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  • Title: A synthetic peptide containing a predominant protein kinase C site within p47phox inhibits the NADPH oxidase in intact neutrophils.
    Author: Labadia ME, Zu YL, Huang CK.
    Journal: J Leukoc Biol; 1996 Jan; 59(1):116-24. PubMed ID: 8558059.
    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.
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