A Simple Model to Study Tau Pathology
Tau proteins play a role in the stabilization of microtubules, but in pathological conditions, tauopathies, tau is modified by phosphorylation and can aggregate into aberrant aggregates. These aggregates could be toxic to cells, and different cell models have been used to test for compounds that mig...
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doaj-982ffcd4fafd498a8454e3b1aa46a48f2020-11-25T01:25:46ZengSAGE PublishingJournal of Experimental Neuroscience1179-06952016-01-011010.4137/JEN.S25100A Simple Model to Study Tau PathologyAlexander L. Houck0Félix Hernández1Jesús Ávila2Centro de Biologia Molecular Severo Ochoa (CSIC-UAM), Madrid, Spain. Centro de Investigación Biomédica en Red de Enfermedades Neurodegenerativas (CIBERNED), Madrid, Spain.Centro de Biologia Molecular Severo Ochoa (CSIC-UAM), Madrid, Spain. Centro de Investigación Biomédica en Red de Enfermedades Neurodegenerativas (CIBERNED), Madrid, Spain.Centro de Biologia Molecular Severo Ochoa (CSIC-UAM), Madrid, Spain. Centro de Investigación Biomédica en Red de Enfermedades Neurodegenerativas (CIBERNED), Madrid, Spain.Tau proteins play a role in the stabilization of microtubules, but in pathological conditions, tauopathies, tau is modified by phosphorylation and can aggregate into aberrant aggregates. These aggregates could be toxic to cells, and different cell models have been used to test for compounds that might prevent these tau modifications. Here, we have used a cell model involving the overexpression of human tau in human embryonic kidney 293 cells. In human embryonic kidney 293 cells expressing tau in a stable manner, we have been able to replicate the phosphorylation of intracellular tau. This intracellular tau increases its own level of phosphorylation and aggregates, likely due to the regulatory effect of some growth factors on specific tau kinases such as GSK3. In these conditions, a change in secreted tau was observed. Reversal of phosphorylation and aggregation of tau was found by the use of lithium, a GSK3 inhibitor. Thus, we propose this as a simple cell model to study tau pathology in nonneuronal cells due to their viability and ease to work with.https://doi.org/10.4137/JEN.S25100 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Alexander L. Houck Félix Hernández Jesús Ávila |
spellingShingle |
Alexander L. Houck Félix Hernández Jesús Ávila A Simple Model to Study Tau Pathology Journal of Experimental Neuroscience |
author_facet |
Alexander L. Houck Félix Hernández Jesús Ávila |
author_sort |
Alexander L. Houck |
title |
A Simple Model to Study Tau Pathology |
title_short |
A Simple Model to Study Tau Pathology |
title_full |
A Simple Model to Study Tau Pathology |
title_fullStr |
A Simple Model to Study Tau Pathology |
title_full_unstemmed |
A Simple Model to Study Tau Pathology |
title_sort |
simple model to study tau pathology |
publisher |
SAGE Publishing |
series |
Journal of Experimental Neuroscience |
issn |
1179-0695 |
publishDate |
2016-01-01 |
description |
Tau proteins play a role in the stabilization of microtubules, but in pathological conditions, tauopathies, tau is modified by phosphorylation and can aggregate into aberrant aggregates. These aggregates could be toxic to cells, and different cell models have been used to test for compounds that might prevent these tau modifications. Here, we have used a cell model involving the overexpression of human tau in human embryonic kidney 293 cells. In human embryonic kidney 293 cells expressing tau in a stable manner, we have been able to replicate the phosphorylation of intracellular tau. This intracellular tau increases its own level of phosphorylation and aggregates, likely due to the regulatory effect of some growth factors on specific tau kinases such as GSK3. In these conditions, a change in secreted tau was observed. Reversal of phosphorylation and aggregation of tau was found by the use of lithium, a GSK3 inhibitor. Thus, we propose this as a simple cell model to study tau pathology in nonneuronal cells due to their viability and ease to work with. |
url |
https://doi.org/10.4137/JEN.S25100 |
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