The cyclic AMP-mediated expression of acetylcholinesterase in myotubes shows contrasting activation and repression between avian and mammalian enzymes.

摘要: Abstract Cyclic adenosine 3′,5′-monophosphate (cAMP)-dependent signalling pathway has been proposed to regulate acetylcholinesterase (AChE) expression in chick muscle; however, its role mammalian enzyme is not known. We provide several lines of evidence suggest that the cAMP-mediated AChE myotube oppositely regulated between avian and enzymes. Human promoter was tagged with luciferase, namely Hp-Luc, which transfected into cultured myotubes. Application cAMP forskolin induced but reduced human promoter-driven luciferase activity. Transfection cDNAs encoding active mutants G proteins altered intracellular level myotubes as well AChE. When constitutively forms Activating Transcription Factor-1 (EWS/ATF-1 oncogene) were over expressed Hp-Luc myotubes, transcript protein increased from ∼1.8- ∼2.5-fold, activity decreased by 60%. Overexpression cAMP-responsive element binding (CREB) markedly enhanced up- downregulated enzymes, respectively. In addition, CREB bound CRE sequence promoter. Mutation on site luciferase; response inhibition still retained. These findings a cAMP-dependent contrasting activation repression muscles.