ABSTRACT
This chapter considers that role of S-nitrosoglutathione (GSNO) in the critical regulation of the actions of nitric oxide in a mammalian system. GSNO can transfer its NO moiety to a cysteine thiol, resulting in the posttranslational modification of S-nitrosation of a target thiol. The posttranslational modification of proteins has long been recognized as a key regulator of cellular function. S-Nitrosation in the cell is highly dependent on the availability of intracellular GSNO. As GSNO concentrations increase, so do levels of total protein S-nitrosation. S-Nitrosoglutathione reductase utilizes the coenzyme NADH to carry out a 2e- reduction of GSNO to generate glutathione sulfinamide before it is further reduced back to glutathione by glutathione reductase. The aberrant expression of this enzyme is associated with disease. In fact, the deletion of the GSNO reductase gene increases both the levels of GSNO and total protein S-nitrosation in vivo.
