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- W1977030607 abstract "It has been claimed recently that, in several cell types, ATP can induce a stimulation of cAMP production which is sensitive to methylxanthine inhibition and is not mediated by the ATP degradation product, adenosine. One explanation for these results would be direct activation of adenosine A2 receptors by ATP itself. We have therefore investigated whether adenine nucleotides are ligands of adenosine A2A receptors from bovine striatum. We show here that ATP, ADP, AMP and their phosphorothioates analogues (ATPγS, ADPβS and AMPαS), at a 100 μM concentration, produced a 83–91% inhibition of the binding of [3H]CGS21680, an adenosine A2A receptor agonist, to striatum membranes. However, this action was inhibited by adenosine deaminase or by adenosine 5′-O-(α,β-methylene)diphosphate (APCP), an inhibitor of 5′-nucleotidase-mediated AMP degradation. The effects of adenosine deaminase and APCP were dependent on their concentration. These results indicate that ATP, ADP and even AMP can exert an effect on the adenosine A2A receptors only through their breakdown into adenosine by ectonucleotidases." @default.
- W1977030607 created "2016-06-24" @default.
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- W1977030607 date "1993-09-01" @default.
- W1977030607 modified "2023-09-25" @default.
- W1977030607 title "Evidence that ATP, ADP and AMP are not ligands of the striatal adenosine A2A receptors" @default.
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- W1977030607 doi "https://doi.org/10.1016/0014-2999(93)90932-8" @default.
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