Fine structural localisation of acetylcholinesterase activity in the compound eye of the honeybee (Apis mellifica L.).
Acetylcholinesterase (AChE) activity was demonstrated histochemically at the electron microscopic level in the compound eye of the worker bee (Apis mellifica L.) by use of the method of Lewis and Shute (1969). All photoreceptor axons (short and long visual fibres) display AChE activity. The reaction product is located in the axoplasm and at the plasma membrane. Substantial amounts of the reaction product can be detected in the intercellular spaces between the visual fibres. Along the visual fibres, the enzyme activity is unevenly distributed. High AChE activity is present in the distal parts of te axons, in contrast to lower enzyme levels in the lamina. However, AChE is also present in the proximal terminals of the visual fibres as well as in the intercellular spaces between visual fibre terminals and the postsynaptic neurones (monopolar cells). Intracellular enzyme activity is almost absent in the monopolars. The authors assume the high AChE activity in the visual fibres to be indicative of acetylcholine as the transmitter at the first synapse of the compound eye. This hypothesis is discussed in  view of the results of autoradiographic, electrophysiological and pharmacological investigations of the compound eye and of hte ocellus. Our data are a variance with results of studies on the eyes of Diptera.
D000110:Acetylcholinesterase / Q000378:metabolism*; D000818:Animals; D001369:Axons / Q000201:enzymology / Q000648:ultrastructure; D001516:Bees; D005123:Eye / Q000201:enzymology* / Q000648:ultrastructure; D008854:Microscopy, Electron; D010786:Photoreceptor Cells / Q000201:enzymology / Q000648:ultrastructure
D000110:Acetylcholinesterase