Tau is endogenously nitrated in mouse brain: identification of a tyrosine residue modified in vivo by NO.
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.
Nonnis
Simona
S
DIPAV - Section of Biochemistry, University of Milano, Via Celoria 10, Milano 20100, Italy.
Cappelletti
Graziella
G
Taverna
Francesca
F
Ronchi
Cristina
C
Ronchi
Severino
S
Negri
Armando
A
Grassi
Eleonora
E
Tedeschi
Gabriella
G
D000818:Animals; D015153:Blotting, Western; D001923:Brain Chemistry / Q000187:drug effects*; D015180:Electrophoresis, Gel, Two-Dimensional; D006863:Hydrogen-Ion Concentration; D047468:Immunoprecipitation; D007536:Isomerism; D051379:Mice; D009566:Nitrates / Q000378:metabolism*; D009569:Nitric Oxide / Q000494:pharmacology*; D016716:PC12 Cells; D051381:Rats; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D014443:Tyrosine / Q000378:metabolism*; D016875:tau Proteins / Q000378:metabolism*
D009566:Nitrates; D016875:tau Proteins; D009569:Nitric Oxide; D014443:Tyrosine