Heat Shock Protein 90 in Alzheimer’s Disease
Alzheimer’s disease (AD) is the first most common neurodegenerative disease. Despite a large amount of research, the pathogenetic mechanism of AD has not yet been clarified. The two hallmarks of the pathology of AD are the extracellular senile plaques (SPs) of aggregated amyloid-beta (Aβ) peptide an...
Main Authors: | , , , , |
---|---|
Format: | Article |
Language: | English |
Published: |
Hindawi Limited
2014-01-01
|
Series: | BioMed Research International |
Online Access: | http://dx.doi.org/10.1155/2014/796869 |
id |
doaj-a6b072b0b1744cdebe4691c29b1aade9 |
---|---|
record_format |
Article |
spelling |
doaj-a6b072b0b1744cdebe4691c29b1aade92020-11-24T22:21:09ZengHindawi LimitedBioMed Research International2314-61332314-61412014-01-01201410.1155/2014/796869796869Heat Shock Protein 90 in Alzheimer’s DiseaseJiang-Rong Ou0Meng-Shan Tan1An-Mu Xie2Jin-Tai Yu3Lan Tan4 Department of Neurology, Qingdao Municipal Hospital, School of Medicine, Qingdao University, No. 5 Donghai Middle Road, Qingdao 266071, ChinaDepartment of Neurology, Qingdao Municipal Hospital, College of Medicine and Pharmaceutics, Ocean University of China, Qingdao 266003, ChinaDepartment of Neurology, the Affiliated Hospital of Qingdao University, Qingdao 266000, China Department of Neurology, Qingdao Municipal Hospital, School of Medicine, Qingdao University, No. 5 Donghai Middle Road, Qingdao 266071, China Department of Neurology, Qingdao Municipal Hospital, School of Medicine, Qingdao University, No. 5 Donghai Middle Road, Qingdao 266071, ChinaAlzheimer’s disease (AD) is the first most common neurodegenerative disease. Despite a large amount of research, the pathogenetic mechanism of AD has not yet been clarified. The two hallmarks of the pathology of AD are the extracellular senile plaques (SPs) of aggregated amyloid-beta (Aβ) peptide and the accumulation of the intracellular microtubule-associated protein tau into fibrillar aggregates. Heat shock proteins (HSPs) play a key role in preventing protein misfolding and aggregation, and Hsp90 can be viewed as a ubiquitous molecular chaperone potentially involved in AD pathogenesis. A role of Hsp90 regulates the activity of the transcription factor heat shock factor-1 (HSF-1), the master regulator of the heat shock response. In AD, Hsp90 inhibitors may redirect neuronal aggregate formation, and protect against protein toxicity by activation of HSF-1 and the subsequent induction of heat shock proteins, such as Hsp70. Therefore, we review here to further discuss the recent advances and challenges in targeting Hsp90 for AD therapy.http://dx.doi.org/10.1155/2014/796869 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Jiang-Rong Ou Meng-Shan Tan An-Mu Xie Jin-Tai Yu Lan Tan |
spellingShingle |
Jiang-Rong Ou Meng-Shan Tan An-Mu Xie Jin-Tai Yu Lan Tan Heat Shock Protein 90 in Alzheimer’s Disease BioMed Research International |
author_facet |
Jiang-Rong Ou Meng-Shan Tan An-Mu Xie Jin-Tai Yu Lan Tan |
author_sort |
Jiang-Rong Ou |
title |
Heat Shock Protein 90 in Alzheimer’s Disease |
title_short |
Heat Shock Protein 90 in Alzheimer’s Disease |
title_full |
Heat Shock Protein 90 in Alzheimer’s Disease |
title_fullStr |
Heat Shock Protein 90 in Alzheimer’s Disease |
title_full_unstemmed |
Heat Shock Protein 90 in Alzheimer’s Disease |
title_sort |
heat shock protein 90 in alzheimer’s disease |
publisher |
Hindawi Limited |
series |
BioMed Research International |
issn |
2314-6133 2314-6141 |
publishDate |
2014-01-01 |
description |
Alzheimer’s disease (AD) is the first most common neurodegenerative disease. Despite a large amount of research, the pathogenetic mechanism of AD has not yet been clarified. The two hallmarks of the pathology of AD are the extracellular senile plaques (SPs) of aggregated amyloid-beta (Aβ) peptide and the accumulation of the intracellular microtubule-associated protein tau into fibrillar aggregates. Heat shock proteins (HSPs) play a key role in preventing protein misfolding and aggregation, and Hsp90 can be viewed as a ubiquitous molecular chaperone potentially involved in AD pathogenesis. A role of Hsp90 regulates the activity of the transcription factor heat shock factor-1 (HSF-1), the master regulator of the heat shock response. In AD, Hsp90 inhibitors may redirect neuronal aggregate formation, and protect against protein toxicity by activation of HSF-1 and the subsequent induction of heat shock proteins, such as Hsp70. Therefore, we review here to further discuss the recent advances and challenges in targeting Hsp90 for AD therapy. |
url |
http://dx.doi.org/10.1155/2014/796869 |
work_keys_str_mv |
AT jiangrongou heatshockprotein90inalzheimersdisease AT mengshantan heatshockprotein90inalzheimersdisease AT anmuxie heatshockprotein90inalzheimersdisease AT jintaiyu heatshockprotein90inalzheimersdisease AT lantan heatshockprotein90inalzheimersdisease |
_version_ |
1725771965240705024 |