Expression of HSP70 Heat-Shock Proteins under Oxidative Stress

The development of oxidative stress inevitably causes damage to cell proteins in need of timely refolding. The synthesis of the proteins of the heat-shock group is the most ancient and effective mechanism of cell protection. The life-long cellular adaptation to a huge number of cytotoxic factors, both of xenobiotic and natural origin, have provided heat-shock proteins with polyfunctionality: in the processes of programmed death, they act as either anti- or pro-apoptogenic factors or as regulators of the activity of these factors. The important role of heat-shock proteins in adaptation, inflammation, and immune response had also been shown. Various experimental and clinical studies confirmed the important role of heat-shock proteins in the development of pathophysiological phenomena of oxidative stress, aging, tumor formation, and immune reactions. The data presented in the review includes domestic and foreign studies on the physiological significance of heat-shock proteins, their role in the mechanisms of cell, and body stability in general and are relevant to modern medicine and biology.