Histochemical demonstration of acetylcholinesterase activity in human Meibomian glands.

The distribution of acetylcholinesterase activity in human Meibomian glands was evaluated using enzyme-histochemical methods. The butyrylcholinesterase (BuChE) inhibitor, tetraisopropyl pyrophosphoramide (iso-OMPA), was used to localize acetylcholinesterase (AChE) activity, the AChE inhibitor, 1,5-bis (4-allyldimethylammoniumphenyl) pentan-3-one dibromide (BW284c51), was used to localize BuChE activity, and eserine was used to inhibit all cholinesterase activity in control incubations; the appropriate specific inhibitors for competing enzymic activities were added to the incubation medium. At the light microscopic level, acetylcholinesterase reaction product appeared as cytoplasmic brown deposits, often crystalline. A very dense accumulation of AChE-positive nerve fibers was seen in the form of a network around the acinar and the ductal tissue of the glands. No discrete nerve endings were observed, whereas a strong reaction was elicited in some fibers in close association with blood vessels. These observations suggest that the cholinergic system is involved in the regulation of the Meibomian glands secretory function.