Heat shock protein and Alzheimer's disease: an updated systematic review

Background:Alzheimer's disease (AD) is widely acknowledged as a global medical and social concern, and is characterized by the absence of a definitive cure. One of the primary challenges in AD research is the difficulty in targeting and isolating the intricate biochemical pathways that are implicated in the disease, particularly the mechanisms underlying protein misfolding that lead to the generation of harmful substances. Given the role of misfolding processes in the etiology of AD, there is potential for therapeutic interventions that focus on molecular chaperones.Objective:This review evaluated the association between AD and molecular chaperones, focusing specifically on the prominent heat shock proteins (HSPs) that serve as key constituents of the human chaperone.Methods:Publications from several electronic databases including PubMed, Scopus, and Web of Sciences, were examined by the reviewers, and 10 articles were selected after the screening process following the PRISMA guidelines. The search was conducted using specific keywords such as HSP, AD, neurocognitive disorders, and dementia.Results:The findings of our review indicate that HSPs play a role in the process of refolding or degrading misfolded proteins. Additionally, they contribute to the reduction of abnormal protein accumulation and neuronal degeneration, the mitigation of synaptic dysfunction, and the gradual and continuous decline of cognitive function observed in individuals with AD.Conclusion:The findings of this study indicate that HSPs have a role in the process of refolding or degrading misfolded proteins.