Current Molecular Medicine

David W. Li  
College of Medicine
University of Nebraska Medical Center
Omaha, NE


HSP27: Mechanisms of Cellular Protection Against Neuronal Injury

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

Affiliation: Department of Neurology, University of Pittsburgh, 507 South Biomedical Science Tower, 200 Lothrop Street, Pittsburgh, PA 15261, USA.

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


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.

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Article Details

Page: [863 - 872]
Pages: 10
DOI: 10.2174/156652409789105561