Effect of Nitric Oxide on ADP-ribose Pyrophosphatase Activity.
- Author:
Jong Hyun KIM
1
Author Information
- Publication Type:In Vitro ; Original Article
- Keywords: Nitric oxide; ADP-ribose pyrophosphatase; macrophage; ribosylation
- MeSH: Adenosine Diphosphate Ribose*; Bacteria; Cysteine; Humans; Hydrolysis; Macrophage Activation; Macrophages; Metabolism; Nitric Oxide*; Nitroprusside; Protein Processing, Post-Translational; Pyrophosphatases
- From:Immune Network 2005;5(4):199-204
- CountryRepublic of Korea
- Language:English
- Abstract: BACKGROUND: ADP-ribosyl pyrophosphatases (ADPRase) has been known to catalyze the hydrolysis of ADP-ribose to ribose-5-phosphate and AMP. The role of ADPRase has been suggested to sanitize the cell by removing potentially toxic ADP-ribose. In this study, we examined the effect of nitric oxide on ADPRase activity in macrophages. METHODS: ADPRase activity was measured in NO-inducing J774 cells. For in vitro experiments, recombinant human ADPRase was prepared in bacteria. RESULTS: ADPRase activity was increased by the treatment of exogenous NO generating reagent, sodium nitroprusside (SNP), in J774 cells. The increased ADPRase activity was mediated by the post-translational modification, likely to cause cADP-ribosylation via nitrosylation of cysteine residue on the enzyme. The stimulation with endogeneous NO inducers, TNF-alpha/IFN-gamma, also increased ADPRase activity through NO synthesis. Futhermore, ADPRase activity may be mediated by the post-translational modification of ADPRase, ADP-ribosylation. CONCLUSION: These results indicate that NO synthesized by macrophage activation plays a critical role in the increase in ADPRase activity following ADP-ribose metabolism.
