Alejandro Ibáñez-Salazar, Bernardo Bañuelos-Hernández, Ildefonso Rodríguez-Leyva, Erika Chi-Ahumada, Elizabeth Monreal-Escalante, María E. Jiménez-Capdeville, Sergio Rosales-Mendoza
Abstract
Since the tau protein is closely involved in the physiopathology of Alzheimer's disease (AD), studying its behavior in cellular models might lead to new insights on understanding this devastating disease at molecular levels. In the present study, primary cultures of human fibroblasts were established and used to determine the expression and localization of the tau protein in distinct phosphorylation states in both untransfected and tau gene-transfected cells subjected to oxidative stress. Higher immunopositivity to phospho-tau was observed in cell nuclei in response to oxidative stress, while the levels of total tau in the cytosol remained unchanged. These findings were observed in both untransfected cells and those transfected with the tau gene. The present work represents a useful model for studying the physiopathology of AD at the cellular level in terms of tau protein implications.
This research output has an Altmetric Attention Score of 2. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 23 September 2017.
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#15,173,117
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#6,404
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Outputs of similar age from Frontiers in Neuroscience
#101
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