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Tyrosine-Nitrated Proteins: Proteomic and Bioanalytical Aspects
#MMPMID27324931
Batthyány C
; Bartesaghi S
; Mastrogiovanni M
; Lima A
; Demicheli V
; Radi R
Antioxid Redox Signal
2017[Mar]; 26
(7
): 313-328
PMID27324931
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SIGNIFICANCE: "Nitroproteomic" is under active development, as 3-nitrotyrosine in
proteins constitutes a footprint left by the reactions of nitric oxide-derived
oxidants that are usually associated to oxidative stress conditions. Moreover,
protein tyrosine nitration can cause structural and functional changes, which may
be of pathophysiological relevance for human disease conditions. Biological
protein tyrosine nitration is a free radical process involving the intermediacy
of tyrosyl radicals; in spite of being a nonenzymatic process, nitration is
selectively directed toward a limited subset of tyrosine residues. Precise
identification and quantitation of 3-nitrotyrosine in proteins has represented a
"tour de force" for researchers. Recent Advances: A small number of proteins are
preferential targets of nitration (usually less than 100 proteins per proteome),
contrasting with the large number of proteins modified by other
post-translational modifications such as phosphorylation, acetylation, and,
notably, S-nitrosation. Proteomic approaches have revealed key features of
tyrosine nitration both in vivo and in vitro, including selectivity, site
specificity, and effects in protein structure and function. CRITICAL ISSUES:
Identification of 3-nitrotyrosine-containing proteins and mapping nitrated
residues is challenging, due to low abundance of this oxidative modification in
biological samples and its unfriendly behavior in mass spectrometry (MS)-based
technologies, that is, MALDI, electrospray ionization, and collision-induced
dissociation. FUTURE DIRECTIONS: The use of (i) classical two-dimensional
electrophoresis with immunochemical detection of nitrated proteins followed by
protein ID by regular MS/MS in combination with (ii) immuno-enrichment of
tyrosine-nitrated peptides and (iii) identification of nitrated peptides by a
MIDAS? experiment is arising as a potent methodology to unambiguously map and
quantitate tyrosine-nitrated proteins in vivo. Antioxid. Redox Signal. 26,
313-328.
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