Oruch Ramadhan, Hodneland Erlend, Pryme Ian F, Holmsen Holm
Department of Biomedicine, University of Bergen, Bergen, Norway.
Biochim Biophys Acta. 2008 Oct;1778(10):2165-76. doi: 10.1016/j.bbamem.2008.04.007. Epub 2008 Apr 27.
Incubation of platelets with increasing concentrations of thrombin produced large amounts of phosphatidic acid (PA) and distinct changes in phosphatidylinositol-4-phosphate (PIP) and phosphatidylinositol-4,5-bisphosphate (PIP2), prominent metabolites in the polyphosphoinositide (PPI) cycle. The relation between normalized PA and PIP or PIP2 levels in such thrombin-treated platelets from 22 normal donors gave a very similar pattern, suggesting tight control of the metabolites in the polyphosphoinositide (PPI) cycle. Prochlorperazine (PCP), trifluoperazine (TFP), haloperidol (HPD), quetiapine (QTP), pimozide (PMZ) and clozapine (CLO) interfered with this tight coupling produced by treating platelets with increasing thrombin concentrations. All drugs decreased the formation of PA at a given thrombin concentration, a decrease that varied greatly among platelets from different donors. This made it difficult to treat the PIP/PA and PIP2/PA relationships with ordinary, descriptive statistics. The data were therefore subjected to regression analysis using polynomials of second or first degree and gave the interference ranking order: PCP>TFP>>PMZ = HPD>CLO>QTP. All six drugs increased the mean molecular area of monolayers of dipalmitoyl phosphatidylserine on pure water at 37 degrees C by 20-50%, while they had little effect on monolayers of dipalmitoyl phosphatidylcholine. These results suggest that the drugs are membrane-active and may intercalate in biomembranes containing negatively charged phospholipids. Since human platelets do not contain D2 receptors, the interference with the tight coupling of PPI cycle metabolites was not receptor-mediated. We suggest that the drugs are intercalated in the plasma membrane and alter the relative, spatial positioning of phospholipid-consuming enzymes and thereby alter the velocities of the enzyme-catalyzed reactions. Such intercalation could be part of the side effects of the drugs and may explain their psychotropic action(s).
用浓度递增的凝血酶孵育血小板,会产生大量磷脂酸(PA),并使磷脂酰肌醇 - 4 - 磷酸(PIP)和磷脂酰肌醇 - 4,5 - 二磷酸(PIP2)发生明显变化,这两种物质是多磷酸肌醇(PPI)循环中的重要代谢产物。来自22名正常供体的经凝血酶处理的血小板中,标准化的PA与PIP或PIP2水平之间的关系呈现出非常相似的模式,这表明多磷酸肌醇(PPI)循环中的代谢产物受到严格调控。氯丙嗪(PCP)、三氟拉嗪(TFP)、氟哌啶醇(HPD)、喹硫平(QTP)、匹莫齐特(PMZ)和氯氮平(CLO)会干扰因用浓度递增的凝血酶处理血小板而产生的这种紧密耦合。在给定的凝血酶浓度下,所有药物都会降低PA的形成,不同供体的血小板中这种降低程度差异很大。这使得用普通的描述性统计方法来处理PIP/PA和PIP2/PA的关系变得困难。因此,对数据进行了二次或一次多项式回归分析,得出干扰排序为:PCP>TFP>>PMZ = HPD>CLO>QTP。所有这六种药物都使37℃纯水上二棕榈酰磷脂酰丝氨酸单层的平均分子面积增加了20 - 50%,而它们对二棕榈酰磷脂酰胆碱单层的影响很小。这些结果表明,这些药物具有膜活性,可能会插入含有带负电荷磷脂的生物膜中。由于人类血小板不含D2受体,对PPI循环代谢产物紧密耦合的干扰不是受体介导的。我们认为,这些药物插入质膜并改变了消耗磷脂的酶的相对空间定位,从而改变了酶催化反应的速度。这种插入可能是药物副作用的一部分,并且可能解释了它们的精神otropic作用。