HSP27: Mechanisms of Cellular Protection Against Neuronal Injury

Title: HSP27: Mechanisms of Cellular Protection Against Neuronal Injury

Volume: 9 Issue: 7

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

Affiliation:

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

Abstract: 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.

Cite this article as:

Stetler A. R., Gao Y., Signore P. A., Cao G. and Chen J., HSP27: Mechanisms of Cellular Protection Against Neuronal Injury, Current Molecular Medicine 2009; 9 (7) . https://dx.doi.org/10.2174/156652409789105561