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In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein
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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
PubMed

Insights

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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