Zeng L, An S, Goetzl E J
Department of Medicine, University of California, San Francisco 94143-0711, USA.
Immunology. 1995 Dec;86(4):620-8.
Co-expression of EP2 and EP3 subtypes of prostaglandin E2 (PGE2) receptors (R) by U937 human monocytic cells permitted comparative studies of desensitization of each subtype. Specific binding of [3H]PGE2 to membranes of U937 cells showed a Kd of 2.9 +/- 0.3 nM (mean +/- SEM) and a Bmax of 40.5 +/- 1.0 fmol/mg protein, and was competitively inhibited by PGE2 > or = PGE1 > PGF2 alpha > PGD2 > PGI2. EP2 R and EP3 R mRNA were detected by reverse transcription-polymerase chain reaction and Northern blots. EP3 R expression was demonstrated by inhibition of [3H]PGE2 binding with the EP1/EP3 agonist sulprostone [50% inhibitory concentration (IC50 = 3.3 +/- 0.6 nM)] and the EP3/EP2 agonist M&B 28767 (IC50 = 2.1 +/- 0.3 nM), but not with the EP1 antagonist SC-19220. EP2 R protein was identified by Western blot analysis using specific rabbit IgG antibodies to an amino-terminal peptide of the EP2 R. EP2 R transduced PGE2 stimulation of significant increases in cellular [cAMP]i [50% effective concentration (EC50 = 20 +/- 2.5 nM)], and EP3 R mediated sulprostone inhibition of forskolin elevation of [cAMP]i (IC50 = 1.3 +/- 0.4 nM). Pretreatment of U937 cells with phorbol 12-myristate 13-acetate (PMA), which activates protein kinase C (PKC), for 1 hr reduced the total number, but not the affinity, of PGE2 R by down-regulating principally EP2 R. In contrast, a 24-hr exposure to PMA, which is known to down-regulate PKC, suppressed both the total number and affinity of PGE2 R on U937 cells with concurrent reductions in EP2 R and EP3 R. The down-regulation of EP2 R by PMA at 1 hr was blocked by staurosporine, an inhibitor of PKC, whereas the down-regulation of EP3 R by PMA at 24 hr was blocked by indomethacin. Pretreatment of U937 cells with PGE2 for 1 and 24 hr reduced both the binding affinity and the total number of PGE2 R, by co-ordinate suppression of the EP2 R and EP3 R. Desensitization of EP2 R and EP3 R for 1 hr with PGE2 suppressed subsequent PGE2-evoked chemokinetic responses to PGE2, whereas selective down-regulation of EP2 R alone by PMA for 1 hr had no effects on U937 cell migration. Thus expression of each subtype of PGE2 R is regulated independently and EP3 R, but not EP2 R, transduces PGE2 effects on migration of mononuclear phagocytes.
人U937单核细胞中前列腺素E2(PGE2)受体(R)的EP2和EP3亚型共表达,这使得对各亚型脱敏作用的比较研究成为可能。[3H]PGE2与U937细胞膜的特异性结合显示,解离常数(Kd)为2.9±0.3 nM(平均值±标准误),最大结合容量(Bmax)为40.5±1.0 fmol/mg蛋白,且PGE2≥PGE1>PGF2α>PGD2>PGI2对其具有竞争性抑制作用。通过逆转录-聚合酶链反应和Northern印迹法检测到了EP2 R和EP3 R的信使核糖核酸(mRNA)。用EP1/EP3激动剂舒前列素[50%抑制浓度(IC50 = 3.3±0.6 nM)]和EP3/EP2激动剂M&B 28767(IC50 = 2.1±0.3 nM)可抑制[3H]PGE2结合,从而证实了EP3 R的表达,但EP1拮抗剂SC-19220则无此作用。使用针对EP2 R氨基末端肽的特异性兔免疫球蛋白G(IgG)抗体,通过蛋白质印迹分析鉴定出了EP2 R蛋白。EP2 R转导PGE2刺激,使细胞内[环磷酸腺苷(cAMP)]i显著增加[50%有效浓度(EC50 = 20±2.5 nM)],而EP3 R介导舒前列素抑制福斯高林引起的[cAMP]i升高(IC50 = 1.3±0.4 nM)。用佛波醇12-肉豆蔻酸酯13-乙酸酯(PMA)预处理U937细胞1小时,PMA可激活蛋白激酶C(PKC),通过主要下调EP2 R来减少PGE2 R的总数,但不影响其亲和力。相比之下,已知PMA可下调PKC,U937细胞暴露于PMA 24小时后,PGE2 R的总数和亲和力均受到抑制,同时EP2 R和EP3 R也减少。1小时时PMA对EP2 R的下调被PKC抑制剂星形孢菌素阻断,而24小时时PMA对EP3 R的下调被吲哚美辛阻断。用PGE2预处理U937细胞1小时和24小时,通过协同抑制EP2 R和EP3 R,可降低PGE2 R的结合亲和力和总数。用PGE2使EP2 R和EP3 R脱敏1小时,可抑制随后PGE2诱发的对PGE2的化学动力学反应,而单独用PMA对EP2 R进行1小时的选择性下调对U937细胞迁移无影响。因此,PGE2 R各亚型的表达是独立调节的,EP3 R而非EP2 R转导PGE2对单核吞噬细胞迁移的作用。