Connexin-36 distribution and layer-specific topography in the cat retina

Brain Struct Funct. 2019 Jul;224(6):2183-2197. doi: 10.1007/s00429-019-01876-y. Epub 2019 Jun 6.

Abstract

Connexin-36 (Cx36) is the major constituent of mammalian retinal gap junctions positioned in key signal pathways. Here, we examined the laminar and large-scale topographical distribution of Cx36 punctate immunolabels in the retina of the cat, a classical model of the mammalian visual system. Calretinin-immunoreactive (CaR-IR) cell populations served to outline the nuclear and plexiform layers and to stain specific neuronal populations. CaR-IR cells included horizontal cells in the outer retina, numerous amacrine cells, and scattered cells in the ganglion cell layer. Cx36-IR plaques were found among horizontal cell dendrites albeit without systematic colocalization of the two labels. Diffuse Cx36 immunoreactivity was found in the cytoplasm of AII amacrine cells, but no colocalization of Cx36 plaques was observed with either the perikarya or the long varicose dendrites of the CaR-IR non-AII amacrine cells. Cx36 puncta were seen throughout the entire inner plexiform layer showing their highest density in the ON sublamina. The densities of AII amacrine cell bodies and Cx36 plaques in the ON sublamina were strongly correlated across a wide range of eccentricities suggesting their anatomical association. However, the high number of plaques per AII cell suggests that a considerable fraction of Cx36 gap junctions in the ON sublamina is formed by other cell types than AII amacrine cells drawing attention to extensive but less studied electrically coupled networks.

Keywords: AII amacrine cell; Calretinin; Eccentricity; Gap junction.

MeSH terms

  • Amacrine Cells / metabolism
  • Animals
  • Calbindin 2 / metabolism
  • Cats
  • Connexins / metabolism*
  • Dendrites / metabolism*
  • Gap Junctions / metabolism
  • Immunohistochemistry / methods
  • Retina / metabolism*
  • Retinal Rod Photoreceptor Cells / metabolism
  • Visual Pathways / physiology*

Substances

  • Calbindin 2
  • Connexins
  • connexin 36