engleski

Analysis of tau protein spread in rat brain as a model of Alzheimer's disease

Alzheimer's disease (AD) is a neurodegenerative disease and the most common primary cause of dementia syndrome. Many theories exist regarding possible mechanisms of development and progression of AD, one of which is the tau hypothesis. This theory suggests that the hyperphosphorylated tau proteins misfold, oligomerize and aggregate, disrupting microtubule structure and function ultimately leading to the death of synapses and neurons. In this work we investigated changes and spreading of tau fibrils and tau oligomers that were inoculated into the medial entorhinal cortex of nine Wistar rats. The phosphorylated tau proteins were visualised by using the AT8 antibody, which binds to Ser202/Thr205 epitope of tau. Three coronal levels (-8.04, -6.84, and -5.64 mm from bregma) were analysed at 4, 8, and 11- month post-inoculation. The main finding was that the animals inoculated with the tau fibrils displayed significantly greater amount of neurofibrillary changes and spread of tau fibrils, while such changes did not occur in animals inoculated with tau oligomers and phosphate buffer saline (controls). These findings suggest that tau fibrils may be the true culprit in AD and thus deserve further validation and a more detailed analysis in future studies.

Alzheimer's disease ; entorhinal cortex ; hippocampus ; propagation of neurofibrillary changes ; rat model ; tau fibrils ; tau oligomers

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