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Updated: Jun 22, 2026
09:22
In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein
Published on: January 2, 2015
D-Ribosylated Tau forms globular aggregates with high cytotoxicity
Lan Chen1, Yan Wei, Xueqing Wang
1State Key Laboratory of Brain and Cognitive Sciences, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang District, 100101 Beijing, China.
Cellular and Molecular Life Sciences : CMLS
|June 12, 2009
Summary
D-ribose rapidly glycates Tau protein, forming toxic aggregates implicated in Alzheimer's disease. This glycation leads to Tau oligomerization and polymerization, causing cell death.
Area of Science:
- Neuroscience
- Biochemistry
- Cell Biology
Background:
- Tau protein is central to Alzheimer's disease pathogenesis.
- Glycation of Tau contributes to paired helical filament formation.
- The role of D-ribose in Tau glycation remains understudied.
Purpose of the Study:
- To investigate the impact of D-ribose on Tau protein glycation.
- To characterize the resulting Tau aggregates and their cytotoxicity.
Main Methods:
- Incubation of Tau protein with D-ribose.
- Western blotting to detect advanced glycation end-products (AGEs).
- Thioflavin T (ThT) assay for aggregation.
- Atomic force microscopy (AFM) for morphology.
- Cell viability assays using SHSY5Y cells.
Main Results:
- D-ribose rapidly glycated Tau within 24 hours.
- Formation of AGEs and Thioflavin T-positive aggregations observed.
- Ribosylated Tau40 exhibited globular-like morphology.
- Aggregates showed high cytotoxicity, inducing apoptosis and necrosis in SHSY5Y cells.
Conclusions:
- D-ribose significantly accelerates Tau glycation and aggregation.
- Ribosylated Tau forms cytotoxic aggregates relevant to neurodegenerative diseases.
- This highlights a novel pathway in Tau pathology.
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