Neurons segregate clusters of membrane-bound acetylcholinesterase along their neurites.

Immunocytochemical studies with a monoclonal antibody show that acetylcholinesterase (AcChoEase; EC 3.1.1.7) is distributed in clusters along the fibers of cultured sympathetic neurons but is essentially absent from cell bodies. Although tissue-cultured sympathetic neurons synthesize several oligomeric forms of AcChoEase, only the hydrophobic globular (G4) form of AcChoEase is present within these clusters. This G4 form is asymmetrically distributed within neurons and is transported preferentially into nerve fibers following its synthesis in the cell bodies. Thus G4 is found in clusters on neurons and is readily distinguishable from the hydrophilic forms on the surfaces of myotubes. The association of a specialized form of AcChoEase in densities on neurons in culture indicates that neurons and myotubes have distinct mechanisms for localizing AcChoEase molecules on their surfaces and suggests that these two types of electrically excitable cells have different requirements for organizing synaptic components on their plasma membranes.