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The Journal of Experimental Biology 206, 2759-2769 (2003)
doi: 10.1242/jeb.00483

Oxidative stress stimulates multiple MAPK signalling pathways and phosphorylation of the small HSP27 in the perfused amphibian heart

Catherine Gaitanaki, Stathopoulou Konstantina, Stavridou Chrysa and Isidoros Beis^*

Department of Animal and Human Physiology, School of Biology, Faculty of Sciences, University of Athens, Panepistimioupolis, Athens 157 84, Greece

^* Author for correspondence (e-mail: ibeis{at}biol.uoa.gr)

Accepted 12 May 2003

We investigated the activation of three subfamilies of MAPKs (ERK, JNKs and p38-MAPK) by oxidative stress in the isolated perfused amphibian heart. Activation of p43-ERK by 100 µmol l^-1 H₂O₂ was maximally observed within 5 min, remained elevated for 30 min and was comparable with the effect of 1 µmol l^-1 PMA. p43-ERK activation by H₂O₂ was inhibited by PD98059 but not by SB203580. The p46 and p52 species of JNKs were maximally activated by 2.5- and 2.1-fold, respectively, by 100 µmol l^-1 H₂O₂ within 2 min. JNK activation was still detectable after 15 min, reaching control values at 30 min of treatment. p38-MAPK was maximally activated by 9.75-fold by 100 µmol l^-1 H₂O₂ after 2 min and this activation progressively declined thereafter, reaching control values within 45 min of treatment. The observed dose-dependent profile of p38-MAPK activation by H₂O₂ revealed that 30 µmol l^-1 H₂O₂ induced maximal phosphorylation, whereas 100–300 µmol l^-1 H₂O₂ induced considerable activation of the kinase. Our studies also showed that the phosphorylation of MAPKAPK2 by H₂O₂ followed a parallel time-dependent pattern and that SB203580 abolished this phosphorylation. Furthermore, our experiments clearly showed that 30 µmol l^-1 H₂O₂ induced a strong, specific phosphorylation of HSP27. Our immunohistochemical studies showed that immune complexes of phosphorylated forms of both p38-MAPK and HSP27 were strongly enhanced by 30 µmol l^-1 H₂O₂ in the perinuclear region as well as dispersedly in the cytoplasm of ventricular cells and that SB203580 abolished this phosphorylation. These data indicate that oxidative stress is a powerful activator of all three MAPK subfamilies in the amphibian heart. Stimulation of p38-MAPK and the consequent phosphorylation of HSP27 may be important in cardioprotection under such conditions.

Key words: oxidative stress, amphibian heart, MAPK, p38-MAPK, HSP27, signal transduction, Rana ridibunda

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