Publication details
Tau phosphorylation and neuroinflammatory response to Aβ in choroid plexus cells
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| Year of publication | 2024 |
| Type | Appeared in Conference without Proceedings |
| Citation | |
| Description | The pathogenesis of Alzheimer's disease is associated with the accumulation of amyloid-beta peptide and hyperphosphorylated Tau protein, leading to neuronal death. Aß has been found to interfere with pathways that regulate the phosphorylation of Tau protein, especially in neuroinflammatory response. The blood-cerebrospinal fluid barrier and the choroid plexus play a key role in removing Aß from the brain and may propagate its toxicity and Tau phosphorylation through neuroinflammatory reactions. The aim of the study was to confirm the relationship between neuroinflammation and increased Tau protein phosphorylation in a rat model cell line of the choroid plexus epithelium. The rat choroid plexus epithelium cell line Z310 was cultivated with Aß peptide for one and three day timepoints alongside non-treated control. Reverse transcription PCR was used to detect pro-inflammatory cytokines IL1ß, IL6, TNF?, and IFN?, and immunocytochemistry was used to detect p-Tau at the phosphorylation sites T231, S199 and T181. By calculating fold change values of RT-PCR, gene expression changes were observed. By the three day timepoint, a significant rise in expression was evident for most genes, particularly IL6 in the treated group. Notably, IL1ß exhibited prominent expression even after just one day of treatment, indicating its rapid response to Aß exposure. Among the three Tau phosphorylation sites studied, the T231 site exhibited statistically significant changes in response to Aß treatment upon calculating the corrected total cell fluorescence. It was found that the mRNA expression of pro-inflammatory cytokines IL1ß, IL6, TNF?, and IFN?, as well as p-Tau protein levels increased after Aß treatment of the Z310 cells, supporting the main hypothesis that neuroinflammation in the choroid plexus epithelium is connected to Tau phosphorylation. |
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