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The Studies of Heat Shock Proteins in Alzheimer Disease
Zhen-Qiu Tan1,2, Feng Li1,3, Run-Zhong Liu1,3, Shui-Gen Hong1, Jian-Zhi Wang2*, Hua-Xi Xu1,2,3*
1The laboratory of Molecular Cellular Neuroscience, School of Life Science, Xiamen University, Xiamen 361005, China; 2Department of Pathophysiology, Tongji Medical College of Huazhong University of Science and Technology, Wuhan 43003
Abstract: Heat shock proteins (HSPs)， or so-called stress proteins， comprise of several highly conserved families of related proteins. They not only participate in the synthesis， folding， translocation and transport of proteins， but also modulate proteolytic machinery and prevent misfolding and aggregation of proteins in neurodegenerative diseases， e.g. alpha-synuclein and parkin in Parkinson''s disease and huntingtin in Huntinton''s disease. Alzheimer''s disease (AD) is a neurodegenerative disease characterized by two major pathological lesions: neurofibrillary tangles which comprise largely of insoluble hyperphosphorylated tau， and senile or amyloid plaques which mainly composed of β-amyloid peptides (Aβ).The accumulating evidence begins to demonstrate a key role for HSPs in the accumulation/solubility of tau， and inhibition of Aβ-induced neurotoxicity. Although the detailed mechanisms underlying the functions of HSPs in AD pathogenesis remain elusive， the protective roles of HSPs in both normal physiological and pathological processes suggest that HSPs maybe a therapeutic target of AD treatment. Thus， this article intends to review recent findings on HSPs'' roles in AD pathogenesis.
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