ELECTRON MICROSCOPIC CYTOCHEMISTRY OF CHOLINESTERASE ACTIVITY OF MOUSE DIGITAL CORPUSCLE

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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 caveola 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 found in the cistern of the rough endoplasmic reticulum and in the nuclear envelope of the lamellar cell body. The enzyme apparently is synthesized in the lamellar cells and released into the interlamellar and perineural spaces in the corpuscle. The enzyme activity was inhibited by eserine 10-4 M, DFP [diisopropyl fluorophosphate] 10-5 M or iso-OMPA [tetraisopropyl pyrophosphoramide] 10-4 M, but not by BW284C51 [1,5-bis-(4-allyldimethylammonium phenyl) pentan-3-one dibromide] at a concentration lower than 10-4 M. The enzyme activity apparently is not acetylcholinesterase (AChE) but of nonspecific cholinesterase.