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Related Experiment Videos

Hyperphosphorylation of tau in PHF

M Morishima-Kawashima1, M Hasegawa, K Takio

  • 1Department of Neuropathology, Faculty of Medicine, University of Tokyo, Japan.

Neurobiology of Aging
|May 1, 1995
PubMed
Summary

Abnormal tau protein phosphorylation in paired helical filaments (PHF) is linked to neurodegenerative diseases. This study identified specific phosphorylation sites on PHF-tau and fetal tau, revealing distinct hyperphosphorylation patterns in PHF-tau.

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Area of Science:

  • Neuroscience
  • Biochemistry
  • Cell Biology

Background:

  • Paired helical filament (PHF)-tau is a hallmark of tauopathies, characterized by hyperphosphorylation.
  • Immunochemical studies suggest similarities between PHF-tau and fetal tau phosphorylation patterns.

Purpose of the Study:

  • To precisely determine the phosphorylation sites in both PHF-tau and fetal rat tau.
  • To compare the phosphorylation profiles and identify unique sites in PHF-tau.

Main Methods:

  • Utilized ion-spray mass spectrometry for precise identification of phosphorylation sites.
  • Employed sequencing of ethanethiol-modified peptides to analyze tau protein.

Main Results:

  • Identified 19 distinct phosphorylation sites in PHF-tau, primarily in flanking regions of the microtubule-binding domain.

Related Experiment Videos

  • Found that half of the identified phosphorylation sites in PHF-tau are also present in fetal tau.
  • Observed that while fetal tau phosphorylation is predominantly proline-directed, PHF-tau exhibits both proline-directed and nonproline-directed phosphorylation.

    • Conclusions:

    • PHF-tau is significantly hyperphosphorylated compared to fetal tau, with additional nonproline-directed phosphorylation sites.
    • This hyperphosphorylation, including fetal-type and additional sites, may contribute to PHF-tau's aberrant properties, such as assembly incompetence.
    • The findings provide detailed insights into tau pathology and potential therapeutic targets.