Title: The antimicrobial peptide parabutoporin competes with p47(phox) as a PKC-substrate and inhibits NADPH oxidase in human neutrophils
Authors: Remijsen, Quinten
Fontayne, Alexandre
Verdonck, Alfons
Clynen, Elke
Schoofs, Liliane
Willems, Jean # ×
Issue Date: Nov-2006
Publisher: Elsevier on behalf of the Federation of European Biochemical Societies
Series Title: FEBS Letters vol:580 issue:26 pages:6206-6210
Abstract: We investigated parabutoporin (PP), an antimicrobial scorpion peptide, to understand its inhibition on NADPH oxidase in human PMN. We show that PP is a good substrate for all PKC-isotypes, implicated in the activation of NADPH oxidase, and acts as a potent competitive inhibitor of in vitro p47(phox)-phosphorylation by PKC-alpha, -beta I, -beta II and -delta, but not PKC-sigma. In PMN, PP also inhibits the PMA-stimulated phosphorylation of p47(phox) and its subsequent translocation. In contrast, PP affects the PKC-independent activation to a much lesser degree. This indicates that PP inhibits the activation of NADPH oxidase at submicromolar concentrations in a strongly PKC-dependent manner. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
ISSN: 0014-5793
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Interdisciplinary Research Facility Life Sciences, Campus Kulak Kortrijk
Faculty of Medicine - miscellaneous
Faculty of Medicine, Campus Kulak Kortrijk
Animal Physiology and Neurobiology Section - miscellaneous
Microbiology and Immunology, Campus Kulak Kortrijk
Department of Microbiology & Immunology - miscellaneous
× corresponding author
# (joint) last author

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