Journal
CURRENT MOLECULAR MEDICINE
Volume 9, Issue 7, Pages 863-872Publisher
BENTHAM SCIENCE PUBL LTD
DOI: 10.2174/156652409789105561
Keywords
HSP27; heat shock proteins; chaperones; ischemia; aggregates; injury
Categories
Funding
- NIH/NINDS [NS43802, NS45048, NS44178, NS56118, NS36736]
- American Heart Association [0725503U]
- Chinese Natural Science Foundation [30670642, 30870794]
- NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE [R01NS043802, R01NS044178, R01NS045048, R01NS036736, R01NS056118] Funding Source: NIH RePORTER
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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 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.
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