Molecular forms of acetylcholinesterase in Xenopus muscle.
Xenopus adult muscle, whole Xenopus embryos, and cultured embryonic myocytes together contain five acetylcholinesterase forms which can be resolved by sucrose density gradient centrifugation. These are identified as the collagenase-sensitive asymmetric forms A12 and A8, and the globular forms G4, G2, and G1. Asymmetric forms rise in whole embryos during the period of neuromuscular synapse formation, but their rise is not prevented by tricaine methanesulfonate, which abolishes motor activity. Aneural myocyte cultures synthesize primarily asymmetric acetylcholinesterase, much of which is extracellular. Prior nerve contact is not required for its expression. The proportion of asymmetric forms is neither decreased by tetrodotoxin, nor enhanced by veratridine and aconitine. We conclude that muscle activity does not modulate the expression of asymmetric acetylcholinesterase in Xenopus.
R I
RI
Lappin
L L
LL
Rubin
D000110:Acetylcholinesterase; D000157:Aconitine / Q000494:pharmacology; D000818:Animals; D002478:Cells, Cultured; D004625:Embryo, Nonmammalian / Q000378:metabolism; D007473:Ion Channels / Q000187:drug effects; D008968:Molecular Conformation; D009132:Muscles / Q000166:cytology / Q000196:embryology / Q000201:enzymology*; D013779:Tetrodotoxin / Q000494:pharmacology; D014981:Xenopus
D007473:Ion Channels; D013779:Tetrodotoxin; D000110:Acetylcholinesterase; D000157:Aconitine