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DDT(1)MF-2细胞中A(1)-腺苷受体对蛋白激酶B的激活作用。

Activation of protein kinase B by the A(1)-adenosine receptor in DDT(1)MF-2 cells.

作者信息

Germack R, Dickenson J M

机构信息

Department of Life Sciences, Nottingham Trent University, Clifton Lane, Nottingham, NG11 8NS.

出版信息

Br J Pharmacol. 2000 Jun;130(4):867-74. doi: 10.1038/sj.bjp.0703396.

Abstract

In this study the effect of insulin and A(1)-adenosine receptor stimulation on protein kinase B (PKB) activation has been investigated in the hamster vas deferens smooth muscle cell line DDT(1)MF-2. Increases in PKB phosphorylation were determined by Western blotting using an antibody that detects PKB phosphorylation at Ser(473). Insulin, a recognized activator of PKB, stimulated a concentration-dependent increase in PKB phosphorylation in DDT(1)MF-2 cells (EC(50) 5+/-1 pM). The selective A(1)-adenosine receptor agonist N(6)-cyclopentyladenosine (CPA) stimulated time and concentration-dependent increases in PKB phosphorylation in DDT(1)MF-2 cells (EC(50) 1.3+/-0.5 nM). CPA-mediated increases in PKB phosphorylation were antagonized by the A(1)-adenosine receptor selective antagonist 1,3-dipropylcyclopentylxanthine (DPCPX) yielding an apparent K(D) value of 2.3 nM. Pre-treatment of DDT(1)MF-2 cells with pertussis toxin (PTX, 100 ng ml(-1) for 16 h), to block G(i)/G(o)-dependent pathways, abolished CPA (1 microM) induced phosphorylation of PKB. In contrast, responses to insulin (100 nM) were resistant to PTX pre-treatment. The phosphatidylinositol 3-kinase (PI-3K) inhibitors wortmannin (IC(50) 10.3+/-0.6 nM) and LY 294002 (IC(50) 10.3+/-1.2 microM) attenuated the phosphorylation of PKB elicited by CPA (1 microM) in a concentration-dependent manner. Wortmannin (30 nM) and LY 294002 (30 microM) also blocked responses to insulin (100 nM). Removal of extracellular Ca(2+) and chelation of intracellular Ca(2+) with BAPTA had no significant effect on CPA-induced PKB phosphorylation. Similarly, pretreatment (30 min) with inhibitors of protein kinase C (Ro 31-8220; 10 microM), tyrosine kinase (genistein; 100 microM), mitogen-activated protein (MAP) kinase kinase (PD 98059; 50 microM) and p38 MAPK (SB 203580; 20 microM) had no significant effect on CPA-induced PKB phosphorylation. In conclusion, these data demonstrate that A(1)-adenosine receptor stimulation in DDT(1)MF-2 cells increases PKB phosphorylation through a PTX and PI-3K-sensitive pathway.

摘要

在本研究中,已在仓鼠输精管平滑肌细胞系DDT(1)MF-2中研究了胰岛素和A(1)-腺苷受体刺激对蛋白激酶B(PKB)激活的影响。使用检测Ser(473)处PKB磷酸化的抗体,通过蛋白质印迹法测定PKB磷酸化的增加。胰岛素是公认的PKB激活剂,可刺激DDT(1)MF-2细胞中PKB磷酸化呈浓度依赖性增加(半数有效浓度(EC(50))为5±1 pM)。选择性A(1)-腺苷受体激动剂N(6)-环戊基腺苷(CPA)可刺激DDT(1)MF-2细胞中PKB磷酸化呈时间和浓度依赖性增加(EC(50)为1.3±0.5 nM)。CPA介导的PKB磷酸化增加被A(1)-腺苷受体选择性拮抗剂1,3-二丙基环戊基黄嘌呤(DPCPX)拮抗,产生的表观解离常数(K(D))值为2.3 nM。用百日咳毒素(PTX,100 ng/ml,处理16小时)预处理DDT(1)MF-2细胞以阻断G(i)/G(o)依赖性途径,可消除CPA(1 μM)诱导的PKB磷酸化。相反,对胰岛素(100 nM)的反应对PTX预处理具有抗性。磷脂酰肌醇3-激酶(PI-3K)抑制剂渥曼青霉素(IC(50)为10.3±0.6 nM)和LY 294002(IC(50)为10.3±1.2 μM)以浓度依赖性方式减弱了CPA(1 μM)引起的PKB磷酸化。渥曼青霉素(30 nM)和LY 294002(30 μM)也阻断了对胰岛素(100 nM)的反应。去除细胞外Ca(2+)并用BAPTA螯合细胞内Ca(2+)对CPA诱导的PKB磷酸化无显著影响。同样,用蛋白激酶C抑制剂(Ro 31-8220;10 μM)、酪氨酸激酶抑制剂(染料木黄酮;100 μM)、丝裂原活化蛋白(MAP)激酶激酶抑制剂(PD 98059;50 μM)和p38 MAPK抑制剂(SB 203580;20 μM)预处理(30分钟)对CPA诱导的PKB磷酸化无显著影响。总之,这些数据表明,DDT(1)MF-2细胞中A(1)-腺苷受体刺激通过PTX和PI-敏感性途径增加PKB磷酸化。

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