[HTML][HTML] Myeloperoxidase produces nitrating oxidants in vivo

JP Gaut, J Byun, HD Tran, WM Lauber… - The Journal of …, 2002 - Am Soc Clin Investig
JP Gaut, J Byun, HD Tran, WM Lauber, JA Carroll, RS Hotchkiss, A Belaaouaj, JW Heinecke
The Journal of clinical investigation, 2002Am Soc Clin Investig
Despite intense interest in pathways that generate reactive nitrogen species, the
physiologically relevant mechanisms for inflammatory tissue injury remain poorly
understood. One possible mediator is myeloperoxidase, a major constituent of neutrophils,
monocytes, and some populations of macrophages. The enzyme uses hydrogen peroxide
and nitrite to generate 3-nitrotyrosine in vitro. To determine whether myeloperoxidase
produces nitrating intermediates in vivo, we used isotope dilution gas chromatography/mass …
Despite intense interest in pathways that generate reactive nitrogen species, the physiologically relevant mechanisms for inflammatory tissue injury remain poorly understood. One possible mediator is myeloperoxidase, a major constituent of neutrophils, monocytes, and some populations of macrophages. The enzyme uses hydrogen peroxide and nitrite to generate 3-nitrotyrosine in vitro. To determine whether myeloperoxidase produces nitrating intermediates in vivo, we used isotope dilution gas chromatography/mass spectrometry to quantify 3-nitrotyrosine in two models of peritoneal inflammation: mice infected with Klebsiella pneumoniae and mice subjected to cecal ligation and puncture. Both models developed an intense neutrophil inflammatory response, and the inflammatory fluid contained markedly elevated levels of 3-chlorotyrosine, a marker of myeloperoxidase action. In striking contrast, 3-nitrotyrosine levels rose only in the mice infected with K. pneumoniae. Levels of total nitrite and nitrate were 20-fold higher in mice injected with K. pneumoniae than in mice subjected to cecal ligation and puncture. Levels of 3-nitrotyrosine failed to increase in mice infected with K. pneumoniae that lacked functional myeloperoxidase. Our observations provide strong evidence that myeloperoxidase generates reactive nitrogen species in vivo and that it operates in this fashion only when nitrite and nitrate become available.
The Journal of Clinical Investigation