The Small Heat Shock Protein HspB8: Role in Nervous System Physiology and Pathology

Author(s): Mattia Vicario, Stephen D. Skaper, Alessandro Negro

Journal Name: CNS & Neurological Disorders - Drug Targets
Formerly Current Drug Targets - CNS & Neurological Disorders

Volume 13 , Issue 5 , 2014

Become EABM
Become Reviewer
Call for Editor


The accumulation and aggregation of misfolded proteins can be highly cytotoxic and may underlie several human degenerative diseases characterized by neuronal inclusions such as Alzheimer's, Parkinson's, prion-like and polyglutamine repeat diseases. In this context small heat shock proteins, molecular chaperones known to be induced by cell stress, play a fundamental role by facilitating folding of nascent polypeptides, preventing aggregation of misfolded proteins and enhancing their degradation. A recently identified member of the small heat shock protein family, HspB8, is of particular interest in the field of neurological diseases since mutations in its sequence correlate with development of distal hereditary motor neuropathy and Charcot-Marie-Tooth disease. HspB8 expression has been detected in neurodegenerative disorders such as Alzheimer's disease, Parkinson's disease, Huntington disease and spinocerebellar ataxia type 3. In the latter, HspB8 appears to be involved in protecting the cell from accumulation of insoluble aggregates either by preventing aggregation or by promoting degradation of improperly folded proteins. These data propose that HspB8 may be a major player in the neuroprotective response and a promising target for the development of therapeutic strategies.

Keywords: Protein misfolding, neurodegenerative diseases, neuropathies, small heat shock proteins, neuroprotection.

Rights & PermissionsPrintExport Cite as

Article Details

Year: 2014
Published on: 17 July, 2014
Page: [885 - 895]
Pages: 11
DOI: 10.2174/1871527313666140711093344
Price: $65

Article Metrics

PDF: 47