Protein Tyrosine Nitration: Selectivity, physicochemical and biological consequences, denitration and proteomics methods for the identification of tyrosine-nitrated proteins

Abello, N., Kerstjens, H. A. M., Postma, D. S. & Bischoff, R., 2009, In : J Proteome Res.. 8, p. 3222 - 3238

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Protein tyrosine nitration (PTN) is a post-translational modification occurring under the action of a nitrating agent. Tyrosine is modified in the 3-position of the phenolic ring through the addition of a nitro group (NO2). In the present article, we review the main nitration reactions and elucidate why nitration is not a random chemical process. The particular physical and chemical properties of 3-nitrotyrosine (e.g. pKa, spectrophotometric properties, reduction to aminotyrosine) will be discussed as well as the biological consequences of PTN (e.g. modification of enzymatic activity, sensitivity to proteolytic degradation, impact on protein phosphorylation, immunogenicity and implication in disease). Recent data indicate the possibility of an in vivo denitration process, which will be discussed with respect to the different reaction mechanisms that have been proposed. The second part of this article reviews the major challenges in developing analytical methods to determine PTN in complex proteomes
Original languageDutch
Pages (from-to)3222 - 3238
JournalJ Proteome Res.
Publication statusPublished - 2009

ID: 1940314