Activation of mitogen‐activated protein kinases (p38‐MAPKs, SAPKs/JNKs and ERKs) by adenosine in the perfused rat heart

FEBS Letters

Clerk, Angela¹  Sugden, Peter H.²  Haq, Syed E.A.² 

[1] Division of Biomedical Sciences (Molecular Pathology), Imperial College School of Medicine, Exhibition Road, London SW6 2LZ, UK;NHLI Division (Cardiac Medicine), Imperial College School of Medicine, Dovehouse Street, London SW3 6LY, UK

关键词: Heart;    Adenosine;    Mitogen-activated protein kinase;    Ado;    adenosine;    ERK;    extracellularly responsive kinase;    FPLC;    fast protein liquid chromatography;    JNK;    c-Jun N-terminal kinase;    MAPK;    mitogen-activated protein kinase;    MAPKAPK2;    MAPK-activated protein kinase 2;    PMA;    phorbol 12-myristate 13-acetate;    SAPK;    stress-activated protein kinase;   

DOI  :  10.1016/S0014-5793(98)01000-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 μM 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.

【 授权许可】

Unknown