Effect of Nitric Oxide on ADP-ribose Pyrophosphatase Activity
Immune Network
;
: 199-204, 2005.
Article
in English
| WPRIM
| ID: wpr-85874
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.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Pyrophosphatases
/
Bacteria
/
Nitroprusside
/
Adenosine Diphosphate Ribose
/
Protein Processing, Post-Translational
/
Cysteine
/
Hydrolysis
/
Macrophage Activation
/
Macrophages
/
Metabolism
Limits:
Humans
Language:
English
Journal:
Immune Network
Year:
2005
Type:
Article
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