Protein kinase C regulates leukotriene B4 receptors in human neutrophils

FEBS Letters

Redman, Jimmy F.¹  Jacobson, David P.¹  O'Flaherty, Joseph T.¹ 

[1] Department of Medicine, Wake Forest University Medical Center, 300 South Hawthorne Road, Winston-Salem, NC 27103, USA

关键词: (Polymorphonuclear leukocyte);    Protein kinase C;    Leukotriene B4 receptor;    PMN;    polymorphonuclear neutrophils;    PKC;    protein kinase C;    SOD;    Superoxide dismutase;    LTB4;    leukotriene B4;    PMA;    phorbol myristate acetate;    MEZ;    mezerein;    MAG;    rac-1-O-myristoyl-2-acetylglycerol;    HEG;    1-O-hexadecyl-2-ethylglycerol;    ETYA;    eicosatetraynoic acid;    BSA;    bovine serum albumin;    DMSO;    dimethyl sulfoxide;   

DOI  :  10.1016/0014-5793(86)80996-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Three protein kinase C (PKC) activators, viz. phorbol myristate acetate, mezerein, and rac-1-O-myristoyl-2-acetylglycerol, inhibited human neutrophil binding of [³H] leukotriene B₄ (LTB₄) by reducing the number of high-affinity receptors available to the arachidonic acid metabolite. The inhibitory effect occurred in whole cells and cytoplasts but not in isolated membranes; it appeared to involve the activation of PKC rather than direct competition for binding sites. PKC may govern cellular responsiveness by regulating the receptor-linked bioactions of endogenous mediators like LTB₄.

【 授权许可】

Unknown