Cited by 119Alzheimer's disease research and treatmentsAdvanced Glycation End Products researchDementia and Cognitive Impairment Research

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Effect of Pseudophosphorylation and Cross-linking by Lipid Peroxidation and Advanced Glycation End Product Precursors on Tau Aggregation and Filament Formation

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Kuhla, Björn, Haase, Cathleen, Flach, Katharina, Lüth, Hans-Joachim, Arendt, Thomas, Münch, Gerald·2007·Journal of Biological Chemistry

DOI 10.1074/jbc.m609521200

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Abstract

Accumulation of hyperphosphorylated Tau protein as paired helical filaments in pyramidal neurons is a major hallmark of Alzheimer disease. Besides hyperphosphorylation, other modifications of the Tau protein, such as cross-linking, are likely to contribute to the characteristic features of paired helical filaments, including their insolubility and resistance against proteolytic degradation. In this study, we have investigated whether the four reactive carbonyl compounds acrolein, malondialdehyde, glyoxal, and methylglyoxal accelerate the formation of Tau oligomers, thioflavin T-positive aggregates, and fibrils using wild-type and seven pseudophosphorylated mutant Tau proteins. Acrolein and methylglyoxal were the most reactive compounds followed by glyoxal and malondialdehyde in terms of formation of Tau dimers and higher molecular weight oligomers. Furthermore, acrolein and methylglyoxal induced the formation of thioflavin T-fluorescent aggregates in a triple pseudophosphorylation-mimicking mutant to a slightly higher degree than wild-type Tau. Analysis of the Tau aggregates by electron microscopy study showed that formation of fibrils using wild-type Tau and several Tau mutants could be observed with acrolein and methylglyoxal but not with glyoxal and malondialdehyde. Our results suggest that reactive carbonyl compounds, particularly methylglyoxal and acrolein, could accelerate tangle formation in vivo and that this process could be slightly accelerated, at least in the case of methylglyoxal and acrolein, by hyperphosphorylation. Interference with the formation or the reaction of these reactive carbonyl compounds could be a promising way of inhibiting tangle formation and neuronal dysfunction in Alzheimer disease and other tauopathies.

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Authors: Kuhla, B., Haase, C., Flach, K., Lüth, H.-J., Arendt, T., & Münch, G.
Affiliations: Research Institute for Farm Animal Biology (FBN) (DE)
James Cook University (AU)
Corresponding author: Kuhla, Björn
ORCID: Kuhla, Björn
Arendt, Thomas
Münch, Gerald
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 2007-03
Volume: 282
Issue: 10
Pages: 6984-6991
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.m609521200
OpenAlex: W2141232168
Cited by: 119
References: 61
Citations by year: 2026: 3 · 2025: 5 · 2024: 4 · 2023: 1 · 2022: 4 · 2021: 4 · 2020: 7 · 2019: 11 · 2018: 5 · 2017: 3 · 2016: 11 · 2015: 6 · 2014: 13 · 2013: 7 · 2012: 7
FWCI: 3.10
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 4948 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
ResearchOnline at James Cook University (James Cook University) (submittedVersion)
Funders: Deutsche Forschungsgemeinschaft (01KS9504)
James Cook University
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Keywords: tau protein, lipid peroxidation, acrolein, methylglyoxal, malondialdehyde, glyoxal, protein cross-linking, tau oligomerization, fibril formation, paired helical filaments, Alzheimer's disease, tauopathy, thioflavin T, hyperphosphorylation
MeSH terms: Acrolein, Electrophoresis, Polyacrylamide Gel, Fluorescence, Glyoxal, Humans, Malondialdehyde, Microscopy, Electron, Phosphorylation, Pyruvaldehyde, Blotting, Western, Lipid Peroxidation, Neurofibrillary Tangles, tau Proteins, Glycation End Products, Advanced

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Effect of Pseudophosphorylation and Cross-linking by Lipid Peroxidation and Advanced Glycation End Product Precursors on Tau Aggregation and Filament Formation

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