Abstract
Acetylcholinesterase (AChE) is an essential enzymatic component of the neuromuscular junction where it is responsible for terminating neurotransmission by the cholinergic motor neurons. The enzyme at the neuromuscular junction (NMJ) is contributed primarily by the skeletal muscle where it is produced at higher levels in the post-synaptic region of the fibers. The major form of AChE at the NMJ is a large asymmetric form consisting of three tetramers covalently attached to a three-stranded collagen-like tail which is responsible for anchoring it to the synaptic basal lamina. Its location and expression is regulated to a large extent by the motor neurons and occurs at the transcriptional, translational and post-translational levels. While its expression can be quite rapid in tissue cultured cells, its half-life in vivo appears to be quite long, about three weeks, although more rapidly turning over pools have been described. Finally the essential nature of this enzyme is underscored by the fact that no naturally occurring null mutations of the catalytic subunit have been described in higher organisms and the few dozen humans carrying mutations in the collagen tail responsible for anchoring the enzyme at the NMJ are severely affected.
