Positive coupling of beta-like adrenergic receptors with adenylate cyclase in the cnidarian Renilla koellikeri.
Coupling of the previously characterized beta1- and beta2-like adrenoceptors in the sea pansy Renilla koellikeri with adenylate cyclase was examined in membrane preparations from this cnidarian. Adenylate cyclase activity was stimulated by several guanine nucleotides, such as GTP, Gpp(NH)p and GTPgammaS. Fluoride ions and cholera toxin greatly enhanced the enzyme activity, whereas forskolin had no effect on basal or isoproterenol-induced stimulation of the enzyme. The stimulation of adenylate cyclase activity by several beta-adrenergic agonists in different parts of the animal reflected a positive coupling with the beta2- and beta1-like adrenoceptors in autozooid and peduncle tissues, respectively. In addition, isoproterenol-induced stimulation of adenylate cyclase activity was dependent on guanine nucleotides, suggesting coupling mediated by a G protein. The pharmacological profile of various antagonists on isoproterenol-sensitive adenylate cyclase in autozooid and peduncle tissues matched that of previous radioligand binding studies. Isoproterenol-induced stimulation of adenylate cyclase activity in rachidial tissues was partially inhibited by trifluoperazine of (+/-)CGP12177 and was completely blocked in the presence of both antagonists. This suggests that coupling of the enzyme occurs with beta1- and beta2-like adrenoceptors, both being present in the rachis. Serotonin and dopamine were also found to stimulate adenylate cyclase activity. Their stimulatory effect was additive to isoproterenol-induced activation, suggesting the presence of dopaminergic and serotonergic receptors in the tissues of the sea pansy. Along with the data presented previously on beta-adrenergic binding, this study suggests that elements of receptor-dependent G protein signal transduction originated early in invertebrate evolution.
Awad
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Département de sciences biologiques, Université de Montréal, Québec, Canada.
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D000262:Adenylyl Cyclases / Q000502:physiology*; D000319:Adrenergic beta-Antagonists / Q000494:pharmacology; D000818:Animals; D001262:Atenolol / Q000494:pharmacology; D002772:Cholera Toxin / Q000494:pharmacology; D003063:Cnidaria / Q000502:physiology*; D005576:Colforsin / Q000494:pharmacology; D005459:Fluorides / Q000494:pharmacology; D006150:Guanine Nucleotides / Q000494:pharmacology; D007545:Isoproterenol / Q000494:pharmacology; D018377:Neurotransmitter Agents / Q000494:pharmacology; D011943:Receptors, Adrenergic, beta / Q000502:physiology*; D015398:Signal Transduction / Q000187:drug effects; D013806:Theophylline / Q000494:pharmacology; D014268:Trifluoperazine / Q000494:pharmacology
D000319:Adrenergic beta-Antagonists; D006150:Guanine Nucleotides; D018377:Neurotransmitter Agents; D011943:Receptors, Adrenergic, beta; D005576:Colforsin; D014268:Trifluoperazine; D001262:Atenolol; D002772:Cholera Toxin; D013806:Theophylline; D000262:Adenylyl Cyclases; D007545:Isoproterenol; D005459:Fluorides