Acetylcholinesterase is a key molecule in the control of cholinergic transmission. In the mammalian neuromuscular junction (NMJ), the efficiency of this phenomenon depends on the enzyme location, between the presynaptic site where acetylcholine is released and the postsynaptic membrane where the acetylcholine receptors are packed. Various molecular forms of the enzyme that possess the same catalytic activity are expressed. The relative amounts of these forms are tissue-specific. At the subcellular level, this panoply of forms allows the enzyme to be attached to the membrane or to the basal lamina. Analysis of the forms secreted and their position in the cytoarchitecture of the NMJ is essential to understand the functioning of this synapse. This review will consider the origin of the enzyme polymorphism and its physiological implication.
Copyright 2000 Wiley-Liss, Inc.