[Organophosphorus compounds as tools for the pharmaco-histochemical study of cholinesterase in the rat striatum]

Arch Anat Microsc Morphol Exp. 1986;75(3):135-48.
[Article in French]

Abstract

A series of organophosphorous compounds (OP) was tested using a pharmacohistochemical method applied in vitro on the rat striatum, the central structure which contains the highest levels of acetylcholine and its metabolic enzymes; the OP showed a great variety of action towards the specific cholinesterase (AChE) and non-specific cholinesterase (BuChE). Except for iso-OMPA which is specific for BuChE localized in the microvessels endothelium, all the OP doses used in the present study were more or less potent inhibitors of cholinesterases (ChE). 15 mn after LD 50 doses of OP administered by subcutaneous route, a partial inhibition of the neurophile AChE occurred, revealing some striatal neurons which displayed high residual activity, i.e. the cholinergic interneurons. During the recovery phase following the inhibition of AChE by 1.5 LD 50 doses (the animals being treated with atropine) the AChE reaction product was detected almost simultaneously in some axo-spinous synapses probably non-cholinergic. The partial inhibition and the de novo synthesis of AChE also revealed the presence of small and less reactive non-cholinergic neurons. Among all the OP tested, soman was remarkable for its patchy inhibition of AChE in the striatum. The significance of the alternation of reactive and non-reactive areas is discussed.

MeSH terms

  • Acetylcholinesterase / metabolism*
  • Animals
  • Butyrylcholinesterase / metabolism*
  • Cholinesterase Inhibitors / pharmacology*
  • Cholinesterases / metabolism*
  • Corpus Striatum / cytology
  • Corpus Striatum / enzymology*
  • Corpus Striatum / ultrastructure
  • Histocytochemistry
  • Microscopy, Electron
  • Organophosphorus Compounds / pharmacology*
  • Rats
  • Structure-Activity Relationship

Substances

  • Cholinesterase Inhibitors
  • Organophosphorus Compounds
  • Acetylcholinesterase
  • Butyrylcholinesterase
  • Cholinesterases