Adie E J, Mullaney I, McKenzie F R, Milligan G
Department of Biochemistry, University of Glasgow, Scotland, U.K.
Biochem J. 1992 Jul 15;285 ( Pt 2)(Pt 2):529-36. doi: 10.1042/bj2850529.
Neuroblastoma x glioma hybrid NG108-15 cells express a high-affinity IP prostanoid receptor. Saturation binding analysis of this receptor, using [3H]prostaglandin E1 ([3H]PGE1) as ligand, indicated that it was present at some 1.5 pmol/mg of membrane protein and displayed a dissociation constant for this ligand of 30-40 nM. Prolonged exposure of these cells either to PGE1 or to iloprost, which is a stable analogue of prostacyclin, caused a 40-70% decrease in levels of the receptor. The remaining receptors were capable of interacting with the stimulatory G-protein (Gs) of the adenylate cyclase cascade, as saturation analysis of the binding of [3H]PGE1 indicated that they had a similar affinity for the 3H-labelled ligand, and because the specific binding of [3H]PGE1 to these receptors was still sensitive to the presence of poorly hydrolysed analogues of GTP. We have recently demonstrated that prolonged exposure of NG108-15 ells to PGE1 causes a cyclic AMP-independent loss of Gs alpha-subunit (Gs alpha) from these cells [McKenzie & Milligan (1990) J. Biol. Chem. 265, 17084-17093]. Steady-state concentration of the larger 45 kDa form of Gs alpha (which is the predominant form expressed in these cells) was assessed to be 9.6 pmol/mg of membrane protein, and treatment with iloprost decreased levels of this polypeptide to some 3.0 pmol/mg of protein. Time courses of iloprost-mediated down-regulation of the IP prostanoid receptor, loss of Gs alpha protein as assessed by immunoblotting and loss of Gs alpha activity as assessed by the reconstitution of NaF stimulation of adenylate cyclase activity to membranes of S49 cyc- cells by sodium cholate extracts of NG108-15 cells were identical, suggesting that the loss of the IP prostanoid receptor and G-protein occurred in parallel. Each of these effects was half-maximal between 2 and 3 h of exposure to the agonist. Stoichiometry of loss of Gs alpha and IP prostanoid receptor was unchanged by the percentage receptor occupancy, and quantification indicated the loss of some 7-10 mol of Gs alpha/mol of receptor. This is the first report to demonstrate the temporal concurrence of loss of Gs alpha and of a receptor which interacts with this G-protein. Chronic activation of the IP prostanoid receptor on these cells results in the development of a heterologous form of desensitization to agents which function to activate adenylate cyclase [Kelly, Keen, Nobbs & MacDermot (1990) Br. J. Pharmacol. 99, 306-316]. Agonist regulation of Gs alpha levels in these cells may contribute to this process.
神经母细胞瘤 - 胶质瘤杂交细胞NG108 - 15表达一种高亲和力的前列环素受体。以[³H]前列腺素E1([³H]PGE1)为配体对该受体进行饱和结合分析表明,其在膜蛋白中的含量约为1.5 pmol/mg,对该配体的解离常数为30 - 40 nM。将这些细胞长时间暴露于PGE1或依洛前列素(前列环素的一种稳定类似物)会导致受体水平降低40 - 70%。剩余的受体能够与腺苷酸环化酶级联反应的刺激性G蛋白(Gs)相互作用,因为对[³H]PGE1结合的饱和分析表明它们对³H标记的配体具有相似的亲和力,并且因为[³H]PGE1与这些受体的特异性结合仍然对水解不良的GTP类似物的存在敏感。我们最近证明,将NG108 - 15细胞长时间暴露于PGE1会导致这些细胞中Gsα亚基(Gsα)出现不依赖于环磷酸腺苷的丢失[麦肯齐和米利根(1990年)《生物化学杂志》265卷,17084 - 17093页]。评估较大的45 kDa形式的Gsα(这是这些细胞中表达的主要形式)的稳态浓度为9.6 pmol/mg膜蛋白,用依洛前列素处理会使该多肽水平降至约3.0 pmol/mg蛋白。通过免疫印迹评估依洛前列素介导的IP前列环素受体下调、Gsα蛋白丢失以及通过用NG108 - 15细胞的胆酸钠提取物将NaF刺激腺苷酸环化酶活性重建到S49 cyc - 细胞的膜上来评估Gsα活性丢失的时间进程是相同的,这表明IP前列环素受体和G蛋白的丢失是并行发生的。这些效应在暴露于激动剂2至3小时之间达到半数最大效应。Gsα和IP前列环素受体丢失的化学计量关系不受受体占有率百分比的影响,定量分析表明每摩尔受体丢失约7 - 10摩尔的Gsα。这是第一份证明Gsα丢失与与该G蛋白相互作用的受体丢失在时间上同时发生的报告。这些细胞上IP前列环素受体的慢性激活导致对激活腺苷酸环化酶的药物产生一种异源脱敏形式[凯利、基恩、诺布斯和麦克德莫特(1990年)《英国药理学杂志》99卷,306 - 316页]。激动剂对这些细胞中Gsα水平的调节可能促成了这一过程。