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Fillion G, Rousselle JC, Beaudoin D, Pradelles P, Goiny M, Dray F, Jacob J. 
“Serotonin Sensitive Adenylate Cyclase In Horse Brain Synaptosomal Membranes”. 
Life Sciences. 1979;24:1813-1822.
Summary In different membranal preparations isolated from horse brain striatum we have shown the existence of an adenylate cyclase system sensitive to serotonin (5-HT). Activation of the adenylate cyclase was determined by measuring cAMP using a radioimmunoassay. This serotoninergic sensitive enzyme is characterized by a high apparent affinity constant (in the nanomolar range), located on synaptosomal membranes. It is inhibited by antiserotoninergic drugs (cyproheptadine, cinanserin, methysergide, LSD), and synergistically activated by GTP. This serotoninergic activation is clearly additive to the activation induced by dopamine. It appears different from the adenylate cyclase system previously described in the literature which is also activated by 5-HT, but which has a low apparent affinity constant (in the micromolar range); the latter is apparently located in non-synaptosomal membranes, and its activation by 5-HT is non-additive to the activation induced by dopamine. The serotoninergic senstive adenylate cyclase reported in this study, might be related to the serotoninergic binding system which we have previously described which has a similar affinity constant, a similar subcellular distribution and which is inhibited in the same concentration ranges by antiserotoninergic drugs. These two systems might represent a synaptosomal serotoninergic receptor complex.
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