FEBS Letters | |
Guanine nucleotides stimulate NADPH oxidase in membranes of human neutrophils | |
Rosenthal, W.1  Schultz, G.1  Seifert, R.1  | |
[1] Institut für Pharmakologie, Freie Universität Berlin, Thielallee 69/73, D-1000 Berlin 33, Germany | |
关键词: Neutrophil; NADPH oxidase; Guanine nucleotide-binding protein; Arachidonic acid; AppNHp; adenylyl imidodiphosphate; ATPγS; adenosine 5'O-(3-thiotriphosphate); FMLP; N-formyl-L-methionyl-L-leucyl-L-phenylalanine; GDPßS; guanosine 5'-O-(2-thiodiphosphate); GppNHp; guanylyl imidodiphosphate; GTPγS; guanosine 5'-O-(3-thiotriphosphate); N-protein; guanine nucleotide-binding protein; PMA; phorbol 12-myristate 13-acetate; | |
DOI : 10.1016/0014-5793(86)80886-9 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
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.
【 授权许可】
Unknown
【 预 览 】
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