HSP27: mechanisms of cellular protection against neuronal 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 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.
Department of Neurology, University of Pittsburgh, 507 South Biomedical Science Tower, 200 Lothrop Street, Pittsburgh, PA 15261, USA.
R A
RA
Stetler
Y
Y
Gao
A P
AP
Signore
G
G
Cao
J
J
Chen
D016923:Cell Death / Q000502:physiology; D005786:Gene Expression Regulation; D055551:HSP27 Heat-Shock Proteins / Q000235:genetics / Q000378:metabolism*; D018869:Heat-Shock Response / Q000502:physiology; D006801:Humans; D009422:Nervous System Diseases / Q000378:metabolism / Q000473:pathology / Q000503:physiopathology; D009474:Neurons / Q000378:metabolism / Q000473:pathology*; D018696:Neuroprotective Agents / Q000378:metabolism*; D017510:Protein Folding; D011499:Protein Processing, Post-Translational; D015398:Signal Transduction / Q000502:physiology
D055551:HSP27 Heat-Shock Proteins; D018696:Neuroprotective Agents