Meade C J, Turner G A, Bateman P E
Biochem J. 1986 Sep 1;238(2):425-36. doi: 10.1042/bj2380425.
Stimulation of rabbit polymorphonuclear leucocytes with A23187 causes phospholipase C mediated breakdown of polyphosphoinositides, as evidenced by accumulation of [3H]inositol-labelled inositol bisphosphate and inositol trisphosphate. At the same time the polyphosphoinositides and the products of their breakdown, diacylglycerol and phosphatidic acid, label rapidly with radioactive arachidonic acid. Enhancement of polyphosphoinositide labelling is not as great as enhancement of diacylglycerol or phosphatidic acid labelling, suggesting additional early activation of a second independent synthetic pathway to the last named lipids. Experiments using double (3H/14C) labelling, to distinguish pools with different rates of turnover, suggest the major pool of arachidonic acid used for synthesis of lipoxygenase metabolites turns over more slowly than arachidonic acid in diacylglycerol, but at about the same rate as arachidonic acid esterified in phosphatidylcholine or phosphatidylinositol. Further, when cells are prelabelled with [14C]arachidonic acid, then stimulated for 5 min, it is only from phosphatidylcholine, and to a lesser extent phosphatidylinositol, that radiolabel is lost. Release of arachidonic acid is probably via phospholipase A2, since it is blocked by the phospholipase A2 inhibitor manoalide. The absence of accumulated lysophosphatides can be explained by reacylation and, in the case of lysophosphatidylinositol, deacylation. The importance of phospholipase A2 in phosphatidylinositol breakdown contrasts with the major role of phospholipase C in polyphosphoinositide hydrolysis. Measurements of absolute free fatty acid levels, as well as studies showing a correlation between production of radiolabelled hydroxyeicosatetraenoic acids and release of radiolabel from the phospholipid pool, both suggest that hydrolysis of arachidonic acid esterified into phospholipids is the limiting factor regulating formation of lipoxygenase metabolites. By contrast with A23187, fMet-Leu-Phe (a widely used polymorphonuclear leucocyte activator) is a poor stimulant for arachidonic acid release unless a 'second signal' (e.g. cytochalasin B, or a product of A23187-stimulated cells) is also present. In the presence of cytochalasin B, fMet-Leu-Phe, like A23187, stimulates release of radiolabelled arachidonic acid principally from phosphatidylcholine.
用A23187刺激兔多形核白细胞会导致磷脂酶C介导的多磷酸肌醇分解,这可通过[3H]肌醇标记的肌醇二磷酸和肌醇三磷酸的积累来证明。与此同时,多磷酸肌醇及其分解产物二酰甘油和磷脂酸会迅速被放射性花生四烯酸标记。多磷酸肌醇标记的增强不如二酰甘油或磷脂酸标记的增强显著,这表明存在另一条独立的合成途径,该途径在早期被额外激活,用于合成后一种脂质。使用双(3H/14C)标记来区分周转率不同的池的实验表明,用于合成脂氧合酶代谢物的花生四烯酸的主要池的周转率比二酰甘油中的花生四烯酸慢,但与磷脂酰胆碱或磷脂酰肌醇中酯化的花生四烯酸的周转率大致相同。此外,当细胞用[14C]花生四烯酸预标记,然后刺激5分钟时,只有磷脂酰胆碱会丢失放射性标记,磷脂酰肌醇丢失的程度较小。花生四烯酸的释放可能是通过磷脂酶A2,因为它被磷脂酶A2抑制剂 manoalide阻断。没有积累溶血磷脂可以通过再酰化来解释,对于溶血磷脂酰肌醇来说,则是通过脱酰化来解释。磷脂酶A2在磷脂酰肌醇分解中的重要性与磷脂酶C在多磷酸肌醇水解中的主要作用形成对比。对绝对游离脂肪酸水平的测量,以及显示放射性标记的羟基二十碳四烯酸的产生与磷脂池中的放射性标记释放之间存在相关性的研究,都表明酯化到磷脂中的花生四烯酸的水解是调节脂氧合酶代谢物形成的限制因素。与A23187不同,除非存在“第二信号”(例如细胞松弛素B或A23187刺激细胞的产物),否则fMet-Leu-Phe(一种广泛使用的多形核白细胞激活剂)对花生四烯酸释放的刺激作用较差。在细胞松弛素B存在的情况下,fMet-Leu-Phe与A23187一样,主要刺激放射性标记的花生四烯酸从磷脂酰胆碱中释放。