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Immunocytochemical localization of the GABA C receptor ρ subunits in the cat, goldfish, and chicken retina
Author(s) -
Koulen Peter,
Brandstätter Johann Helmut,
Kröger Stephan,
Enz Ralf,
Bormann Joachim,
Wässle Heinz
Publication year - 1997
Publication title -
journal of comparative neurology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.855
H-Index - 209
eISSN - 1096-9861
pISSN - 0021-9967
DOI - 10.1002/(sici)1096-9861(19970421)380:4<520::aid-cne8>3.0.co;2-3
Subject(s) - inner plexiform layer , retina , outer plexiform layer , colocalization , axon , biology , retinal , microbiology and biotechnology , receptor , protein subunit , immunostaining , axon terminal , neuroscience , immunohistochemistry , biochemistry , gene , immunology
Polyclonal antibodies against the N‐terminus of the rat ρ 1 subunit were used to study the distribution of γ‐aminobutyric acid C (GABA C ) receptors in the cat, goldfish, and chicken retina. Strong punctate immunoreactivity was present in the inner plexiform layer (IPL) of all three species. The punctate labelling suggests a clustering of the GABA C receptors at synaptic sites. Weak label was also found in the outer plexiform layer (OPL) and over the cell bodies of bipolar cells. Double immunostaining of vertical sections with an antibody against protein kinase C (PKC) showed the punctate immunofluorescence to colocalize with bipolar cell axon terminals. In the goldfish retina, the axon terminals of Mb1 bipolar cells were enclosed by ρ‐immunoreactive puncta. In the chicken retina, several distinct strata within the IPL showed a high density of ρ‐immunoreactive puncta. The results suggest a high degree of sequence homology between the ρ subunits of different vertebrate species, and they show that the retinal localization of GABA C receptors is similar across different species. J. Comp. Neurol. 380:520–532, 1997. © 1997 Wiley‐Liss, Inc.