Heat Shock Protein 90 in Alzheimer’s Disease
Autor: | Lan Tan, Jin-Tai Yu, Jiang-Rong Ou, Anmu Xie, Meng-Shan Tan |
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Jazyk: | angličtina |
Rok vydání: | 2014 |
Předmět: |
General Immunology and Microbiology
biology Tau protein lcsh:R lcsh:Medicine Review Article General Medicine medicine.disease Hsp90 General Biochemistry Genetics and Molecular Biology Hsp70 Cell biology Biochemistry Alzheimer Disease Heat shock protein medicine biology.protein Humans HSP90 Heat-Shock Proteins Molecular Targeted Therapy Senile plaques Heat shock Alzheimer's disease Transcription factor |
Zdroj: | BioMed Research International, Vol 2014 (2014) BioMed Research International |
ISSN: | 2314-6141 2314-6133 |
Popis: | 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. |
Databáze: | OpenAIRE |
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