Effects of persistent selective suppression of ganglionic butyrylcholinesterase on steady state and regenerating levels of acetylcholinesterase: implications regarding function of butyrylcholinesterase and regulation of protein synthesis.
Persistent selective suppression of the butyrylcholinesterase (cholinesterase; acylcholine acyl-hydrolase, EC 3.1.1.8) activity of the superior cervical, stellate, and ciliary ganglia of cats by the daily administration of tetramonoisopropyl pyrophosphortetramide, 3.0 mumol/kg, intravenously, for 6 days produced a significant elevation in the levels of ganglionic acetylcholinesterase (acetylcholine hydrolase, EC 3.1.1.7). When the same procedure was preceded by the inactivation of over 95% of the ganglionic acetylcholinesterase by sarin, 2.0 mumol/kg, intravenously, the rate of regeneration of acetylcholinesterase was decreased. Results are interpreted as evidence that ganglionic butyrylcholinesterase may serve as a precursor to acetylcholinesterase, and that the level of butyrylcholinesterase may regulate the rate of acetylcholinesterase synthesis.
D000110:Acetylcholinesterase / Q000096:biosynthesis*; D000818:Animals; D002091:Butyrylcholinesterase / Q000378:metabolism; D002415:Cats; D002800:Cholinesterase Inhibitors / Q000494:pharmacology; D004790:Enzyme Induction; D005725:Ganglia, Autonomic / Q000201:enzymology; D012524:Sarin / Q000494:pharmacology; D013770:Tetraisopropylpyrophosphamide / Q000494:pharmacology; D013997:Time Factors
D002800:Cholinesterase Inhibitors; D013770:Tetraisopropylpyrophosphamide; D012524:Sarin; D000110:Acetylcholinesterase; D002091:Butyrylcholinesterase