Ultrastructural localization of acetylcholinesterase and choline acetyltransferase in oligodendrocytes, glioblasts and vascular endothelial cells in the external cuneate nucleus of the gerbil

Anat Embryol (Berl). 1996 Aug;194(2):177-85. doi: 10.1007/BF00195011.

Abstract

This study reports the reactivities of acetylcholinesterase (AChE) and choline acetyltransferase (ChAT) in some of the nonneuronal elements in the external cuneate nucleus (ECN) of gerbils. AChE reaction products were localized in some oligodendrocytes in their cisternae of rough endoplasmic reticulum, nuclear envelope and Golgi saccules. The basal lamina lining the capillary endothelia also displayed AChE reactivity. In ChAT immunocytochemistry, the reaction products were found to be associated with the vascular basal lamina as well as the endothelial plasma membrane facing the lumen. The most remarkable finding was the localization of ChAT immunoreactivity in some oligodendrocytes and occasional glioblasts (small glial precursor cells containing a thin rim of cytoplasm surrounding an irregular nucleus with homogeneous chromatin materials). The ChAT-positive oligodendrocytes consisted of two types, medium-dense and dark cells, either associated with blood vessels or ChAT-stained neuronal elements. It is suggested from these new findings that at least some of the oligodendrocytes and glioblasts in the ECN of gerbils may be involved in the synthesis, storage, release and degradation of acetylcholine.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylcholinesterase / analysis*
  • Animals
  • Autonomic Pathways / enzymology
  • Choline O-Acetyltransferase / analysis*
  • Endothelium, Vascular / enzymology*
  • Endothelium, Vascular / ultrastructure
  • Female
  • Gerbillinae
  • Immunohistochemistry
  • Male
  • Medulla Oblongata / enzymology*
  • Medulla Oblongata / ultrastructure
  • Microscopy, Electron
  • Oligodendroglia / enzymology*
  • Oligodendroglia / ultrastructure

Substances

  • Choline O-Acetyltransferase
  • Acetylcholinesterase