ABSTRACT
The possibility of using modified peroxyredoxins as powerful antioxidant agents has been considered. Peroxyredoxins immobilized on perfluorocarbon emulsions and PTD-modified peroxyredoxins have been studied. It has been shown that peroxyredoxins efficiently bind to particles of perfluorocarbon emulsions, while maintaining their antioxidant properties. A panel of PTD-modified peroxyredoxins has been created and peroxyredoxins most effective both in antioxidant properties and the ability to penetrate cells have been selected. The modified peroxyredoxins obtained may serve as the basis for the design of drug with powerful antioxidant action.
Subject(s)
Drug Delivery Systems/methods , Oxidative Stress/drug effects , Peroxiredoxins , Animals , Antioxidants/therapeutic use , Cell Line , Cell-Penetrating Peptides/chemistry , Emulsions/administration & dosage , Fluorocarbons/administration & dosage , Free Radicals/adverse effects , Humans , Mice , Oxygen/metabolism , Peroxiredoxins/administration & dosage , Peroxiredoxins/chemistry , Recombinant Fusion ProteinsABSTRACT
The effect of negatively charged ions on respiratory organs and blood of rats has been studied. It was shown that the inhaling of negative air ions (NAI) for 60 min with a concentration of NAI at the place of location of animals 320-350 000 ions/cm2 activated the secretion of goblet cells without damaging the mucosa of the trachea and changed the spectrum of proteins of bronchopulmonary lavage. It was also found that the spontaneous production of reactive oxygen species (ROS) by cells of nonfractionated blood after the exposure to NAI increased in both males and females; the intensity of ROS generation induced by opsonized zymosan increased only in females. Different sensitivity of the antioxidant enzymes superoxide dismutase and glutathione reductase of blood to NAI in females and males was revealed. These results enable one to consider the effect of NAI as priming and a weak activation of the respiratory organs through the direct action on the mucosa of the primary target organs of the respiratory tract and then on the blood.
Subject(s)
Air , Glutathione Reductase/blood , Ions/pharmacology , Respiratory Mucosa/metabolism , Superoxide Dismutase/blood , Trachea/metabolism , Animals , Bronchoalveolar Lavage Fluid , Female , Male , Rats , Rats, Wistar , Reactive Oxygen Species/metabolism , Respiratory Mucosa/cytology , Time Factors , Trachea/cytology , Zymosan/pharmacologyABSTRACT
cDNA of human peroxiredoxin VI, one of the recently discovered novel antioxidant proteins, was expressed in Escherichia coli cells. The expression product was obtained in water-soluble form and purified by a two-step chromatographic procedure using DEAE-Sepharose and Sephacryl S-200. According to CD data, the polypeptide chain of the recombinant human peroxiredoxin VI contains approximately 40% alpha-helical region and 30% beta-structure, which is the same as for native rat peroxiredoxin VI. The protective properties of the recombinant protein determined as its ability to prevent the inactivation of glutamine synthetase from E. coli in a model oxidation system were comparable with the protective properties of native rat peroxiredoxin VI.
