Protein kinase C regulates leukotriene B4 receptors in human neutrophils.
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.
D002462:Cell Membrane / Q000378:metabolism; D004075:Diglycerides / Q000494:pharmacology; D004224:Diterpenes; D004789:Enzyme Activation / Q000187:drug effects; D006801:Humans; D007975:Leukotriene B4 / Q000097:blood; D009504:Neutrophils / Q000378:metabolism*; D011493:Protein Kinase C / Q000097:blood*; D011971:Receptors, Immunologic / Q000187:drug effects / Q000378:metabolism*; D018102:Receptors, Leukotriene B4; D013729:Terpenes / Q000494:pharmacology; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology
D004075:Diglycerides; D004224:Diterpenes; D011971:Receptors, Immunologic; D018102:Receptors, Leukotriene B4; D013729:Terpenes; D007975:Leukotriene B4; C011309:mezerein; C044777:1-O-myristoyl-2-acetyl-glycerol; D011493:Protein Kinase C; D013755:Tetradecanoylphorbol Acetate