Tau is endogenously nitrated in mouse brain: identification of a tyrosine residue modified in vivo by NO

Neurochem Res. 2008 Mar;33(3):518-25. doi: 10.1007/s11064-007-9467-x. Epub 2007 Sep 2.

Abstract

Nitration of tau protein is normally linked to neurodegeneration but, until now, no comprehensive information is available regarding tau nitration in healthy subjects. It has been previously reported that in differentiated PC12 cells, tau co-immunoprecipitated with alpha-tubulin is nitrated at tyrosine residues and that this post-translation modification doesn't impair the association of tau with the cytoskeleton. The present paper is focused on the identification of tyrosine residues endogenously modified in tau from PC12 cells and reports for the first time that tau is also nitrated in vivo in normal mouse brain and that one tyrosine is endogenously modified.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Blotting, Western
  • Brain Chemistry / drug effects*
  • Electrophoresis, Gel, Two-Dimensional
  • Hydrogen-Ion Concentration
  • Immunoprecipitation
  • Isomerism
  • Mice
  • Nitrates / metabolism*
  • Nitric Oxide / pharmacology*
  • PC12 Cells
  • Rats
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
  • Tyrosine / metabolism*
  • tau Proteins / metabolism*

Substances

  • Nitrates
  • tau Proteins
  • Nitric Oxide
  • Tyrosine