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.

Tau is endogenously nitrated in mouse brain : identification of a tyrosine residue modified in vivo by NO / S. Nonnis, G. Cappelletti, F. Taverna, C. Ronchi, S. Ronchi, A. Negri, E. Grassi, G. Tedeschi. - In: NEUROCHEMICAL RESEARCH. - ISSN 0364-3190. - 33:3(2008), pp. 518-525.

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

S. Nonnis;G. Cappelletti;F. Taverna;C. Ronchi;S. Ronchi;A. Negri;E. Grassi;G. Tedeschi
2008

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.
Settore BIO/10 - Biochimica
Settore BIO/06 - Anatomia Comparata e Citologia
2008
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/54886
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