R. A. Stetler, Y. Gao, A. P. Signore, G. Cao and J. Chen Pages 863 - 872 ( 10 )
The 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 HSP27s 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.
HSP27, heat shock proteins, chaperones, ischemia, aggregates, injury
Department of Neurology, University of Pittsburgh, 507 South Biomedical Science Tower, 200 Lothrop Street, Pittsburgh, PA 15261, USA.