Cited by 143Alzheimer's disease research and treatmentsMicrotubule and mitosis dynamicsNeuroinflammation and Neurodegeneration Mechanisms

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Selective Destruction of Stable Microtubules and Axons by Inhibitors of Protein Serine/Threonine Phosphatases in Cultured Human Neurons (NT2N Cells)

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Merrick, Sandra E., Trojanowski, John Q., Lee, Virginia M.-Y.·1997·The Journal of Neuroscience

DOI 10.1523/jneurosci.17-15-05726.1997PMC PMC6573204

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Abstract

Paired helical filaments (PHFs) in the neurofibrillary tangles (NFTs) in Alzheimer’s disease (AD) brains are composed of highly phosphorylated isoforms of tau (PHFtau) that fail to bind microtubules (MTs), and the levels of MT-binding competent tau are decreased in AD brains with abundant PHFtau. Because this loss of MT binding could compromise the viability of tangle-bearing AD neurons by destabilizing MTs, we asked whether these events could be initiated by inhibiting protein phosphatase 1 (PP1) and PP2A in cultured human neurons (NT2N cells) using okadaic acid (OK) and calyculin-A (CL-A). The treatment of NT2N cells with OK and CL-A increased tau phosphorylation, decreased the binding of tau to MTs, and selectively depolymerized the more stable detyrosinated MTs but not the more labile tyrosinated MTs. Significantly, this led to the rapid degeneration of axons, which are enriched in the more stable detyrosinated MTs, and PP2A was implicated in the initiation of this cascade of events because PP2A but not PP1 was closely associated with MTs in the NT2N cells. These studies imply that inactivation of PP2A in vulnerable neurons of the AD brain may play a mechanistic role in the conversion of normal tau into PHFtau, in the depolymerization of stable MTs, and in the degeneration of axons emanating from tangle-bearing neurons.

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Authors: Merrick, S. E., Trojanowski, J. Q., & Lee, V. M.-Y.
Affiliations: University of Pennsylvania (US)
ORCID: Trojanowski, John Q.
Lee, Virginia M.-Y.
Venue: The Journal of Neuroscience
Publisher: Society for Neuroscience
Published: 1997-08-01
Volume: 17
Issue: 15
Pages: 5726-5737
ISSN: 0270-6474 (ISSN-L)
1529-2401
DOI: 10.1523/jneurosci.17-15-05726.1997
PMC: PMC6573204
OpenAlex: W1674770932
Semantic Scholar: ac79a6d58482597051dd8a2a3f551f09044640f7
Cited by: 143
References: 62
Citations by year: 2026: 1 · 2025: 2 · 2024: 2 · 2023: 2 · 2022: 1 · 2021: 3 · 2020: 5 · 2019: 2 · 2018: 2 · 2017: 2 · 2016: 7 · 2015: 1 · 2014: 4 · 2013: 4 · 2012: 4
FWCI: 4.27
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by-nc-sa
creativecommons.org/licenses/by-nc-sa/4.0/ (vor, 184 d)
Locations: Journal of Neuroscience (publishedVersion, cc-by-nc-sa)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health
National Institute on Aging
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Keywords: Alzheimer's disease, neurofibrillary tangles, paired helical filaments, tau phosphorylation, protein phosphatase 2A, protein phosphatase 1, okadaic acid, calyculin A, microtubule depolymerization, axonal degeneration
MeSH terms: Axons, Enzyme Inhibitors, Humans, Marine Toxins, Microtubules, Neurons, Oxazoles, Serine, Threonine, Tumor Cells, Cultured, Okadaic Acid

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Selective Destruction of Stable Microtubules and Axons by Inhibitors of Protein Serine/Threonine Phosphatases in Cultured Human Neurons (NT2N Cells)

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