Immune Netw.  2005 Dec;5(4):199-204. 10.4110/in.2005.5.4.199.

Effect of Nitric Oxide on ADP-ribose Pyrophosphatase Activity

• Kim JH

• KMID: 1846706
• DOI: http://doi.org/10.4110/in.2005.5.4.199

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.

Keyword

Nitric oxide; ADP-ribose pyrophosphatase; macrophage; ribosylation

MeSH Terms

Adenosine Diphosphate Ribose*
Bacteria
Cysteine
Humans
Hydrolysis
Macrophage Activation
Macrophages
Metabolism
Nitric Oxide*
Nitroprusside
Protein Processing, Post-Translational
Pyrophosphatases
Adenosine Diphosphate Ribose
Cysteine
Nitric Oxide
Nitroprusside
Pyrophosphatases