Prostacyclin synthase , tyrosine nitration

There are numerous data that peroxynitrite is involved in cell death and tissue injuries in many clinical conditions. An important mechanism underlying peroxynitrite toxicity is the reaction of tyrosine nitration. Tyrosine nitration inactivates certain enzymes, as was postulated for prostacyclin (PGI2) synthase (M14), cytochrome P450 2B1 (RIO), tyrosine hydroxylase (A 14), and MnSOD (Yl). Moreover, nitration blocks tyrosine phosphorylation, and thus interferes with the tyrosine kinase signaling pathways (K18). The peroxynitrite treatment of rat liver epithelial cells stimulates mitogen-activated protein kinases p38 MAPK, JNK1/2, and ERK1/2 the mechanism of this effect awaits elucidation (S9). 

Zou, M., C. Martin, and V Ullrich (1997). Tyrosine nitration as a mechanism of selective inactivation of prostacyclin synthase by peroxynitrite. Biol. Chem. 378, 707-713. 

M. Arsic, M. Bachschmid et al. (2003). Specific nitration at tyrosine-430 revealed by high resolution mass spectrometry as basis for redox regulation of bovine prostacyclin synthase. J. Biol. Chem. 278, 12813-12819. 

Nie, H., Wu, J.-L, Zhang, M.,etal. (2006) EndotheUal Nitric Oxide Synthase-Dependent Tyrosine Nitration of Prostacyclin Synthase in Diabetes In Vivo. Diabetes, 55 (11), 3133-3141. 

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