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1- and ß-adrenoceptor stimulation differentially activate p38-MAPK and atrial natriuretic peptide production in the perfused amphibian heart
1 Department of Animal and Human Physiology, School of Biology, Faculty of
Sciences, University of Athens, Panepistimioupolis, Athens, Greece 157
84
2 Laboratory of Animal Physiology, Department of Zoology, School of Biology,
Aristotle University of Thessaloniki, Thessaloniki, Greece 54 006
* Author for correspondence (e-mail: ibeis{at}biol.uoa.gr )
Accepted 15 May 2002
We investigated the activation of p38-MAPK by various adrenergic agents in
the perfused Rana ridibunda heart. Phenylephrine (50 µmol
l-1) rapidly induced the differential activation of all three
mitogen-activated protein kinase (MAPK) subfamilies (ERK, JNKs and p38-MAPK)
in this experimental system. Focusing on p38-MAPK response to phenylephrine,
we found that the kinase phosphorylation reached maximal values at 30 s,
declining thereafter to basal values at 15 min. p38-MAPK activation by
phenylephrine was verified as exclusively 
1-AR-mediated.
Furthermore, SB203580 (1 µmol l-1) abolished the kinase
phosphorylation by phenylephrine. Isoproterenol (50 µmol l-1)
was also shown to activate p38-MAPK in a time- and temperature-dependent
manner. A marked, sustained p38-MAPK activation profile was observed at
25°C, while at 18°C the kinase response to isoproterenol was modest.
Isoproterenol effect on p38-MAPK stimulation was ß-AR-mediated.
Immunohistochemical studies revealed the enhanced presence of phosphorylated
p38-MAPK and atrial natriuretic peptide (ANP) in both phenylephrine- and
isoproterenol-stimulated hearts, a reaction completely blocked by the
respective specific antagonists, or the specific p38-MAPK inhibitor SB203580.
These findings indicate a functional correlation between p38-MAPK activation
and ANP accumulation in the perfused amphibian heart.
Key words: p38-MAPK, adrenoceptor, amphibian heart, atrial natriuretic peptide, adrenergic agonist, Rana ridibunda
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