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One of the most conserved mechanisms for transmission of a nerve pulse acrossa synapse relies on acetylcholine. Ever since the Nobel-prize winning works ofDale and Loewi, it has been assumed that acetylcholine - subsequent to itsaction on a postsynaptic cell - is split into inactive by-products byacetylcholinesterase. Herein, this widespread assumption is falsified.Excitable cells (Chara australis internodes), which had previously beenunresponsive to acetylcholine, became acetylcholine-sensitive in presence ofacetylcholinesterase. The latter was evidenced by a striking difference in cellmembrane depolarisation upon exposure to 10 mM intact acetylcholine(deltaV=-2plus/minus5 mV) and its hydrolysate respectively(deltaV=81plus/minus19 mV) for 60 sec. This pronounced depolarization, whichalso triggered action potentials, was clearly attributed to one of thehydrolysis products: acetic acid (deltaV=87plus/minus9 mV at pH 4.0; cholineineffective in range 1-10 mM). In agreement with our findings, numerous studiesin the literature have reported that acids excite gels, lipid membranes, plantcells, erythrocytes as well as neurons. Whether excitation of the postsynapticcell in a cholinergic synapse is due to protons or due to intact acetylcholineis a most fundamental question that has not been addressed so far.

On the excitation of action potentials by protons and its potential implications for cholinergic transmission