Guanine nucleotides stimulate NADPH oxidase in membranes of human neutrophils

FEBS Letters

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