A synthetic peptide containing a predominant protein kinase C site within p47phox inhibits the NADPH oxidase in intact neutrophils

Mark E. Labadia, You Li Zu, Chi Kuang Huang

Research output: Contribution to journalArticle

15 Scopus citations

Abstract

In vivo loading of a synthetic peptide (peptide 4) corresponding to residues 314-331 (RSRKRLSQDAYRRNSVRF) consistently diminished the oxidative burst in response to either phorbol 12-myristate 13-acetate (PMA) or formylmethionyl-leucyl-phenylalanine and cytochalasin B (fMLP/CB) compared to other synthetic peptides derived from the p47phox sequence. The effects of peptide 4 were concentration dependent with respect to both PMA and fMLP/CB. In contrast, peptide 4 enhanced the oxidative burst in response to fMLP alone. Peptide 4 inhibited the PMA and fMLP-mediated phosphorylation of endogenous neutrophil cytosolic proteins including p47phox. The PMA-induced translocation of p47phox to the plasma membrane was diminished in neutrophils loaded with peptide 4. These data represent the first report of a synthetic peptide derived from p47phox that inhibits the NADPH oxidase in intact neutrophils and inhibits the protein kinase C-mediated phosphorylation of endogenous p47phox.

Original languageEnglish (US)
Pages (from-to)116-124
Number of pages9
JournalJournal of Leukocyte Biology
Volume59
Issue number1
DOIs
StatePublished - Jan 1996

Keywords

  • Oxidative burst
  • Peptides
  • Phosphorylation
  • Translocation

ASJC Scopus subject areas

  • Cell Biology

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