Abstract
Peroxiredoxins (Prxs) are ubiquitous thiol peroxidases that are involved in the reduction of peroxides. It has been reported that prokaryotic Prxs generally show greater structural robustness than their eukaryotic counterparts, making them less prone to inactivation by overoxidation. This difference has inspired the search for new antioxidants from prokaryotic sources that can be used as possible therapeutic biodrugs. Bacterioferritin comigratory proteins (Bcps) of the hyperthermophilic archaeon Sulfolobus solfataricus that belong to the Prx family have recently been characterized. One of these proteins, Bcp1, was chosen to determine its antioxidant effects in H9c2 rat cardiomyoblast cells. Bcp1 activity was measured in vitro under physiological temperature and pH conditions that are typical of mammalian cells; the yeast thioredoxin reductase (yTrxR)/thioredoxin (yTrx) reducing system was used to evaluate enzyme activity. A TAT-Bcp1 fusion protein was constructed to allow its internalization and verify the effect of Bcp1 on H9c2 rat cardiomyoblasts subjected to oxidative stress. The results reveal that TAT-Bcp1 is not cytotoxic and inhibits H2O2-induced apoptosis in H9c2 cells by reducing the H2O2 content inside these cells.
Highlights
Reactive oxygen species (ROS), the hydroxyl radical (HO∙), and notably, superoxide (O2∙− hydrogen peroxide (H2O2), ), are potent oxidants that are generated during aerobic metabolism and in response to external factors
This analysis suggests that prokaryotic Bcp1 could be a robust peroxiredoxin that functions in all eukaryotic environments
Our results showed that Bcp1 was able to remove 100% of H2O2 at 37∘C and that the optimal peroxidase activity was achieved at pH 7.0 (Figure 2(a))
Summary
Reactive oxygen species (ROS), the hydroxyl radical (HO∙), and notably, superoxide (O2∙− hydrogen peroxide (H2O2), ), are potent oxidants that are generated during aerobic metabolism and in response to external factors. Reactive oxygen species (ROS), the hydroxyl radical (HO∙), and notably, superoxide ROS can damage all major classes of biological macromolecules, leading to protein oxidation, lipid peroxidation, DNA base modifications, and strand breaks. H2O2 plays a key role in cellular metabolism because it functions as a signalling molecule that regulates cell growth, cell adhesion, cell differentiation, and apoptosis. For these reasons, the ROS concentrations must be strictly controlled. Superoxide dismutase (SOD) is involved in the dismutation reaction of O2∙− in H2O2 that in turn is converted to H2O by an array of enzymes, such as catalase, glutathione peroxidase (GPx), and peroxiredoxin (Prx).
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