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

被引：13

作者：

Nonnis, Simona ^{[1
]}

Cappelletti, Graziella ^{[2
]}

Taverna, Francesca ^{[1
]}

Ronchi, Cristina ^{[1
]}

Ronchi, Severino ^{[1
]}

Negri, Armando ^{[1
]}

Grassi, Eleonora ^{[1
]}

Tedeschi, Gabriella ^{[1
]}

机构：

[1] Univ Milan, DIPAV, Sect Biochem, I-20100 Milan, Italy

[2] Univ Milan, Dept Biol, I-20133 Milan, Italy

来源：

NEUROCHEMICAL RESEARCH | 2008年 / 33卷 / 03期

关键词：

tau; nitric oxide; brain; cytoskeleton; MALDI-TOF; PC12; cells;

D O I：

10.1007/s11064-007-9467-x

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

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收藏

页码：518 / 525

页数：8

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