Haq S E, Clerk A, Sugden P H
NHLI Division (Cardiac Medicine), Imperial College School of Medicine, London, UK.
FEBS Lett. 1998 Sep 4;434(3):305-8. doi: 10.1016/s0014-5793(98)01000-x.
Adenosine and mitogen-activated protein kinases (MAPKs) have been separately implicated in cardiac ischaemic preconditioning. We investigated the activation of MAPK subfamilies by adenosine in perfused rat hearts. p38-MAPK was rapidly phosphorylated and activated (10-fold activation, maximal at 5 min) by 10 mM adenosine, as was the p38-MAPK substrate, MAPKAPK2 (4.5-fold). SAPKs/JNKs were activated (5-fold) and ERKs were phosphorylated (both maximal at 5 min). The concentration dependences of activation of p38-MAPK and ERKs were biphasic with a 'high affinity' component (maximal at 10-100 microM adenosine) and a 'low affinity' component that had not saturated at 10 mM. SAPKs/JNKs were activated only by 10 mM adenosine. These results are consistent with MAPK involvement in adenosine-mediated ischaemic preconditioning.
腺苷和丝裂原活化蛋白激酶（MAPKs）分别与心脏缺血预处理有关。我们研究了灌注大鼠心脏中腺苷对MAPK亚家族的激活作用。10 mM腺苷可使p38-MAPK迅速磷酸化并激活（激活10倍，5分钟时达到最大值），p38-MAPK底物MAPKAPK2也是如此（激活4.5倍）。应激激活蛋白激酶/应激活化蛋白激酶（SAPKs/JNKs）被激活（激活5倍），细胞外信号调节激酶（ERKs）发生磷酸化（两者均在5分钟时达到最大值）。p38-MAPK和ERKs激活的浓度依赖性呈双相，具有一个“高亲和力”组分（在10 - 100 microM腺苷时达到最大值）和一个在10 mM时未饱和的“低亲和力”组分。SAPKs/JNKs仅被10 mM腺苷激活。这些结果与MAPK参与腺苷介导的缺血预处理一致。
