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Neurofibrillary degeneration and microtubule associated protein tau

S H Yen1, W K Liu

  • 1Department of Pathology, Albert Einstein College of Medicine, Bronx New York.

Insights

Alzheimer disease involves abnormal tau protein filaments. This review details differences in phosphorylation between normal tau and paired helical filament-tau, exploring PHF development mechanisms.

Area of Science:

  • Neuroscience
  • Biochemistry
  • Pathology

Background:

  • Alzheimer disease pathology features neurofibrillary tangles composed of paired helical filaments (PHF).
  • These PHF are derived from the microtubule-associated protein tau.
  • Abnormal phosphorylation of tau is a key modification in PHF formation.

Purpose of the Study:

  • To review recent studies on the differences between normal tau and PHF-tau.
  • To focus on the extent and specific sites of tau phosphorylation.
  • To discuss potential mechanisms underlying PHF development.

Main Methods:

  • Literature review of recent studies on tau phosphorylation.
  • Comparative analysis of normal tau and PHF-tau.
  • Discussion of proposed molecular mechanisms for PHF formation.

Main Results:

  • Significant differences exist in the phosphorylation patterns of normal tau versus PHF-tau.
  • Specific phosphorylation sites are altered in PHF-tau compared to normal tau.
  • Multiple phosphorylation events contribute to tau's transformation into PHF.

Conclusions:

  • Altered phosphorylation is central to the pathogenesis of Alzheimer disease.
  • Understanding tau phosphorylation differences is crucial for elucidating PHF formation.
  • Further research into these mechanisms may reveal therapeutic targets for Alzheimer disease.

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