Acetylcholinesterase (AchE) can be induced in a non-neuronal, epithelial cell line from Chironomus tentans by the moulting hormone 20-OH-ecdysone. Maximal response is reached after 7 days. The increase in enzymatic activity can be suppressed by simultaneous incubation with inhibitors of transcription and translation. The potency of various steroid hormones to induce AchE coincides with their affinity to the ecdysteroid hormone receptor.
AchE from Chironomus is tightly bound to membranes and cannot be solubilized by heparin or collagenase treatment. Incubation under conditions where phospholipase C is most active releases activity into the supernatant. If phospholipase is applied in addition, the amount of solubilized enzyme increases, but there is still membrane-bound activity left. This is in accordance with a globular form of AchE linked to membranes by a phospholipid-anchor. The enzyme sediments as a single peak of 5.4 S.
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