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271182
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funding vehicle for: Oxidative stress modifies the levels and phosphorylation state of tau protein in human fibroblasts

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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
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date: 2026-08-24T21:50:59
publisher: vivo
type: Document

Article
type: Class

Oxidative stress modifies the levels and phosphorylation state of tau protein in human fibroblasts
type: Article
doi: 10.3389/fnins.2017.00495
related by: authorship_31675
related by: authorship_31670
related by: authorship_31669
accesstype: All Open Access, Gold, Green
freetext keyword: 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
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related by: authorship_31673
abstract: 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.
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artnum: 495
estado: published
date time value: article date 5207
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volume: 11
has funding vehicle: 271182
has publication venue: Frontiers in Neuroscience
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crisid: 5207
related by: authorship_31672
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. © 2017 Ibáñez-Salazar, Bañuelos-Hernández, Rodríguez-Leyva, Chi-Ahumada, Monreal-Escalante, Jiménez-Capdeville and Rosales-Mendoza.
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Frontiers in Neuroscience
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publication venue for: Oxidative stress modifies the levels and phosphorylation state of tau protein in human fibroblasts
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