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In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein
Published on: January 2, 2015
Pre-aggregated Aβ1-42 peptide increases tau aggregation and hyperphosphorylation after short-term application
Sabine Ott1, Andreas Wolfram Henkel, Maria Kerstin Henkel
1Department of Psychiatry and Psychotherapy, University Hospital of Erlangen, Erlangen, Germany.
Molecular and Cellular Biochemistry
|November 30, 2010
Summary
Pre-aggregated amyloid-beta (Aβ1-42) rapidly triggers tau protein hyperphosphorylation and aggregation in neuronal cells. This finding directly links the amyloid hypothesis to tau pathology in Alzheimer disease.
Area of Science:
- Neuroscience
- Cell Biology
- Biochemistry
Background:
- Alzheimer disease (AD) is characterized by amyloid plaques and neurofibrillary tangles.
- The precise connection between amyloid-beta (Aβ) and tau pathology in AD remains unclear.
Purpose of the Study:
- To investigate the effect of Aβ1-42 on tau hyperphosphorylation and aggregation.
- To explore the functional and physiological link between Aβ and tau in Alzheimer disease.
Main Methods:
- Overexpression of wildtype (2N4R) and mutant (P301L) tau constructs in SY5Y cells.
- Incubation with pre-aggregated Aβ1-42.
- Immunofluorescence microscopy to visualize tau aggregation.
- Assessment of tau solubility.
Main Results:
- Short incubation (90 min) with Aβ1-42 induced tau hyperphosphorylation and aggregation.
- Aβ1-42 decreased tau solubility for both wildtype and mutant tau constructs.
- Pathological changes in tau occurred rapidly in response to Aβ1-42.
Conclusions:
- Pathological Aβ1-42 directly and rapidly induces tau hyperphosphorylation and aggregation.
- This study provides a direct link between the amyloid hypothesis and tau pathology in Alzheimer disease.
- Findings suggest Aβ's role in initiating tau-related neurodegeneration.
