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• W1930805306 endingPage "82" @default.
• W1930805306 startingPage "477" @default.
• W1930805306 abstract "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 A(1), A(2A), A(2B), and A(3), 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 A(1) and A(3) receptor-transfected cells, intermediate in A(2A) and low in A(2B) receptor-expressing CHO cells. For all receptors the half-maximal ERK1/2 phosphorylation was observed at 19-115 nM NECA. NECA acting on adenosine A(2B) receptors was much more potent in stimulating ERK1/2 phosphorylation (EC(50) = 19 nM) than cAMP formation (EC(50) = 1.4 microM). 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 microM) 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." @default.
• W1930805306 created "2016-06-24" @default.
• W1930805306 creator A5008327136 @default.
• W1930805306 creator A5060927839 @default.
• W1930805306 date "2000-09-01" @default.
• W1930805306 modified "2023-10-17" @default.
• W1930805306 title "Human adenosine A(1), A(2A), A(2B), and A(3) receptors expressed in Chinese hamster ovary cells all mediate the phosphorylation of extracellular-regulated kinase 1/2." @default.
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• W1930805306 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/10953039" @default.
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