Peroxynitrite-induced nitrative and oxidative modifications alter tau filament formation.

ABSTRACT: Tau undergoes numerous posttranslational modifications during the progression of Alzheimer's disease (AD). Some of these changes accelerate tau aggregation, while others are inhibitory. AD-associated inflammation is thought to create oxygen and nitrogen radicals such as peroxynitrite (PN). In vitro, PN can nitrate many proteins, including tau. We have previously demonstrated that tau's ability to form filaments is profoundly affected by treatment with PN and have attributed this inhibition to tyrosine nitration. However, PN is highly reactive and unstable leading to oxidative amino acid modifications through its free radical byproducts. To test whether PN can modify other amino acids in tau via oxidative modifications, a mutant form of the tau protein lacking all tyrosines (5XY → F) was co

SUBMITTER: Vana L 

PROVIDER: S-EPMC3040256 | biostudies-literature | 2011 Feb

REPOSITORIES: biostudies-literature