Original contribution
Reaction products of 1-naphthol with reactive oxygen species prevent NADPH oxidase activation in activated human neutrophils, but leave phagocytosis intact

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Abstract

Activation of human neutrophils with opsonized particles in the presence of a nontoxic dose of 1-naphthol resulted in inhibition of superoxide anion production but not of the phagocytotic activity of the cells. In this study we have investigated the mechanism of action of 1-naphthol. The inhibition is not at the level of cellular activation since the FMLP-induced rise of intracellular free calcium was unaffected. Our results show that the (metabolic) activation of 1-naphthol to 1,4-naphthoquinone by reaction with H2O2 from the oxidative burst is a necessary event for the inhibition to occur. The study provides evidence that by its reactivity with essential thiol groups 1,4-naphthoquinone (1,4-NQ) prevents the assembly of a functional NADPH-oxidase in the neutrophil membrane.

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Cited by (22)

  • The reactivity of ortho-methoxy-substituted catechol radicals with sulfhydryl groups: Contribution for the comprehension of the mechanism of inhibition of NADPH oxidase by apocynin

    2007, Biochemical Pharmacology
    Citation Excerpt :

    The same property has been reported for N-ethylmaleimide and oxidation products of 1-naphthol. The explanation for the effects of these compounds is based on the generation of electrophilic quinones that conjugate with essential thiol residues, present in the cytosolic component p47phox via Michael addition [25,26]. For apocynin, the inhibition of the migration of the cytosolic component p47phox does not match this mechanism.

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