Abstract
Cholinesterase (ChE) activity was ultracytochemically demonstrated in mouse digital (Meissner-like) corpuscles by Karnovsky's or Koelle-Friedenwald's method. Intense enzyme activity was found in the caveolae of lamellar cell processes, in the interlamellar spaces and in the narrow perineural spaces between the nerve endings and the apposing lamellar processes. Prominent enzyme activity was also found in the cistern of the rough endoplasmic reticulum as well as in the nuclear envelope of the lamellar cell body. These findings suggest that the enzyme is synthesized in the lamellar cells and released into the interlamellar and perineural spaces in the corpuscle. The enzyme activity was inhibited by eserine 10-4M, DFP 10-5M, or iso-OMPA 10-4M, but not by BW284C51 at a concentration lower than 10-4M. This result indicates that the enzyme activity studied is not that of acetylcholinesterase (AChE) but of nonspecific cholinesterase.
