ArticleThe Biochemical journal2000
Deactivation of neutrophil NADPH oxidase by actin-depolymerizing agents in a cell-free system.
Article in The Biochemical journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 31 citations in OpenAlex.
- Differential dysregulation of granule subsets in WASH-deficient neutrophil leukocytes resulting in inflammation.Nature communications · 2022Article
- Siglec-8 Signals Through a Non-Canonical Pathway to Cause Human Eosinophil DeathFrontiers in immunology · 2021Article
- Capping Protein Modulates Actin Remodeling in Response to Reactive Oxygen Species during Plant Innate Immunity.Plant physiology · 2017Article
- Post-translational modification and regulation of actin.Current opinion in cell biology · 2013Review
- Effects of F/G-actin ratio and actin turn-over rate on NADPH oxidase activity in microglia.BMC immunology · 2010Article
- DNase I inhibits a late phase of reactive oxygen species production in neutrophils.Journal of innate immunity · 2009Article
- Phosphorylation of the leucocyte NADPH oxidase subunit p47(phox) by casein kinase 2: conformation-dependent phosphorylation and modulation of oxidase activity.The Biochemical journal · 2001Article
- Effect of cytochalasin D on the respiratory burst of primed neutrophils activated with a secondary stimulus.Doklady. Biochemistry and biophysicsArticle
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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.
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