A synthetic peptide containing a predominant protein kinase C site within p47phox inhibits the NADPH oxidase in intact neutrophils. Academic Article uri icon

Overview

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.

publication date

  • January 1, 1996

Research

keywords

  • Enzyme Inhibitors
  • NADH, NADPH Oxidoreductases
  • NADPH Dehydrogenase
  • Neutrophils
  • Peptide Fragments
  • Phosphoproteins
  • Protein Kinase C

Identity

Scopus Document Identifier

  • 0030056857

Digital Object Identifier (DOI)

  • 10.1002/jlb.59.1.116

PubMed ID

  • 8558059

Additional Document Info

volume

  • 59

issue

  • 1