| Autor: |
Labadia ME; Department of Pathology, University of Connecticut Health Center, Farmington 06030-3105, USA., Zu YL, Huang CK |
| Jazyk: |
angličtina |
| Zdroj: |
Journal of leukocyte biology [J Leukoc Biol] 1996 Jan; Vol. 59 (1), pp. 116-24. |
| DOI: |
10.1002/jlb.59.1.116 |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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