ADENYLATE-CYCLASE ACTIVITY OF SYNAPTIC-MEMBRANES FROM RAT STRIATUM - INHIBITION BY MUSCARINIC RECEPTOR AGONISTS

  • 1 January 1983
    • journal article
    • research article
    • Vol. 23 (2), 393-398
Abstract
Acetylcholine inhibits by 30-40% the basal adenylate cyclase activity of purified synaptic plasma membranes prepared from rat striatum (EC50 [median effective concentration] = 3 mM). Cholinergic receptor agonists inhibit this cyclase activity with the following rank order of potency: oxotremorine > acetylcholine > arecoline > methacholine .gtoreq. muscarine .gtoreq. carbachol > bethanechol. Nicotine fails to inhibit the cyclase, and d-tubocurarine fails to inhibit the action of cholinergic drugs. Atropine and scopolamine antagonize the effect of acetylcholine. The enzyme inhibition elicited by acetylcholine requires the presence of GTP, and disappears after intrastriatal injection of kainic acid. Striatal adenylate cyclase can evidently be modulated by muscarinic receptors.