Protein tyrosine nitration in mouse peritoneal macrophages activated in vitro and in vivo: evidence against an essential role of peroxynitrite

Citation
S. Pfeiffer et al., Protein tyrosine nitration in mouse peritoneal macrophages activated in vitro and in vivo: evidence against an essential role of peroxynitrite, FASEB J, 15(13), 2001, pp. 2355-2364
Citations number
58
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Experimental Biology
Journal title
FASEB JOURNAL
ISSN journal
0892-6638 → ACNP
Volume
15
Issue
13
Year of publication
2001
Pages
2355 - 2364
Database
ISI
SICI code
0892-6638(200111)15:13<2355:PTNIMP>2.0.ZU;2-B
Abstract
Tyrosine nitration is considered a key reaction of peroxynitrite-triggered tissue injury in inflammatory diseases. We investigated the potential invol vement of peroxynitrite in protein tyrosine nitration in isolated murine pe ritoneal macrophages activated either in vitro with interferon-gamma /lipop olysaccharide or in vivo by priming mice with Corynebacterium parvum (10 mg x kg(-1)). Both protocols led to release of NO and accumulation of nitrite accompanied by formation of protein-bound 3-nitrotyrosine. Oxidation of di hydrorhodamine 123, a measure of peroxynitrite release, remained close to b asal levels upon in vitro activation of the macrophages but was increased;t wofold in vivo. Tyrosine nitration in macrophages activated in vitro was in hibited by catalase and the time course of nitration correlated with nitrit e accumulation, whereas superoxide (O-2(radical anion)) and H2O2 release oc curred at much earlier times. To address the contribution of O-2(radical an ion) and peroxynitrite to in vivo nitration, a O-2(radical anion) scavenger (MnTBAP; 1 mg x kg(-1)) was given to C. parvum-primed mice. MnTBAP led to almost complete inhibition of C. parvum-triggered O-2(radical anion) and pe roxynitrite release, whereas nitrite accumulation and formation of 3-nitrot yrosine were less affected (similar to 50% of controls). These results argu e against an essential role of peroxynitrite in protein tyrosine nitration in vivo.