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Structure of NFT: Biochemical Approach.

Masato Hasegawa1

  • 1Department of Dementia and Higher Brain Function, Tokyo Metropolitan Institute of Medical Science, Tokyo, Japan. hasegawa-ms@igakuken.or.jp.

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|February 26, 2020
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Summary

Neurofibrillary tangles (NFTs), a hallmark of Alzheimer's disease (AD), are composed of hyperphosphorylated tau protein. Different tau pathologies drive neurodegeneration in various dementias, with distinct aggregate structures.

Keywords:
FilamentsPhosphorylationPrion-likePropagationProtease-resistantTau

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Area of Science:

  • Neuroscience
  • Biochemistry
  • Pathology

Background:

  • Neurofibrillary tangles (NFTs) are key pathological hallmarks of Alzheimer's disease (AD).
  • NFTs are primarily composed of hyperphosphorylated tau protein, and their spread correlates with AD progression.
  • Tau gene mutations (FTDP-17) demonstrate tau abnormalities cause neurodegeneration.

Purpose of the Study:

  • To investigate the composition and structure of NFTs in Alzheimer's disease and related tauopathies.
  • To understand the role of tau protein abnormalities in neurodegenerative diseases.
  • To elucidate the molecular mechanisms of protein aggregation and prion-like propagation.

Main Methods:

  • Partial purification of NFTs based on insolubility.
  • Production and characterization of antibodies against NFT components.
  • Biochemical and proteinchemical analyses of pathological tau proteins.
  • Cryo-electron microscopy (Cryo-EM) analysis of tau filament structures.

Main Results:

  • Hyperphosphorylated tau protein identified as the major component of NFTs.
  • Abnormal tau pathology observed in various neurodegenerative dementias (PiD, PSP, CBD) with distinct tau isoforms.
  • Biochemical analyses revealed disease-specific microtubule-binding regions in tau aggregates.
  • Cryo-EM confirmed distinct core structures of tau filaments in AD and PiD.

Conclusions:

  • Tau protein abnormalities are central to the pathogenesis of AD and other tauopathies.
  • Disease-specific structures of tau aggregates suggest distinct mechanisms of aggregation and propagation.
  • Further research into tau and other abnormal proteins is crucial for understanding neurodegenerative diseases.