Open AccesscAMP stimulation of acetylcholine receptor expression is mediated through posttranslational mechanisms.
Author(s) -
William N. Green,
Anthony F. Ross,
Toni Claudio
Publication year - 1991
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.88.3.854
Subject(s) - protein subunit , forskolin , biology , cholera toxin , intracellular , gi alpha subunit , acetylcholine receptor , heterologous expression , microbiology and biotechnology , g alpha subunit , interleukin 10 receptor, alpha subunit , cyclic adenosine monophosphate , stimulation , receptor , biochemistry , recombinant dna , gene , endocrinology
When the four Torpedo acetylcholine receptor (AcChoR) subunit cDNAs are stably integrated into the genome of mouse fibroblast cells, alpha 2 beta gamma delta pentamers with proper pharmacological and electrophysiological properties are expressed on the cell surface. Expression of these AcChoRs can be regulated by agents that stimulate intracellular cAMP levels with the result that increased numbers of cell-surface AcChoRs are produced. Theophylline, 8-(4-chlorophenylthio)-adenosine 3':5'-cyclic monophosphate, cholera toxin, and forskolin stimulated AcChoR cell-surface expression 1.2-, 1.6-, 2.2-, and 2.3-fold, respectively. cAMP-stimulated expression is mediated through a posttranslational mechanism, and the observed increase in surface AcChoRs correlates with increased lifetimes of each newly synthesized subunit. Increased subunit lifetimes are not observed in cell lines expressing each subunit individually, indicating that subunit stabilization arises through heterologous subunit-subunit interactions.