Nitric Oxide and Posttranslational Modification of the Vascular Proteome: S-Nitrosation of Reactive Thiols

D. E. Handy
2006 Arteriosclerosis, Thrombosis and Vascular Biology  
Nitric oxide (NO⅐) is known to exert its effects via guanylyl cyclase and cyclic GMP-dependent pathways and by cyclic GMP-independent pathways, including the posttranslational modification of proteins. Much ongoing research is focused on defining the mechanisms of NO⅐-mediated protein modification, the identity and function of the modified proteins, and the significance of these changes in health and disease. S-nitrosation or thionitrite formation has only been found on a limited number of
more » ... ues in a subset of proteins in in vitro and in vivo studies. Protein S-nitrosation also appears to be reversible. There are several theories about the in vivo S-nitrosating agent, and most suggest a role for oxidation products of NO⅐ in this process. Flux in cellular S-nitrosoprotein pools appears to be regulated by NO⅐ availability and is redox-sensitive. An analysis of S-nitrosation in candidate proteins has clarified the mechanism by which NO⅐ regulates enzymatic and cellular functions. These findings suggest the utility of using proteomic methods to identify unique targets for protein S-nitrosation to understand further the molecular mechanisms of the effects of NO⅐.
doi:10.1161/01.atv.0000217632.98717.a0 pmid:16543494 fatcat:dhh5jfplhzhujham2pfqvbr3wq