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Specific post-translational modifications of soluble tau protein distinguishes Alzheimer’s disease and primary tauopathies
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Specific post-translational modifications of soluble tau protein distinguishes Alzheimer’s disease and primary tauopathies
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Journal Article
Specific post-translational modifications of soluble tau protein distinguishes Alzheimer’s disease and primary tauopathies
2023
Overview
Tau protein aggregates in several neurodegenerative disorders, referred to as tauopathies. The tau isoforms observed in
post mortem
human brain aggregates is used to classify tauopathies. However, distinguishing tauopathies
ante mortem
remains challenging, potentially due to differences between insoluble tau in aggregates and soluble tau in body fluids. Here, we demonstrated that tau isoforms differ between tauopathies in insoluble aggregates, but not in soluble brain extracts. We therefore characterized post-translational modifications of both the aggregated and the soluble tau protein obtained from
post mortem
human brain tissue of patients with Alzheimer’s disease, cortico-basal degeneration, Pick’s disease, and frontotemporal lobe degeneration. We found specific soluble signatures for each tauopathy and its specific aggregated tau isoforms: including ubiquitination on Lysine 369 for cortico-basal degeneration and acetylation on Lysine 311 for Pick’s disease. These findings provide potential targets for future development of fluid-based biomarker assays able to distinguish tauopathies in vivo.
Post-translational modifications on tau protein in the brain could distinguish primary tauopathies. Here, the authors assess insoluble and soluble tau extracted from
post
mortem
human tauopathy brains and show 4R/3R tau isoform ratio in aggregates is associated with specific modifications on soluble tau protein.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 82/1
/ 82/16
/ 82/58
/ 82/83
/ Alzheimer Disease - diagnosis
/ Alzheimer Disease - metabolism
/ Brain
/ Humanities and Social Sciences
/ Humans
/ Isoforms
/ Lysine
/ Pick Disease of the Brain - metabolism
/ Protein Isoforms - metabolism
/ Protein Processing, Post-Translational
/ Proteins
/ Science
