Characterizing Heat Shock Protein Expression Patterns in a Fruit Fly Model of Glial Tauopathy



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Tauopathies are degenerative diseases characterized by the accumulation of aberrantly phosphorylated tau in both neuronal and glial cells. The aggregation and fibrilization of tau in both neuronal and glial cells is a pathological hallmark of at least 15 different neurodegenerative tauopathies. The presence of tau aggregates in these diseases implies that this protein can somehow escape normal intracellular quality control machinery, aberrantly accumulate, and become toxic. Therefore, it is vital to investigate the role of the protein quality control systems in the pathogenesis of tauopathies. By doing so, we can develop an understanding about the cooperation between molecular chaperones and the ubiquitin proteasome system responding to the tau aggregates in order to find molecular targets for therapeutic intervention. In this project, a Drosophila melanogaster model of glial tauopathy is used to study how the overexpression of tau can impact intracellular defense systems. More specifically, we are investigating the effect human tau expression has on the induction of chaperones upon exposure to thermal stress over a period of six hours. Western blot analysis was used to determine the time course of tau expression. To measure the messenger RNA (mRNA) levels of various molecular chaperones, we utilized Quantitative Real-Time PCR. Our results indicate that that the induction of human tau expression is a possible stressor on the cell, leading to a spike in the expression of specific chaperones. Additionally, tau expression over time impairs the ability of the cell to participate in cellular defense mechanisms. Finally, the impact tau expression has on cellular defense is chaperone specific which may have important implications for designing therapeutic strategies for tauopathies.