ArticleMolecular and cellular biochemistry2011
Pre-aggregated Aβ1-42 peptide increases tau aggregation and hyperphosphorylation after short-term application.
Article in Molecular and cellular biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 12 citations in OpenAlex.
- Native PLGA nanoparticles attenuate Aβ-seed induced tau aggregation under in vitro conditions: potential implication in Alzheimer's disease pathology.Scientific reports · 2024Article
- Relationship between neuropsychiatric symptoms and Alzheimer's disease pathology: An in vivo positron emission tomography study.International journal of geriatric psychiatry · 2021Article
- Racemization in Post-Translational Modifications Relevance to Protein Aging, Aggregation and Neurodegeneration: Tip of the Iceberg.Symmetry · 2021Article
- The Protective Effect of Vanadium on Cognitive Impairment and the Neuropathology of Alzheimer's Disease in APPSwe/PS1dE9 Mice.Frontiers in molecular neuroscience · 2020Article
- Review
- Atorvastatin ameliorates cognitive impairment, Aβ1-42 production and Tau hyperphosphorylation in APP/PS1 transgenic mice.Metabolic brain disease · 2016Article
- Caffeoylquinic acids in Centella asiatica protect against amyloid-β toxicity.Journal of Alzheimer's disease : JAD · 2014Article
- Chaperone-dependent Neurodegeneration: A Molecular Perspective on Therapeutic Intervention.Journal of Alzheimer's disease & Parkinsonism · 2013Article
- A partially folded structure of amyloid-beta(1-40) in an aqueous environment.Biochemical and biophysical research communications · 2011Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Neuritic amyloid plaques and neurofibrillary tangles, consisting of hyperphosphorylated tau protein, are the hallmarks of Alzheimer disease. It is not clear so far, how both structures are functionally and physiologically connected. We have investigated the role of Aβ1-42 on hyperphosphorylation and aggregation of tau in SY5Y cells by transfection and overexpression with two tau constructs, a shortened wildtype tau (2N4R) and a point mutation tau (P301L), found in fronto-temporal dementia. It was found that the tau protein becomes hyperphosphorylated and forms large aggregates inside cells, visualized by immunofluorescence, after short incubation of 90 min with preaggregated Aβ1-42. In Addition, Aβ1-42 caused a decrease of tau solubility in both tau constructs in this relatively short time period. Taken together, these experiments suggest that pathological preaggregated Aβ1-42 in physiological concentrations quickly induces hyperphosphorylation and pathological structural changes of tau protein and thereby directly linking the 'amyloid hypothesis' to tau pathology, observed in Alzheimer disease.
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Registered trials
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