Inducible heat shock protein 70 (HSP70) is a stress protein whose expression is upregulated when the cell or organism is placed under conditions of stress. HSP70 is essential for cellular recovery, survival, and maintenance of normal cellular function. It is also a molecular chaperone that prevents protein aggregation and refolds damaged proteins in response to cellular stress caused by environmental insults, pathogens, and disease. Current research is aimed at exploiting HSP70’s cellular protective abilities as a therapeutic strategy against damaging cellular stress.

In most mammals, the expression of inducible HSP70 is strictly stress inducible and can only be detected following a significant stress upon the cell or organism. However, in humans and primates, inducible HSP70 is present at basal levels and is upregulated in response to stress. The role of HSP70 has been studied in a variety of medically relevant models or conditions such as hyperthermia, hypertension, toxic exposure to chemical agents, hypoxia, ischemia, inflammation, autoimmunity, apoptosis, cancer, organ transplantation, and bacterial and viral infections. HSP70 has also been studied in the normal processes of aging, spermatogenesis, menstruation, and physical activity such as exercise.

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