Expanding role of molecular chaperones in regulating α-synuclein misfolding; implications in Parkinson’s disease
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- 作者：Sandeep K. Sharma ; Smriti Priya
- 关键词：Parkinson’s disease ; α ; Synuclein ; Molecular chaperones ; Hsp70 ; Hsp100 ; Hsp110 ; Small Hsps ; Protein homeostasis
- 刊名：Cellular and Molecular Life Sciences
- 出版年：2017
- 出版时间：February 2017
- 年：2017
- 卷：74
- 期：4
- 页码：617-629
- 全文大小：
- 刊物类别：Biomedical and Life Sciences
- 刊物主题：Cell Biology; Biomedicine, general; Life Sciences, general; Biochemistry, general;
- 出版者：Springer International Publishing
- ISSN：1420-9071
- 卷排序：74
文摘
Protein misfolding under stressful environmental conditions cause several cellular problems owing to the disturbed cellular protein homeostasis, which may further lead to neurological disorders like Parkinson’s disease (PD), Alzheimer’s disease (AD), Amyloid lateral sclerosis and Huntington disease (HD). The presence of cellular defense mechanisms like molecular chaperones and proteasomal degradation systems prevent protein misfolding and aggregation. Molecular chaperones plays primary role in preventing protein misfolding by mediating proper native folding, unfolding and refolding of the polypeptides along with vast number of cellular functions. In past few years, the understanding of molecular chaperone mechanisms has been expanded enormously although implementation to prevent protein aggregation diseases is still deficient. We in this review evaluated major classes of molecular chaperones and their mechanisms relevant for preventing protein aggregation, specific case of α-synuclein aggregation. We also evaluate the molecular chaperone function as a novel therapeutic approach and the chaperone inhibitors or activators as small molecular drug targets.