s-nitrosocysteine has been researched along with nitroxyl* in 2 studies
2 other study(ies) available for s-nitrosocysteine and nitroxyl
| Article | Year |
|---|---|
N-nitrosomelatonin outcompetes S-nitrosocysteine in inhibiting glyceraldehyde 3-phosphate dehydrogenase: first evidence that N-nitrosomelatonin can modify protein function.
Low-molecular-weight S-nitrosothiols (RSNOs) are well known for their capability to transnitrosate cysteine residues of enzymes thereby altering their catalytic activity. It is unknown, however, whether N-nitrosomelatonin (NOMela) which is highly effective in transnitrosating low-molecular-weight thiols (RSHs) can also alter protein function. In the present study, we report on such a capability with glyceraldehyde 3-phosphate dehydrogenase (GAPDH) as a target enzyme. Reaction of NOMela with GAPDH resulted in an increase of RSNOs at the expense of RSHs. Somewhat surprisingly, NOMela was about 10-fold more effective than S-nitrosocysteine in inhibiting GAPDH. Vitamin C and glutathione increased the NOMela-dependent inhibition of the enzyme by accelerating the intermediacy of nitroxyl which is also highly effective in nitrosating RSHs. The occurrence of this intermediate during the NOMela-vitamin C reaction was verified by using Mn(III)-tetrakis(1-methyl-4-pyridyl)porphorin pentachloride as nitroxyl scavenger. The NOMela-dependent inactivation of GAPDH was so effective that this reaction can be used to quantify NOMela with high sensitivity. Topics: Ascorbic Acid; Cysteine; Free Radical Scavengers; Glutathione; Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating); Maleimides; Melatonin; Metalloporphyrins; Nitrogen Oxides; Nitroso Compounds; S-Nitrosothiols; Sulfhydryl Compounds | 2008 |
Nitric oxide (NO.) stabilizes whereas nitrosonium (NO+) enhances filopodial outgrowth by rat retinal ganglion cells in vitro.
Recent observations suggest that nitric oxide (NO(.)) can increase or decrease growth cone motility. Here, these apparently paradoxical results are explained by distinct actions of different NO-related species. Filopodial morphology of 223 rat retinal ganglion cells was monitored under computer-enhanced video microscopy in the presence of NO synthase (NOS) substrates or inhibitors, donors of specific NO-related species, and membrane-permeant cyclic nucleotide analogs. Physiological NOS activity induced filopodial outgrowth, whereas inhibition of NOS stabilized filopodia. Similar to NOS, nitrosonium (NO(+) transfer) and peroxynitrite (ONOO(-)), which can regulate the activity of growth-associated proteins by S-nitrosylation and oxidation, respectively, induced filopodial outgrowth. In contrast, NO(.), which stimulates guanylate cyclase to increase cGMP, stabilized filopodial activity. Thus disparate NO-related species may offer a dynamic process of filopodial growth regulation. Topics: Animals; Antioxidants; Cells, Cultured; Cyclic GMP; Cysteine; In Vitro Techniques; Nitric Oxide; Nitric Oxide Donors; Nitrites; Nitrogen Oxides; Nitroso Compounds; Pseudopodia; Rats; Rats, Long-Evans; Retinal Ganglion Cells; S-Nitrosothiols | 2000 |