was found that peroxiredoxins 1 and 2 (Prx1 and Prx2), which are known to be efficient H2O2 scavengers, participate in the oxidative modification of oxidation-sensitive cysteine residues. Peroxiredoxins have been shown to transiently form intermolecular disulfide bonds with signaling proteins, which in a second step result in intramolecular disulfide bond formation within signaling proteins (Sobotta et al. 2015).
Proteomic analysis of whole-body responses in medaka (Oryzias latipes) exposed to benzalkonium chloride
Published in Journal of Environmental Science and Health, Part A, 2020
Young Sang Kwon, Jae-Woong Jung, Yeong Jin Kim, Chang-Beom Park, Jong Cheol Shon, Jong-Hwan Kim, June-Woo Park, Sang Gon Kim, Jong-Su Seo
Our findings demonstrated that BAC induced enzymes related to the oxidative stress response in medaka. Various stress response proteins, including superoxide dismutase (spot 4), peroxiredoxin 6 (spots 5 and 8), and glutathione S-transferase (spots 6 and 12), were increased in response to BAC exposure. The formation of ROS and oxidative stress is closely involved in the toxicity response of aquatic organisms to various toxins. Prior studies demonstrated that ROS generated in vivo by marine medaka exposed to the environmental pollutants benzo [a] pyrene (BaP) and endosulfan are involved in the immune response in this context.[38,39] Zhang et al. (2017) demonstrated that ROS levels are increased in zebrafish exposed to oxide (GO) carbon nanomaterials.[40] Superoxide dismutase is an antioxidant enzyme that plays an important role in the oxidative stress response by scavenging ROS such as superoxide anions and hydroxyl radicals to alleviate oxidative stress.[41,42] Peroxiredoxin is a peroxidase family protein that plays an important role in signaling pathways by regulating H2O2 concentration and removal of ROS, and in minimizing the deleterious effects of external biotic and abiotic stimuli.[43–45] Glutathione S-transferase is a phase II detoxification enzyme that forms a conjugate with glutathione in the context of cellular damage, and plays an important role in defense against oxidative stress.[46]