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Related Experiment Videos

From tangles to tau protein.

K Iqbal1, M Novak

  • 1New York State Institute for Basic Research in Developmental Disabilities, Staten Island, New York, USA. iqbalk@worldnet.att.net

Bratislavske Lekarske Listy
|February 1, 2007
PubMed
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Neurofibrillary tangles in Alzheimer's disease are composed of paired helical filaments (PHF) made of tau protein. Abnormal tau phosphorylation and truncation are key drivers of neurodegeneration in tauopathies.

Area of Science:

  • Neuroscience
  • Biochemistry
  • Pathology

Background:

  • Neurofibrillary tangles (NFTs) are a hallmark of Alzheimer's disease (AD).
  • Their structure and composition remained elusive for decades after initial discovery.
  • Paired helical filaments (PHF) were identified as the main structural component in 1963.

Observation:

  • Microtubule-associated protein tau was identified as the primary component of NFTs in 1986.
  • Tau protein in AD brains exhibits abnormal hyperphosphorylation.
  • Monoclonal antibodies later confirmed tau as the integral component of PHF.

Findings:

  • Tau pathology, including hyperphosphorylation and truncation, is increasingly recognized as central to neurodegenerative diseases.
  • Studies show a correlation between NFT distribution and cognitive decline in AD.

Related Experiment Videos

  • Tau gene mutations are linked to fronto-temporal dementia, highlighting tau's pathogenic role.

    • Implications:

    • Understanding tau's role is crucial for unraveling neurodegenerative mechanisms.
    • Truncation of tau protein has been shown to induce Alzheimer's-type neurofibrillary pathology in vivo.
    • Further research into tau modifications offers potential therapeutic targets for tauopathies.