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Erratum: Lai, R.Y.K.; Harrington, C.R.; Wischik, C.M. Absence of a Role for Phosphorylation in the Tau Pathology of Alzheimer’s Disease. Biomolecules 2016, 6, 19
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Biomolecules 2016, 6(3), 36; doi:10.3390/biom6030036

Internalization of the Extracellular Full-Length Tau Inside Neuro2A and Cortical Cells Is Enhanced by Phosphorylation

1
Department of Neuroscience, Research Institute for Biosciences, University of Mons, Mons 7000, Belgium
2
Department of Proteomics and Microbiology, Research Institute for Biosciences, University of Mons, Mons 7000, Belgium
*
Author to whom correspondence should be addressed.
Academic Editors: Claude M. Wischik and Charles Harrington
Received: 9 March 2016 / Revised: 4 July 2016 / Accepted: 20 July 2016 / Published: 19 August 2016
(This article belongs to the Special Issue Tau Protein and Alzheimer’s disease)
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Abstract

Tau protein is mainly intracellular. However, several studies have demonstrated that full-length Tau can be released into the interstitial fluid of the brain. The physiological or pathological function of this extracellular Tau remains unknown. Moreover, as evidence suggests, extracellular Tau aggregates can be internalized by neurons, seeding Tau aggregation. However, much less is known about small species of Tau. In this study, we hypothesized that the status of phosphorylation could alter the internalization of recombinant Tau in Neuro2A and cortical cells. Our preliminary results revealed that the highly phosphorylated form of Tau entered the cells ten times more easily than a low phosphorylated one. This suggests that hyperphosphorylated Tau protein could spread between neurons in pathological conditions such as Alzheimer’s disease. View Full-Text
Keywords: Tau; phosphorylation; internalization; spreading Tau; phosphorylation; internalization; spreading
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Wauters, M.; Wattiez, R.; Ris, L. Internalization of the Extracellular Full-Length Tau Inside Neuro2A and Cortical Cells Is Enhanced by Phosphorylation. Biomolecules 2016, 6, 36.

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