Protein S-nitrosylation: A physiological signal for neuronal nitric oxide Journal Article
| Authors: | Jaffrey, S. R.; Erdjument-Bromage, H.; Ferris, C. D.; Tempst, P.; Snyder, S. H. |
| Article Title: | Protein S-nitrosylation: A physiological signal for neuronal nitric oxide |
| Abstract: | Nitric oxide (NO) has been linked to numerous physiological and pathophysiological events that are not readily explained by the well established effects of NO on soluble guanylyl cyclase. Exogenous NO S-nitrosylates cysteine residues in proteins, but whether this is an important function of endogenous NO is unclear. Here, using a new proteomic approach, we identify a population of proteins that are endogenously S-nitrosylated, and demonstrate the loss of this modification in mice harbouring a genomic deletion of neuronal NO synthase (nNOS). Targets of NO include metabolic, structural and signalling proteins that may be effectors for neuronally generated NO. These findings establish protein S-nitrosylation as a physiological signalling mechanism for nNOS. |
| Keywords: | signal transduction; gene deletion; nonhuman; cell proliferation; mass spectrometry; proteins; proteome; animal cell; animals; mice; cerebellum; apoptosis; nerve tissue proteins; animalia; molecular sequence data; immunoblotting; target cell; rats; genes, ras; nerve cell; glutathione; nitric oxide synthase; nitric oxide synthase type i; enzyme modification; protein modification; acetylation; biotinylation; enzyme active site; hydrazines; nitric oxide; neurotransmitter release; nitrogen oxides; chemoluminescence; protein s; nitric oxide donors; priority journal; article; mercaptoethanol; nitroso compounds; s-nitrosoglutathione; s-nitrosothiols |
| Journal Title: | Nature Cell Biology |
| Volume: | 3 |
| Issue: | 2 |
| ISSN: | 1465-7392 |
| Publisher: | Nature Publishing Group |
| Date Published: | 2001-02-01 |
| Start Page: | 193 |
| End Page: | 197 |
| Language: | English |
| DOI: | 10.1038/35055104 |
| PUBMED: | 11175752 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | Export Date: 21 May 2015 -- Source: Scopus |
