Superoxide production in human neutrophils: Evidence for signal redundancy and the involvement of move than one PKC isoenzyme class

Judit Pongracz, Janet M. Lord

Research output: Contribution to journalArticle

36 Citations (Scopus)


Selective protein kinase C (PKC) activators and inhibitors and a physiological agonist, fMLP, were used to study superoxide production and PKC isoenzyme activation in human neutrophils. The data show that the classical PKC isoenzymes, α and β, were activated by TPA and at a time prior to NADPH oxidase complex assembly. fMLP induced activation of PKC-β over a similar time course. Inhibition of c-PKCs reduced, but did not block, TPA-induced superoxide production completely, suggesting additional PKC isoenzymes were involved beyond NADPH oxidase assembly. PKC inhibitors were unable to inhibit fMLP-induced superoxide generation, indicative of signal redundancy in the induction of superoxide generation in human neutrophils.

Original languageEnglish
Pages (from-to)624-629
Number of pages6
JournalBiochemical and biophysical research communications
Issue number3
Publication statusPublished - Jun 29 1998


ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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