Inhibition of neutrophil superoxide secretion by of preservative, methylhydroxybenzoate: Effects mediated by perturbation of intracellular ca2+?

Steven W. Edwards, John M. Humphreys, Charles D. Taylor, Alexia M. A. Soulioti, Anne H. Brunton, Geoffrey M. Gadd, C. Anthony Hart, B. Halliwell

    Research output: Contribution to journalArticlepeer-review

    5 Citations (Scopus)

    Abstract

    The preservative, methylhydroxybenzoate inhibited O2- secretion from human neutrophils activated by both the chemotactic peptide fMet-Leu-Phe and phorbol myristate acetate (PMA): the low level of oxidant secretion activated by the ionophore A23187 was similarly reduced in preservative-treated suspensions. Oxidant secretion was similarly reduced in fMet-Leu-Phe and A23187 treated suspensions in which intracellular Ca2+ was buffered by loading with Quin-2, indicating that methylhydroxybenzoate may exert its effects by perturbation of intracellular Ca2+ -dependent processes. Methylhydroxybenzoate could mimic EGTA in preventing the Ca2+ dependent enhancement of trypsin activity and could also bind this cation in experiments using a Ca2+ electrode, although the preservative bound Ca2+ more slowly and had a lower affinity than EGTA. These data indicate that methylhydroxybenzoate may exert its effects on neutrophils by perturbation of Ca2+-dependent activation pathways and this phenomenon may also explain its other known pharmacological effects. Furthermore, these observations provide an insight into the mechanisms by which intracellular Ca2+ may regulate oxidant secretion.

    Original languageEnglish
    Pages (from-to)333-343
    Number of pages11
    JournalFree Radical Research
    Volume10
    Issue number6
    DOIs
    Publication statusPublished - 1990

    Keywords

    • Calcium
    • Methylhydroxybenzoate
    • Neutrophils
    • Oxidants
    • Superoxide

    ASJC Scopus subject areas

    • Biochemistry

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