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A synthetic peptide containing a predominant protein kinase C site within p47 phox inhibits the NADPH oxidase in intact neutrophils
Author(s) -
Labadia Mark E.,
Zu YouLi,
Huang ChiKuang
Publication year - 1996
Publication title -
journal of leukocyte biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.819
H-Index - 191
eISSN - 1938-3673
pISSN - 0741-5400
DOI - 10.1002/jlb.59.1.116
Subject(s) - peptide , nadph oxidase , respiratory burst , cytochalasin b , protein kinase c , biochemistry , n formylmethionine leucyl phenylalanine , phosphorylation , phorbol , biology , oxidative phosphorylation , protein kinase a , in vitro , neutrophile , enzyme
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 p47 phox 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 p47 phox . The PMA‐induced translocation of p47 phox to the plasma membrane was diminished in neutrophils loaded with peptide 4. These data represent the first report of a synthetic peptide derived from p47 phox that inhibits the NADPH oxidase in intact neutrophils and inhibits the protein kinase C–mediated phosphorylation of endogenous p47 phox .