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Related Experiment Videos

Neurofibrillary tangles and tau phosphorylation.

J P Brion1, B H Anderton, M Authelet

  • 1Laboratory of Histology, Neuroanatomy and Neuropathology, Université Libre de Bruxelles, 808 Route de Lennik, 1070 Brussels, Belgium.

Biochemical Society Symposium
|July 13, 2001
PubMed
Summary

Neurofibrillary tangles in Alzheimer's disease are linked to reduced microtubule stability. Glycogen synthase kinase-3 beta activity influences tau phosphorylation, impacting microtubule function and potentially contributing to neuronal dysfunction.

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Area of Science:

  • Neuroscience
  • Cell Biology
  • Pathology

Background:

  • Neurofibrillary tangles (NFTs) composed of hyperphosphorylated tau are hallmarks of Alzheimer's disease (AD).
  • Microtubule stability is crucial for neuronal function.

Purpose of the Study:

  • Investigate the relationship between NFTs and microtubule stability.
  • Examine how tau phosphorylation and function are affected in AD models.
  • Determine the role of glycogen synthase kinase-3 beta (GSK-3 beta) in tau phosphorylation and microtubule interactions.

Main Methods:

  • Analysis of acetylated alpha-tubulin and tubulin mRNA in NFT-bearing neurons.
  • Transfection studies with mutated tau forms and co-expression with beta-amyloid precursor protein and presenilins.
  • Neuroanatomical study of GSK-3 beta distribution.

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  • Studies on GSK-3 beta activity in cultured neurons and transfected cells.
  • Generation of transgenic mouse models (tau isoform, tau + mutated presenilin 1).

    • Main Results:

    • NFT-bearing neurons showed reduced acetylated alpha-tubulin and tubulin mRNA.
    • Mutated tau forms were less effective in sustaining microtubule growth.
    • GSK-3 beta compartmentalization paralleled phosphorylated tau development.
    • GSK-3 beta activity controlled tau phosphorylation and microtubule interaction.
    • Tau phosphorylation was unaffected by beta-amyloid precursor protein overexpression.
    • Transgenic mice showed somatodendritic accumulation of phosphorylated tau but not NFTs.

    Conclusions:

    • Microtubule network destabilization is a key mechanism in Alzheimer's disease neuronal dysfunction.
    • GSK-3 beta plays a critical role in regulating tau phosphorylation and its interaction with microtubules.
    • Additional factors beyond tau and presenilin mutations may be required for NFT formation.