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Vol. 58, Issue 3, 477-482, September 2000
Karolinska Institutet, Department of Physiology and Pharmacology,
Section of Molecular Neuropharmacology, Stockholm, Sweden
The known diverse effects of adenosine on mitogenesis may be related to
changes in mitogen-activated protein kinases. In this study we
therefore compared the phosphorylation of extracellular-regulated kinase 1/2 (ERK1/2) via the four known human adenosine receptors A1, A2A, A2B, and A3,
stably transfected into Chinese hamster ovary (CHO) cells. The
adenosine analog 5'-N-ethylcarboxamidoadenosine (NECA),
known to act on all subtypes, had no effect on untransfected CHO cells,
but did cause a substantial time- and dose-dependent phosphorylation in
CHO cells transfected with each of the receptors. The maximal
phosphorylation was highest in A1 and A3
receptor-transfected cells, intermediate in A2A and low in
A2B receptor-expressing CHO cells. For all receptors the
half-maximal ERK1/2 phosphorylation was observed at 19-115 nM NECA.
NECA acting on adenosine A2B receptors was much more potent
in stimulating ERK1/2 phosphorylation (EC50 = 19 nM)
than cAMP formation (EC50 = 1.4 µM). Stimulation
with the endogenous ligand adenosine resulted in the same pattern of ERK1/2 phosphorylation as NECA. Concentrations of adenosine that occur
physiologically caused an increased phosphorylation after 5 min in CHO
cells transfected with any one of the four adenosine receptors.
Adenosine at levels reached during ischemia (3 µM) induced a more
pronounced, but still transient, activation of ERK1/2. In conclusion,
this study shows that all the human adenosine receptors transfected
into CHO cells are able to activate ERK1/2 at physiologically relevant
concentrations of the endogenous agonist.
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