Unknown

Dataset Information

0

Deactivation of neutrophil NADPH oxidase by actin-depolymerizing agents in a cell-free system.


ABSTRACT: The cell-free activation of human neutrophil NADPH oxidase (O(2)(-)-generating enzyme) is enhanced by actin [Morimatsu, Kawagoshi, Yoshida and Tamura (1997) Biochem. Biophys. Res. Commun. 230, 206--210]. In an attempt to elucidate the mechanism, we examined the effect of actin-depolymerizing agents on the duration of NADPH oxidase in a cell-free system. The addition of DNase I, an F-actin-depolymerizing protein, caused an accelerated deactivation of the oxidase. The deactivation was also facilitated by latrunculin A, a sponge toxin that depolymerizes F-actin. Exogenously added actin prevented the deactivation by DNase I or latrunculin A, whereas EDTA accelerated a dilution-induced deactivation of the oxidase and Mg(2+) ions retarded it. The stability in dilution was found to correlate well with free Mg(2+) concentration. Estimation of F-actin in the system showed that F-actin increased during the oxidase activation and that DNase I or EDTA decreased F-actin content in parallel with the activity. Treatment of the cell-free mixture with a chemical cross-linker prevented the deactivation and F-actin decrease by EDTA. Taken together, these results suggest that actin filaments which grow during the activation of NADPH oxidase prolong the lifetime of the oxidase.

SUBMITTER: Tamura M 

PROVIDER: S-EPMC1221158 | biostudies-other | 2000 Jul

REPOSITORIES: biostudies-other

Similar Datasets

| S-EPMC1132836 | biostudies-other
| S-EPMC1138850 | biostudies-other
| S-EPMC3095934 | biostudies-literature
| S-EPMC1216942 | biostudies-other
| S-EPMC5969376 | biostudies-literature
| S-EPMC4221629 | biostudies-literature
| S-EPMC2937925 | biostudies-literature
| S-EPMC7082617 | biostudies-literature
| S-EPMC1220046 | biostudies-other
| S-EPMC6834254 | biostudies-literature