ArticleThe Biochemical journal1996
Spermine suppresses the activation of human neutrophil NADPH oxidase in cell-free and semi-recombinant systems.
Article in The Biochemical journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 29 citations in OpenAlex.
- The arginase-polyamine signaling axis in immune cells: Implications for immune modulation and host-pathogen interactions.iScience · 2026Review
- METTL3-IGF2BP3-axis mediates the proliferation and migration of pancreatic cancer by regulating spermine synthase m6A modification.Frontiers in oncology · 2022Article
- Reactive oxygen species and nitric oxide are involved in polyamine-induced growth inhibition in wheat plants.Protoplasma · 2018Article
- Investigation of Polyamine Metabolism and Homeostasis in Pancreatic Cancers.Medical sciences (Basel, Switzerland) · 2017Article
- Protein cross-linking by chlorinated polyamines and transglutamylation stabilizes neutrophil extracellular traps.Cell death & disease · 2016Article
- [The influence of diabetes mellitus on male reproductive function: a poorly investigated aspect of male infertility].Der Urologe. Ausg. A · 2011Article
- Article
- Involvement of polyamines in the chilling tolerance of cucumber cultivars.Plant physiology · 2000Article
- Deactivation of neutrophil NADPH oxidase by actin-depolymerizing agents in a cell-free system.The Biochemical journal · 2000Article
- Effects of polyamine levels on the degradation of short-lived and long-lived proteins in cultured L-132 human lung cells.The Biochemical journal · 1998Article
- Spermine partially normalizes in vivo antioxidant defense potential in certain brain regions in transiently hypoperfused rat brain.Neurochemical research · 1996Article
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
Abstract
Spermine, a cellular polyamine, down-regulates O2- generation in human neutrophils stimulated by receptor-linked agonist [Ogata, Tamura and Takeshita (1992) Biochem. Biophys. Res. Commun. 182, 20-26]. In this study, to elucidate the mechanism for the inhibition, the effect of spermine on cell-free activation of the O2- generating enzyme (NADPH oxidase) was examined. Spermine suppressed the SDS-induced activation of NADPH oxidase in a dose-dependent manner with an IC50 of 18 microM. The inhibition was specific for spermine over its precursor amines, spermidine and putrescine. Spermine did not alter the Km for NADPH or the optimal concentration of SDS for activation. The amine was inhibitory only when added before activation, indicating that it affects the activation process rather than the enzyme's activity. An increased concentration of cytosol partly prevented the inhibition by spermine. In semi-recombinant cell-free system, spermine inhibited the activation of NADPH oxidase as effectively as in the cell-free system (IC50 = 13 microM). Pretreatment of each recombinant cytosolic component with spermine revealed that they (especially p67phox) are sensitive to spermine. These results suggest that spermine interacts with cytosolic component(s) and impairs the assembly of NADPH oxidase.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.