Activation of phospholipase D in rabbit neutrophils by fMet‐Leu‐Phe is mediated by a pertussis toxin‐sensitive GTP‐binding protein that may be distinct from a phospholipase C‐regulating protein

FEBS Letters

Kanoh, Hiroyuki¹  Kanaho, Yasunori¹  Nozawa, Yoshinori¹ 

[1] Department of Biochemistry, Gifu University School of Medicine, Tsukasamachi-40, Gifu 500, Japan

关键词: Phospholipase D;    Formylmethionylleucylphenylalanine;    N-;    GTP-binding protein;    Pertussis toxin;    Rabbit neutrophil;    PLD;    phospholipase D;    PI-PLC;    phosphoinositide-specific phospholipase C;    PC;    phosphatidylcholine;    PA;    phosphatidic acid;    fMLP;    N-formyl-Met-Leu-Phe;    IAP;    pertussis toxin;    G-protein;    GTP-binding protein;    [3H]lyso PAF;    l-O-[3H]octadecyl lyso platelet-activating factor;    PEt;    phosphatidylethanol;    BSA;    bovine serum albumin;   

DOI  :  10.1016/0014-5793(91)80160-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Stimulation by N-formyl-Met-Leu-Phe (fMLP) of rabbit peritoneal neutrophils, in which phosphatidylcholine was preferentially labeled with l-O-[³H]octadecyl lyso platelet-activating factor, activated phospholipase D, resulting in the formation of [³H]PA from [³H]PC. A direct activator of GTP-binding proteins (G-proteins), NaF, also stimulated [³H]PA formation. fMLP-stimulated [³H]PA formation was inhibited by pertussis toxin (IAP) in a time- and dose-dependent manner. IAP also inhibited fMLP-stimulated IP₃ formation, but the inhibition of IP₃ formation was significantly greater than that of [³H]PA formation. These results indicate that activation of phospholipase D by fMLP in rabbit neutrophils is mediated by an IAP-sensitive G-protein that may be distinct from a phospholipase C-regulating protein.

【 授权许可】

Unknown