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RDF description of Oxidative stress modifies the levels and phosphorylation state of tau protein in human fibroblasts - http://orbis.uaslp.mx/vivo/individual/scopus5206
Article
Alzheimer's disease; Fibroblasts; Oxidative stress; Phosphorylation state; Tau protein tau protein; Alzheimer disease; animal experiment; Article; cell nucleus; cell stress; cellular distribution; controlled study; cytosol; female; fibroblast; genetic transfection; human; human cell; human cell culture; human tissue; molecular pathology; mouse; nonhuman; oxidative stress; protein expression; protein localization; protein phosphorylation; tau gene
Oxidative stress modifies the levels and phosphorylation state of tau protein in human fibroblasts
Since the tau protein is closely involved in the physiopathology of Alzheimer%27s 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. © 2017 Ibáñez-Salazar, Bañuelos-Hernández, Rodríguez-Leyva, Chi-Ahumada, Monreal-Escalante, Jiménez-Capdeville and Rosales-Mendoza.
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. © 2017 Ibáñez-Salazar, Bañuelos-Hernández, Rodríguez-Leyva, Chi-Ahumada, Monreal-Escalante, Jiménez-Capdeville and Rosales-Mendoza.
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