ABSTRACT
Inducers of the heat shock response include heat, hypoxia-reoxygenation, ethanol, sulfhydryl agents, protein synthesis inhibitors, heavy metals, tissue trauma, and certain normal conditions such as embryonic development. The heat shock proteins (HSP) are strongly conserved proteins found in all organisms and tissues. Because many types of stress induce HSP synthesis, they are sometimes called stress proteins. The role of stress proteins in protein folding and assembly may be major function of HSPs, for example, HSPs as molecular chaperones. Cross-protection between heat shock and ischemia-reperfusion has been shown in the heart. Greatest recovery from ischemia-reperfusion occurred in hearts taken from animals 48 h after heat shock. Protection against cardiac ischemia has also been shown when conditioning stress was short-term ischemia. Ischemia-induced changes of HSPs and glutathione may occur primarily in this organelle. This chapter observes several changes in HSPs during stress conditioning compared to HSPs in ischemia, including lack of HSP 70 aggregation and synthesis of HSC 70 and HSP 60.
