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Stress Proteins as Molecular Chaperones: Implications for Toxicology.

B. Sanders

Published 1994 in Environmental Health Perspectives

ABSTRACT

Although organisms encounter both natural and anthropogenic stress, until quite recently our knowledge of how they adapt to stress at the molecular and cellular levels has been limited. It is now becoming apparent that just as cells have evolved mechanisms to repair DNA, they have evolved an epigenetic repair and recycling system to maintain protein integrity. Protein denaturation and misfolding caused by weakening of polar bonds and exposure of hydrophobic groups are important targets of stressor-induced damage. A Stressed out. Cellular functions of stress proteins unde conditions (top) and conditions of environmental stress (I system that repairs this damage could provide valuable insights into the molecular mechanisms of toxicity, identification of target organs, and evaluation of physiological state. The epigenetic repair system is called the cellular stress response or the heat-shock response. It is involved in protecting organisms from damage as a result of exposure to a wide variety of environmental stressors including elevated temperatures, ultraviolet light, trace metals, and xenobi-otics. A major feature of the response is the rapid synthesis of "stress pro-teins" upon exposure to environ-I mental stress. Stress proteins are i highly conserved in evolution and play similar roles in organisms from bacteria to humans. Cell lines selected for survival at high temperatures constitutively synthesize the stress protein hsp7O at high levels, whereas temperature-sensitive mutants do not. A number of stress protein families, including stress9O, stress7O, chaperonin6O, hsp4O, the low molecular weight stress proteins, and ubiquitin, have been identified in diverse phyla.

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