Abstract
The heat shock response is a highly conserved stress response which can be activated by a variety of thermal and nonthermal stimuli such as ischaemia, heavy metals, sodium arsenite, ethanol, oxidants, and infection [1–5]. Stress-induced heat shock protein (HSP) accumulation is thought to be cytoprotective. Initial studies focused on thermo-tolerance, the ability to survive an otherwise lethal heat stress; later studies demonstrated tolerance to a variety of stresses, including ischaemia [6], ultraviolet irradiation [7], and cytokines such as tumor necrosis factor-α (TNF-α). The fact that overexpression of various HSPs confers tolerance in the absence of conditioning stress [8] and that inhibition of HSP accumulation through blocking antibodies [9] impairs stress tolerance strongly supports the hypothesis that HSPs themselves confer the stress tolerance. The HSPs are grouped into four classes or families according to their molecular weights. Each class is composed for a number of proteins, and the designation of the class refers to the “round number” approximating the molecular weights of its typical members (i.e., 20, 30, 70, 90 and 100 kDa). Depending on the stimulus and the cell type, different HSPs are expressed [10]. For example, the heme oxygenase is a low-molecular-weight HSP (HSP30) consisting of two isoforms [11]: HO-2 is expressed constitutively, and HO-1 is highly inducible by heme, heavy metals, sodium arsenite, and oxidants [12]. Recent data indicate that heme oxygenase may play an important cytoprotective role against oxidant stress [13]. The HSP70 family, consisting of constitutive (cHSP70) and inducible (iHSP70) isoforms, has been well characterized with regard to ubiquity, regulation, and cytoprotective properties.
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Zhang, H., Kim, Y.K., Slutsky, A.S. (1999). Role of Heat Shock Proteins in Cytoprotection. In: Gullo, A. (eds) Anaesthesia, Pain, Intensive Care and Emergency Medicine — A.P.I.C.E.. Springer, Milano. https://doi.org/10.1007/978-88-470-2145-7_56
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DOI: https://doi.org/10.1007/978-88-470-2145-7_56
Publisher Name: Springer, Milano
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