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lüll HSP27: mechanisms of cellular protection against neuronal injury Stetler RA; Gao Y; Signore AP; Cao G; Chen JCurr Mol Med 2009[Sep]; 9 (7): 863-72The heat shock protein (HSP) family has long been associated with a generalized cellular stress response, particularly in terms of recognizing and chaperoning misfolded proteins. While HSPs in general appear to be protective, HSP27 has recently emerged as a particularly potent neuroprotectant in a number of diverse neurological disorders, ranging from ALS to stroke. Although its robust protective effect on a number of insults has been recognized, the mechanisms and regulation of HSP27's protective actions are still undergoing intense investigation. On the basis of recent studies, HSP27 appears to have a dynamic and diverse range of function in cellular survival. This review provides a forum to compare and contrast recent literature exploring the protective mechanism and regulation of HSP27, focusing on neurological disorders in particular, as they represent a range from protein aggregate-associated diseases to acute stress.|Cell Death/physiology[MESH]|Gene Expression Regulation[MESH]|HSP27 Heat-Shock Proteins/genetics/*metabolism[MESH]|Heat-Shock Response/physiology[MESH]|Humans[MESH]|Nervous System Diseases/metabolism/pathology/physiopathology[MESH]|Neurons/metabolism/*pathology[MESH]|Neuroprotective Agents/*metabolism[MESH]|Protein Folding[MESH]|Protein Processing, Post-Translational[MESH]|Signal Transduction/physiology[MESH] |