title: Loss of epinephrine stimulated synthesis of cyclic adenosine 3':5' monophosphate during maturation of rabbit and human reticulocytes.
abstract: The adenylate cyclase activity of rabbit reticulocytes is localized in the stroma. Rabbit reticulocytes are four times more active than mature erythrocytes in transforming in situ formed [14C] adenosine triphosphate into [14C] cyclic adenosine 3':5'-monophosphate. Similarly, anaemic human red blood cells show higher activity in effecting this transformation. The adenylate cyclase activity is stimulated by epinephrine, 40% in rabbit reticulocytes, and 70-80% in anaemic human RBC but not in erythrocytes. Both the reticulocytes and erythrocytes can bind [14C] epinephrine, but the reticulocytes bind a relatively large amount. A glycogen phosphorylase that can be activated by cyclic adenosine 3':5'-monophosphate is detected only in reticulocytes. Both reticulocytes and erythrocytes contain a phosphodiesterase which can hydrolyse cyclic 3':5'-adenosine monophosphate and which is activated by imidazole and inhibited by methyl xanthines.
mesh_terms: D015105:3',5'-Cyclic-AMP Phosphodiesterases / Q000097:blood; D000262:Adenylyl Cyclases / Q000097:blood; D000375:Aging; D000740:Anemia / Q000097:blood / Q000201:enzymology; D000818:Animals; D001665:Binding Sites; D002855:Chromatography, Thin Layer; D000242:Cyclic AMP / Q000096:biosynthesis* / Q000097:blood; D004837:Epinephrine / Q000097:blood / Q000494:pharmacology*; D004912:Erythrocytes / Q000201:enzymology / Q000378:metabolism; D006801:Humans; D006005:Phosphorylases / Q000097:blood; D011817:Rabbits; D012156:Reticulocytes / Q000201:enzymology / Q000378:metabolism*; D013268:Stimulation, Chemical
chemical_list: D000242:Cyclic AMP; D006005:Phosphorylases; D015105:3',5'-Cyclic-AMP Phosphodiesterases; D000262:Adenylyl Cyclases; D004837:Epinephrine