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- W2112492912 endingPage "1995" @default.
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- W2112492912 abstract "ATP analogs substituted in the γ-phosphorus (ATPγS, β,γ-imido-ATP, and β,γ-methylene-ATP) were used to probe the involvement of P 2 receptors in the modulation of synaptic transmission in the hippocampus, because their extracellular catabolism was virtually not detected in CA1 slices. ATP and γ-substituted analogs were equipotent to inhibit synaptic transmission in CA1 pyramid synapses (IC 50 of 17–22 μ m ). The inhibitory effect of ATP and γ-phosphorus-substituted ATP analogs (30 μ m ) was not modified by the P 2 receptor antagonist suramin (100 μ m ), was inhibited by 42–49% by the ecto-5′-nucleotidase inhibitor and α,β-methylene ADP (100 μ m ), was inhibited by 74–85% by 2 U/ml adenosine deaminase (which converts adenosine into its inactive metabolite-inosine), and was nearly prevented by the adenosine A 1 receptor antagonist 1,3-dipropyl-8-cyclopentylxanthine (10 n m ). Stronger support for the involvement of extracellular adenosine formation as a main requirement for the inhibitory effect of ATP and γ-substituted ATP analogs was the observation that an inhibitor of adenosine uptake, dipyridamole (20 μ m ), potentiated by 92–124% the inhibitory effect of ATP and γ-substituted ATP analogs (10 μ m ), a potentiation similar to that obtained for 10 μ m adenosine (113%). Thus, the present results indicate that inhibition by extracellular ATP of hippocampal synaptic transmission requires localized extracellular catabolism by ecto-nucleotidases and channeling of the generated adenosine to adenosine A 1 receptors." @default.
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- W2112492912 date "1998-03-15" @default.
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- W2112492912 title "Inhibition by ATP of Hippocampal Synaptic Transmission Requires Localized Extracellular Catabolism by Ecto-Nucleotidases into Adenosine and Channeling to Adenosine A<sub>1</sub>Receptors" @default.
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- W2112492912 doi "https://doi.org/10.1523/jneurosci.18-06-01987.1998" @default.
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