Abstract
Multiple molecular forms of acetylcholinesterase are found in rat primary muscle cell cultures (mainly 4 S, 6.5 S, 10 S, 12 S, and 16 S). During differenciation (myoblasts → immature myotubes → spontaneously contracting, mature myotubes) a precise developmental pattern in total AChE activity in the relative proportion of the different molecular forms have been found. Total AChE increases when myoblasts fusion occurs: later the 16 S form is induced (about 1 day after spontaneous contractions are first noticed in culture). Tetrodotoxin (TTX), which reversibly blocks the contractile activity, acts on the presence of the 16 S form. The 16 S form disappears upon addition of 1 μ M TTX, with a half-life of about 1 day. After removal of TTX, it reappears into the myotubes, is fully restored, after about 2 days, to control levels, and does not seem to be focally distributed on the surface of the myotubes. This culture system seems to be very well suited for studies on the cellular regulation of the high molecular weight forms of AChE.
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