Construction of a Fusion Enzyme Exhibiting Superoxide Dismutase and Peroxidase Activity.

A chimeric gene construct encoding human peroxiredoxin 6 and Mn-superoxide dismutase from Escherichia coli was developed. Conditions for expression of the fusion protein in E. coli cell were optimized.

[Xenopus laevis peroxiredoxins: Gene expression during development and characterization of the enzymes].

Reactive oxygen species (ROS) are produced via catabolic and anabolic processes during normal embryonic development, and ROS content in the cell is maintained at a certain level. Peroxiredoxins are a family of selenium-independent peroxidases and play a key role in maintaining redox homeostasis of the cell. In addition to regulating the ROS level, peroxiredoxins are involved in intracellular and intercellular signaling, cell differentiation, and tissue development.

Cardioprotective Effect of Modified Peroxiredoxins in Retrograde Perfusion of Isolated Rat Heart under Conditions of Oxidative Stress.

Antioxidant properties of recombinant peroxiredoxin-6 and chimeric protein PSH combining peroxidase and superoxide dismutase activities were studied on the model of retrograde perfusion of isolated rat heart under conditions of H2O2-induced oxidative stress. The exogenous antioxidant proteins exhibited cardioprotective properties manifested in heart rate normalization, maintenance of contractile activity of the myocardium, and prevention of H2O2-induced LPO in oxidative stress. Localization of peroxiredoxin-6 and PSH in the cardiac tissue was determined and myocardial structures most effectively protected by the antioxidant enzymes from ischemia/reperfusion-induced damages were identified.

[Peroxyredoxins as multifunctional enzymes].

Peroxiredoxins are evolutionarily ancient, but relatively recently discovered group of seleniumindependent peroxidases. Peroxiredoxins protect cells from various peroxides and play an important role in maintaining the oxidation-reduction homeostasis. Moreover, they are involved in many cellular processes that are not related to peroxidase activity.

[Two peroxiredoxins 6 of Xenopus laevis].

Two different genes of peroxiredoxin 6 are encoded in the genome of Xenopus laevis: xen1 (Acc.no. EMBL Data Bank - BCO54278) and xen2 (Acc.