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Guanine nucleotides stimulate NADPH oxidase in membranes of human neutrophils

Item Type:Article
Title:Guanine nucleotides stimulate NADPH oxidase in membranes of human neutrophils
Creators Name:Seifert, R. and Rosenthal, W. and Schultz, G.
Abstract: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 GTP gamma S and GppNHp, which all activate N-proteins, enhanced NADPH oxidase activity up to 4-fold. GDP beta S inhibited the effect of GTP gamma S. These data suggest that NADPH oxidase is regulated by an N-protein, independent of an elevation of the cytoplasmic calcium concentration.
Keywords:Neutrophil, NADPH Oxidase, Guanine Nucleotide-Binding Protein, Arachidonic Acid
Source:FEBS Letters
ISSN:0014-5793
Publisher:Elsevier (The Netherlands)
Volume:205
Number:1
Page Range:161-165
Date:1986
Official Publication:https://doi.org/10.1016/0014-5793(86)80886-9
PubMed:View item in PubMed

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