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The antimicrobial peptide parabutoporin competes with p47 phox as a PKC‐substrate and inhibits NADPH oxidase in human neutrophils
Author(s) -
Remijsen Quinten F.M.,
Fontayne Alexandre,
Verdonck Fons,
Clynen Elke,
Schoofs Liliane,
Willems Jean
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.10.024
Subject(s) - nadph oxidase , protein kinase c , peptide , substrate (aquarium) , antimicrobial , chemistry , biochemistry , enzyme , biology , organic chemistry , ecology
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‐α, ‐βI, ‐βII and ‐δ, but not PKC‐ζ. 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.