Peroxiredoxins (Prxs) constitute a novel family of antioxidant proteins, which specifically prevent enzymes from metal-catalyzed oxidation. The localization of a member of the mono-cystein subfamily of Prxs, Prx VI in human respiratory system and its antioxidant properties were investigated. By immunoblotting, the Prx VI was found to be present in human respiratory epithelium. Immunostaining with rabbit polyclonal antibody raised against the Prx VI revealed that the said protein was present in apical areas and mucus of all respiratory airways from trachea to bronchioles. Immunodepletion of the Prx VI profoundly decreased the antioxidant activity of the respiratory epithelium extract.
Study was performed using a rat model of thermal burn of upper respiratory tract (URT). The URT burn in rats was induced by intratracheal instillation of 70 °C water vapor using a micro-vapor generator. In a week after the intervention about 50 % of the ciliated epithelium was destructed. In 2 weeks after the intervention the inflammatory response enhanced and tissue edema increased. In 4 weeks after the intervention partial irregular restoration of tracheal epithelium cells was observed. Both IL-1 and IL-4 expression did not change significantly during restoration of tracheal epithelium, but IL-8 and IL-10 expression increased and was high even 1 month after the burn. Simultaneously, dramatic increase in expression of peroxyredoxine 6, which is the main antioxidant protein in trachea, was observed during regeneration of trachea epithelium. Iimmunohistochemical investigations showed that the increase in peroxyredoxine 6 in trachea during the regeneration of trachea epithelium after the burn could be related to increased peroxyredoxine expression in goblet cells. Therefore, activation of peroxyredoxine 6 synthesis by goblet cells appears to be the key step in activation of epithelium defense systems after thermal burn.
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