Preprint Article Version 1 Preserved in Portico This version is not peer-reviewed

Heat Stress Modulates the GSK-3β Levels and Tau Phosphorylation

Version 1 : Received: 25 July 2020 / Approved: 26 July 2020 / Online: 26 July 2020 (17:04:50 CEST)

How to cite: Dubey, T.; Chinnathambi, S. Heat Stress Modulates the GSK-3β Levels and Tau Phosphorylation. Preprints 2020, 2020070645 (doi: 10.20944/preprints202007.0645.v1). Dubey, T.; Chinnathambi, S. Heat Stress Modulates the GSK-3β Levels and Tau Phosphorylation. Preprints 2020, 2020070645 (doi: 10.20944/preprints202007.0645.v1).

Abstract

Alzheimer’s disease is a prominent neurological disorder, which leads to progressive dementia. The microtubule-associated protein Tau is been considered as one of the major causes of Alzheimer’s disease. Physiologically Tau assists in the stabilization of microtubules, contrary to this the pathological state of Tau results in the formation of neurotoxic tangles of Tau. The posttranslational modifications, such as GSK-3β-mediated Tau phosphorylation results in the generation of Tau pathology. Neuroinflammation generated in Alzheimer’s disease, contributes to elevated body temperature. The aim of present work is to study the effect of high temperature on Tau phosphorylation. The neuroblastoma cells were exposed to heat stress for 40 minutes. The immunofluorescence and western blot studies suggested that high temperature increases the levels of GSK-3β in cells. Heat stressed cells was also observed to have elevated levels of phosphorylated Tau. Additionally, heat stressed cells found to have modulated nuclear transport as the level of Ran was reduced. The results of present work suggested that increased temperature could be considered as a risk factor in Alzheimer’s disease as it elevated the GSK-3β levels in cells thus, resulting in increased Tau phosphorylation.

Subject Areas

Alzheimer’s disease; Tau phosphorylation; Heat stress; GSK-3β

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