Kucera G L, Rittenhouse S E
Department of Biochemistry, University of Vermont, College of Medicine, Burlington 05405.
Biochem Biophys Res Commun. 1988 May 31;153(1):417-21. doi: 10.1016/s0006-291x(88)81240-3.
The inhibition by guanosine 5'-[beta-thio]diphosphate (GDP beta S) of phospholipase C was compared in intact and saponin-permeabilized human platelets in order to assess whether effects of GDP beta S on phospholipase C activation unrelated to guanine nucleotide binding function were occurring. GDP beta S exhibited no effect on phospholipase C activity, monitored by phosphatidic acid formation, in intact platelets that were unstimulated or stimulated with 0.5 U/ml thrombin or 20 nM ONO-11113 (a stable thromboxane A2 analogue). However, GDP beta S did cause a marked decrease in the activity of phospholipase C in saponin-permeabilized platelets. Thus GDP beta S is a viable tool for studying the role of G-proteins in transducing receptor-mediated activation of phospholipase C in platelets.
为了评估5'-[β-硫代]二磷酸鸟苷（GDPβS）对磷脂酶C的抑制作用是否与鸟嘌呤核苷酸结合功能无关，我们比较了其在完整的和皂角苷通透的人血小板中的作用。在未受刺激、用0.5U/ml凝血酶或20nM ONO-11113（一种稳定的血栓素A2类似物）刺激的完整血小板中，通过磷脂酸形成监测，GDPβS对磷脂酶C活性没有影响。然而，GDPβS确实导致皂角苷通透的血小板中磷脂酶C活性显著降低。因此，GDPβS是研究G蛋白在血小板中传导受体介导的磷脂酶C激活作用的一种可行工具。
