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S-nitrosylation signaling in cell biology Gaston BM; Carver J; Doctor A; Palmer LAMol Interv 2003[Aug]; 3 (5): 253-63S-Nitrosylated proteins form when a cysteine thiol reacts with nitric oxide (NO) in the presence of an electron acceptor to form an S-NO bond. Under physiological conditions, this posttranslational modification affects the function a wide array of cell proteins, ranging from ion channels to nuclear regulatory proteins. Recent evidence suggests that 1) S-nitrosylated proteins can be synthesized by exposure of specific redox-active motifs to NO, through transnitrosation/transfer reactions, or through metalloprotein-catalyzed reactions; 2) S-nitrosothiols can be sequestered in membranes, lipophilic protein folds, or in vesicles to preserve their activity; and 3) S-nitrosothiols can be degraded by a number of enzymes systems. These recent insights regarding the bioactivities, molecular signaling pathways, and metabolism of endogenous S-nitrosothiols have suggested several new therapies for disease ranging from cystic fibrosis to pulmonary hypertension.|DNA-Binding Proteins/metabolism[MESH]|Enzyme Inhibitors/metabolism[MESH]|Humans[MESH]|Hypoxia-Inducible Factor 1[MESH]|Hypoxia-Inducible Factor 1, alpha Subunit[MESH]|Isoxazoles/metabolism[MESH]|Nitric Oxide Donors/metabolism[MESH]|Nitric Oxide/metabolism[MESH]|Nuclear Proteins/metabolism[MESH]|Oxidation-Reduction[MESH]|S-Nitrosoglutathione/metabolism[MESH]|S-Nitrosothiols/*metabolism[MESH]|Signal Transduction/physiology[MESH]|Superoxide Dismutase/metabolism[MESH]|Transcription Factors/metabolism[MESH] |
