HSP27: Mechanisms of Cellular Protection Against Neuronal Injury

Author(s): R. A. Stetler, Y. Gao, A. P. Signore, G. Cao, J. Chen

Journal Name: Current Molecular Medicine

Volume 9 , Issue 7 , 2009

Become EABM
Become Reviewer
Call for Editor


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.

Keywords: HSP27, heat shock proteins, chaperones, ischemia, aggregates, injury

Rights & PermissionsPrintExport Cite as

Article Details

Year: 2009
Page: [863 - 872]
Pages: 10
DOI: 10.2174/156652409789105561
Price: $65

Article Metrics

PDF: 10