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Okadaic acid inhibits the signal responsible for activation of the NADPH‐oxidase in neutrophils stimulated with serum‐opsonized yeast
Author(s) -
Harbecke Olle,
Lundqvist Helen,
Dahlgren Claes
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.59.5.754
Subject(s) - phagocytosis , nadph oxidase , opsonin , okadaic acid , zymosan , biology , yeast , oxidase test , respiratory burst , chemotaxis , phosphatase , phagocyte , biochemistry , microbiology and biotechnology , phosphorylation , enzyme , receptor , in vitro
The effects of the phosphatase inhibitor okadaic acid (OA) on human neutrophil phagocytic activity were investigated. The chemiluminescence response was found to be greatly reduced in OA‐treated neutrophils during phagocytosis of serum opsonized yeast particles in comparison to control cells. However, the OA‐treated neutrophils phagocytosed yeast particles to the same extent as control cells and the engulfment of the prey was accompanied by phagolysosomal formation in both OA‐ treated and nontreated cells. We thus found that the OA effect was selective in the sense that it inhibits the NADPH‐oxidase activity in neutrophils phagocytosing yeast particles but not uptake of the prey or phagolysosomal formation. Based on the fact that the NADPH‐oxidase activity induced by the chemoattractant formyl‐methionyl‐leucyl‐phenylalanine was not reduced but elevated in OA‐treated neutrophils, we conclude that the state of phosphorylation has no direct effect on the oxidase, but is of importance for the NADPH‐oxidase activating signal(s) generated during phagocytosis of the yeast particles.