HEAT SHOCK PROTEINS A DEFENSIVE SYSTEM FOR CORRECTING IRREGULAR BIOLOGICAL SYSTEMIC EX-PRESSION

Abstract

HSP regulate the response to any detrimental factors, including temperature, radiation, hypoxia, toxins or infectious agents, by controlling the three-dimensional structure of the newly synthesized proteins, preventing their misfolding or degradation. Stress response may evoke the release of HSP outside the cell, as an effect of an active transport or cell disintegration due to the infection, damage, or necrosis. Heat shock proteins or HSP are a class of proteins with related functions. Their expression increases when cells are exposed to elevated temperatures or other stress. Heat shock proteins help protect other proteins from heat stress. Chaperones regulate changes in the protein arrangement through membranes during transport. They regulate conformation - arrangement of proteins at the slight damage. Later studies demonstrated the presence of molecular chaperones in the folding of new synthesized proteins they participate in their transport across membranes, as well as their integration into various organelles. The experimental tools for examining Hsps and the standards for such examinations have both advanced considerably. As a result, much either of the earlier work on evolutionary and ecological physiology of Hsps regrettably does not withstand current scrutiny or contributes little to issues of current interest. Many of the apparently singular Hsps of previous years, often detected by one-dimensional electrophoresis and autoradiography, are now known to represent entire families of Hsps.