Decrease of tailed, asymmetric 16S acetylcholinesterase in rat superior cervical ganglion neurons in vitro after potassium depolarization: partial antagonist action of a calcium-channel blocker.
In primary cell cultures of rat superior cervical ganglia the tailed, asymmetric 16S molecular form of acetylcholinesterase (AChE) is preferentially decreased after potassium depolarization. This effect is not related to noradrenergic differentiation elicited by high potassium concentration. Moreover there is a partial antagonist action of a calcium-channel blocker, methoxyverapamil (D-600). These results suggest that membrane electrical activity exerts a regulatory control on AChE, and Ca2+ fluxes play an important role in regulatory events of AChE biosynthesis.
D000110:Acetylcholinesterase / Q000378:metabolism*; D000818:Animals; D002118:Calcium / Q000502:physiology*; D002795:Choline O-Acetyltransferase / Q000378:metabolism; D046508:Culture Techniques; D005711:Gallopamil / Q000494:pharmacology; D005728:Ganglia, Sympathetic / Q000201:enzymology*; D007473:Ion Channels / Q000502:physiology*; D007527:Isoenzymes / Q000378:metabolism*; D011188:Potassium / Q000494:pharmacology*; D051381:Rats; D014446:Tyrosine 3-Monooxygenase / Q000378:metabolism
D007473:Ion Channels; D007527:Isoenzymes; D005711:Gallopamil; D014446:Tyrosine 3-Monooxygenase; D002795:Choline O-Acetyltransferase; D000110:Acetylcholinesterase; D011188:Potassium; D002118:Calcium