Breton M, Wolf C, Colard O
Biochem Biophys Res Commun. 1983 Dec 28;117(3):809-16. doi: 10.1016/0006-291x(83)91669-8.
Plasma membrane phospholipids were modified by incubation in the presence of linoleyl-CoA with or without added lysolecithin (LPC) for various length of time. In the absence of LPC, a maximum of 10 nmoles linoleyl-phosphatidylcholine (PC) were synthesized and the ATPase specific activities were not affected whereas in the presence of LPC, when linoleyl-PC synthesis rose from 10 to 80 nmoles, the ATPase activities were decreased. The decrease was similar in the Na,K- or in the Mg-dependent-ATPase and reached maximally 30-40%. LPC by itself did not modify the ATPases. A concomitant decrease in DPH polarization was observed when linoleate was incorporated into phospholipids. We concluded that the decreased ATPase specific activities may be due to an increased fluidity of membranes produced by linoleyl- PC synthesis. We compare this modulation of ATPases by the membrane fluidity with the specific effect of linoleyl- PC species on adenylate cyclase.
通过在亚油酰辅酶A存在的情况下孵育,添加或不添加溶血卵磷脂(LPC),并持续不同时长,来修饰质膜磷脂。在没有LPC的情况下,最多合成了10纳摩尔的亚油酰磷脂酰胆碱(PC),且ATP酶的比活性不受影响;而在有LPC存在的情况下,当亚油酰PC的合成量从10纳摩尔增加到80纳摩尔时,ATP酶的活性降低。在钠钾ATP酶或镁依赖性ATP酶中,这种降低情况相似,最大降幅达30%-40%。LPC本身不会改变ATP酶。当亚油酸酯掺入磷脂中时,观察到DPH极化同时降低。我们得出结论,ATP酶比活性的降低可能是由于亚油酰PC合成导致膜流动性增加所致。我们将膜流动性对ATP酶的这种调节作用与亚油酰PC种类对腺苷酸环化酶的特定作用进行了比较。