Journal
SEMINARS IN CELL & DEVELOPMENTAL BIOLOGY
Volume 40, Issue -, Pages 142-152Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.semcdb.2015.03.003
Keywords
Molecular chaperone; Neuroprotection; Neurodegeneration; Protein aggregation; Heat shock response; Unfolded protein response
Categories
Funding
- Wellcome Trust [092621]
- MRC [G0700412]
- RP Fighting Blindness [GR580]
- Fight for Sight [1511/1512]
- China Scholarship Council (CSC) PhD student
- MRC [G0700412] Funding Source: UKRI
- Medical Research Council [G0700412] Funding Source: researchfish
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Protein homeostasis (proteostasis) is essential for maintaining the functionality of the proteome. The disruption of proteostasis, due to genetic mutations or an age- related decline, leads to aberrantly folded proteins that typically lose their function. The accumulation of misfolded and aggregated protein is also cytotoxic and has been implicated in the pathogenesis of neurodegenerative diseases. Neurons have developed an intrinsic protein quality control network, of which molecular chaperones are an essential component. Molecular chaperones function to promote efficient folding and target misfolded proteins for refolding or degradation. Increasing molecular chaperone expression can suppress protein aggregation and toxicity in numerous models of neurodegenerative disease; therefore, molecular chaperones are considered exciting therapeutic targets. Furthermore, mutations in several chaperones cause inherited neurodegenerative diseases. In this review, we focus on the importance of molecular chaperones in neurodegenerative diseases, and discuss the advances in understanding their protective mechanisms. (C) 2015 Elsevier Ltd. All rights reserved.
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