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Both A1 and A2a Purine Receptors Regulate Striatal Acetylcholine Release

Abstract: The receptors responsible for the adenosine‐mediated control of acetylcholine release from immunoaffinitypurified rat striatal cholinergic nerve terminals have been characterized. The relative affinities of three analogues for the inhibitory receptor were (R)‐phenylisopropyladenosine > cyclohexyladenosine > N‐ethylcarboxamidoadenosine (NECA), with binding being dependent of the presence of Mg2+ and inhibited by 5′‐guanylylimidodiphosphate [Gpp(NH)p] and adenosine receptor antagonists. Adenosine A1 receptor agonists inhibited forskolin‐stimulated cholinergic adenylate cyclase activity, with an IC50 of 0.5 nM for (R)‐phenylisopropyladenosine and 500 nM for (S)‐phenylisopropyladenosine. A1 agonists inhibited acetylcholine release at concentrations approximately 10% of those required to inhibit the cholinergic adenylate cyclase. High concentrations (1 μM) of adenosine A1 agonists were less effective in inhibiting both adenylate cyclase and acetylcholine release, due to the presence of a lower affinity stimulatory A2 receptor. Blockade of the A1 receptor with 8‐cyclopentyl‐1,3‐dipropylxanthine revealed a half‐maximal stimulation by NECA of the adenylate cyclase at 10 nM, and of acetylcholine release at approximately 100 nM. NECA‐stimulated adenylate cyclase activity copurified with choline acetyltransferase in the preparation of the cholinergic nerve terminals, suggesting that the striatal A2 receptor is localized to cholinergic neurones. The possible role of feedback inhibitory and stimulatory receptors on cholinergic nerve terminals is discussed.