Dicyclohexylcarbodiimide influences the regulatory properties of the adenylate cyclase system in rat reticulocyte membranes.
Treatment of rat reticulocyte plasma membranes with dicyclohexylcarbodiimide (DCCD) decreased the GTP-stimulated adenylate cyclase activity and reduced the number of receptors that bind the agonist with high affinity in the absence of GTP. Besides, the agonist's competition curve was shifted to the right, irrespective of the presence of guanyl nucleotides. The dissociation constant for the antagonist and the number of binding sites did not change. Preincubation of the DCCD-treated membranes with GMP in the presence of isoproterenol restored the regulation of the agonist's affinity by guanyl nucleotides; however, in this case the GTP-independent change in the agonist's affinity was retained. This suggests that one of the DCCD-modified components of the adenylate cyclase system is a regulatory protein.
D000262:Adenylyl Cyclases / Q000097:blood*; D000818:Animals; D002234:Carbodiimides / Q000494:pharmacology*; D002462:Cell Membrane / Q000378:metabolism; D004024:Dicyclohexylcarbodiimide / Q000494:pharmacology*; D006150:Guanine Nucleotides / Q000494:pharmacology; D066298:In Vitro Techniques; D007545:Isoproterenol / Q000494:pharmacology; D051381:Rats; D011956:Receptors, Cell Surface / Q000378:metabolism; D012156:Reticulocytes / Q000187:drug effects* / Q000378:metabolism
D002234:Carbodiimides; D006150:Guanine Nucleotides; D011956:Receptors, Cell Surface; D004024:Dicyclohexylcarbodiimide; D000262:Adenylyl Cyclases; D007545:Isoproterenol