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Activation of mitogen‐activated protein kinases (p38‐MAPKs, SAPKs/JNKs and ERKs) by adenosine in the perfused rat heart
Author(s) -
Haq Syed E.A.,
Clerk Angela,
Sugden Peter H.
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)01000-x
Subject(s) - adenosine , p38 mitogen activated protein kinases , mapk/erk pathway , kinase , protein kinase a , phosphorylation , chemistry , mitogen activated protein kinase , microbiology and biotechnology , adenosine kinase , biology , biochemistry , adenosine deaminase
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.