Chapter category: Heat Shock Proteins
Physiological Role of Heat Shock Protein 27
Heat Shock Proteins in Myocardial Protection
Edited by: Rakesh C. KukrejaISBN: 1-58706-021-3
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Chapter authors:
Dipak K. Das and Nilanjana Maulik
Heat shock protein 27 (Hsp27) is a stress–inducible cytosolic protein that is ubiquitously present in many normal cells. The synthesis of Hsp27 is induced by heat shock and other environmental and pathophysiologic stresses such as UV radiation, hypoxia and ischemia.1–4 Hsp27 is a member of small heat–shock protein family.5 Besides its putative role in thermoresistance,6 these proteins may be involved in the survival and recovery of the cells when exposed to stressful conditions.7 A recent study demonstrated that Hsp27 may play a role in drug resistance.8 However, the biological role of Hsp27 remains unknown. It is speculated that under stressful conditions, Hsp27 may act as energy–independent traps preventing irreversible protein aggregation. Following adaptation to stress, these proteins are refolded in cooperation with other chaperones.9
Several recent reports indicate that Hsp27 may be involved in signal transduction processes. For example, Hsp27 has been shown to play a role in tumor necrosis factor a (TNFa)–triggered signal transduction during oncoprotein–mediated neoplasticity.10–12 Expression of Hsp27 or ab–crystallin increased the intracellular level of gluthathione thereby enhancing the survival of cells following TNFa–treatment. Stress–mediated phosphorylation of specific serine residues in Hsp27 is believed to be involved in the coupling mechanism that regulates its biological function.13 For example, Hsp27 was shown to be a physiological target for MAP (mitogen activated protein) kinase–activated protein (MAPKAP) kinase–2.14,15
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Heat Shock Proteins in Myocardial Protection, edited by Rakesh C. Kukreja
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