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Site-specific nitration differentially influences tau assembly in vitro.

Matthew R Reynolds1, Robert W Berry, Lester I Binder

  • 1Department of Cell and Molecular Biology and Cognitive Neurology and Alzheimer's Disease Center, Feinberg School of Medicine, Northwestern University, Chicago, Illinois 60611, USA. m-reynolds@md.northwestern.edu

Biochemistry
|October 19, 2005
PubMed
Summary

Site-specific nitration of tau protein differentially impacts its assembly into filaments, affecting filament length and mass. This modification does not prevent the formation of pathological tau conformations recognized by the Alz-50 antibody.

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Area of Science:

  • Neuroscience
  • Biochemistry
  • Protein Chemistry

Background:

  • Neurofibrillary tangles (NFTs) in Alzheimer's disease are primarily composed of tau protein.
  • Previous work showed peroxynitrite (ONOO-) nitration inhibits tau polymerization.
  • This study investigates site-specific nitration of tau.

Purpose of the Study:

  • To analyze how site-specific tyrosine nitration affects tau protein assembly.
  • To determine the impact of nitration on tau filament morphology and critical concentration.
  • To assess if nitration affects the formation of pathological tau conformations.

Main Methods:

  • In vitro nitration of mutant tau proteins at specific tyrosine residues (Tyr18, Tyr29, Tyr197, Tyr394).
  • Quantitative electron microscopy to analyze filament length, number, and mass.

Related Experiment Videos

  • Measurement of tau critical concentration and antibody binding affinity.

    • Main Results:

    • Site-specific nitration differentially altered tau assembly rates and filament morphology.
    • Nitration at Tyr29 and Tyr197 increased filament length without changing polymer mass.
    • Nitration at Tyr18 and Tyr394 reduced filament length/number, decreasing mass and increasing critical concentration.
    • Nitrated tau formed filaments that bound the Alz-50 antibody with higher avidity than wild-type tau.

    Conclusions:

    • Site-specific tau nitration modulates its nucleation and elongation during filament assembly.
    • The Alz-50 conformation may be necessary but not sufficient for tau filament formation.
    • Nitration impacts tau's pathological assembly process in Alzheimer's disease.