Abstract
The reactivating and cholinolytic action of trimedoxime bromide was evaluated during experiments on rat soleus and diaphragm muscles accoridng to the amplitude and time course of miniature end-plate potentials and currents (MEPP and MEPC respectively). This agent reactivates acetylcholinesterase (AChE) phosphorylation. The effects of trimedoxime bromide at concentrations of 5·10−6–5·10−4 M following AChE inhibition on the amplitude and duration of MEPP arises from complex interaction between the reactivating and cholinolytic effects. A separate evaluation of the reactivating effect (once the reactivating agent had been removed) revealed that this action increases throughout the entire range of trimedoxime bromide concentration: complete reactivation of AChE phosphorylation was observed under the action of 2–5·10−4 M trimedoxime bromide. Examination of the cholinolytic effect in isolation (with voltage-clamping at the muscle and intact AChE) showed that blockade of open end-plate ionic channels underlies this effect. Reduction in MEPC amplitude together with retarded (but still exponential) decay of signals were distinguishing features of this blockade, confirming that trimedoxime bromide acts as a “very fast blocker”.
Published Version
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