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Guanine nucleotides stimulate NADPH oxidase in membranes of human neutrophils
Author(s) -
Seifert R.,
Rosenthal W.,
Schultz G.
Publication year - 1986
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 - 10.1016/0014-5793(86)80886-9
Subject(s) - nadph oxidase , gtp' , superoxide , biochemistry , chemistry , pertussis toxin , cytosol , intracellular , oxidase test , g protein , gtp binding protein regulators , arachidonic acid , microbiology and biotechnology , biology , enzyme , receptor
In the chain of events by which chemotactic peptides stimulate NADPH oxidase‐catalyzed Superoxide formation in human neutrophils, the involvements of a pertussis toxin‐sensitive guanine nucleotide‐binding protein (N‐protein), mobilization of intracellular calcium and protein kinase C stimulation have been proposed. Superoxide formation was studied in membranes from human neutrophils; NADPH oxidase was stimulated by arachidonic acid in the presence of neutrophil cytosol. Fluoride and stable GTP analogues, such as GTPγS and GppNHp, which all activate N‐proteins, enhanced NADPH oxidase activity up to 4‐fold. GDPßS inhibited the effect of GTPγS. These data suggest that NADPH oxidase is regulated by an N‐protein, independent of an elevation of the cytoplasmic calcium concentration.