O'Flaherty J T, Redman J F, Jacobson D P
FEBS Lett. 1986 Oct 6;206(2):279-82. doi: 10.1016/0014-5793(86)80996-6.
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.
三种蛋白激酶C（PKC）激活剂，即佛波醇肉豆蔻酸酯乙酸盐、卫矛醇和rac-1-O-肉豆蔻酰-2-乙酰甘油，通过减少花生四烯酸代谢物可利用的高亲和力受体数量，抑制人中性粒细胞对[3H]白三烯B4（LTB4）的结合。这种抑制作用在全细胞和胞质体中出现，但在分离的膜中未出现；它似乎涉及PKC的激活，而不是对结合位点的直接竞争。PKC可能通过调节内源性介质如LTB4的受体相关生物作用来控制细胞反应性。
