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Coexistence in human and primate neuromuscular junctions of enzymes synthesizing acetylcholine, catecholamine, taurine, and gamma-aminobutyric acid.

Coexistence of neurotransmitter-synthesizing enzymes choline acetyltransferase, cysteine sulfinic acid decarboxylase, tyrosine hydroxylase, and L-glutamic acid decarboxylase was demonstrated at human and primate neuromuscular junctions with specific antibodies directed against these enzymes. Motor end plates were identified in unfixed cryostat sections by standard cholinergic markers for acetylcholinesterase and the acetylcholine receptor. Each of the four transmitter-synthesizing enzymes was localized at end plates displaying these markers. The presence of any two of the four enzymes at a given end plate was established by (i) showing immunoreaction for one enzyme followed by elution and demonstration of immunoreaction for a second enzyme, and (ii) paired immunofluorescence with simultaneous demonstration of one enzyme with a rhodamine-labeled second antibody and of the other enzyme with a fluorescein-labeled second antibody. These findings imply that motor nerve terminals have the capacity for synthesizing not only acetylcholine but also taurine, catecholamines, and gamma-aminobutyric acid. These substances, in turn, may participate in the normal regulation of nerve-muscle interaction or be significant in specific disorders involving the motor unit.