Choline acetyltransferase is expressed by non-starburst amacrine cells in the ground squirrel retina

Brain Res. 2003 Feb 21;964(1):21-30. doi: 10.1016/s0006-8993(02)04049-0.

Abstract

We have used immunostaining techniques to reveal a new type of amacrine cell that is immunoreactive for choline acetyltransferase (ChAT), the acetylcholine synthesizing enzyme, in the Ground Squirrel (Spermophilus beecheyi) retina. Cryostat sections and double immunostained wholemount preparations were examined by confocal microscopy. This new ChAT type III cell is distinct in morphology and neurotransmitter content from the well know 'starburst' amacrine cells (types I and II) that are so well represented in the ground squirrel retina [J. Comp. Neurol. 365 (1996) 173-216]. The type III cell colocalizes glycine with the acetylcholine and does not appear to be GABAergic or exhibit calcium-binding proteins like the well-known starburst type. As well, type III cells do not occur as a mirror-symmetric pair with normally placed and displaced varieties. The type III cell is probably a small field amacrine type branching broadly in upper sublamina b of the inner plexiform layer, and is most likely A6 of the Ground Squirrel retina [J. Comp. Neurol. 365 (1996) 173-216]. Type III cells are ideally placed in the architecture of the Ground Squirrel retina to influence ON directionally selective ganglion cell types.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylcholine / metabolism*
  • Acetylcholinesterase / metabolism*
  • Amacrine Cells / cytology
  • Amacrine Cells / enzymology*
  • Animals
  • Calcium-Binding Proteins / metabolism
  • Cell Count
  • Cell Size / physiology
  • Dendrites / enzymology*
  • Dendrites / ultrastructure
  • Fluorescent Antibody Technique
  • Glycine / metabolism
  • Microscopy, Confocal
  • Neural Pathways / cytology
  • Neural Pathways / metabolism
  • Retinal Ganglion Cells / cytology
  • Retinal Ganglion Cells / metabolism
  • Sciuridae / anatomy & histology
  • Sciuridae / classification
  • Sciuridae / metabolism*
  • Synaptic Transmission / physiology
  • Vision, Ocular / physiology
  • gamma-Aminobutyric Acid / metabolism

Substances

  • Calcium-Binding Proteins
  • gamma-Aminobutyric Acid
  • Acetylcholinesterase
  • Acetylcholine
  • Glycine