• glutamic acid decarboxylase;
  • interneurons;
  • digoxigenin;
  • cRNA probes;
  • hippocampus


The physiological properties of α-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA)-type glutamate receptor (GluR) channels are determined by their subunit composition. In particular, the expression of the GluR-B subunit determines the divalent ion selectivity of the channel. We studied the distribution of GluR-B mRNA and protein in adult rat hippocampal GABAergic neurons combining non-radioactive in situ hybridization with immunocytochemistry. The majority of GABAergic hippocampal neurons were GluR-B mRNA-positive, but overall the levels of GluR-B transcript were lower than in pyramidal and granule cells, which showed the highest hybridization signal. The different GluR-B mRNA expression levels in GABAergic versus principal neurons were also observed at the protein level. There was a paucity of GluR-B/C immunoreactivity in the vast majority of somata of the GABAergic neurons studied, which contrasted with the strong expression of GluR-B/C proteins in the hippocampal principal neurons. Our results demonstrate the general low expression of the GluR-B subunit mRNA and GluR-B/C proteins in GABAergic hippocampal neurons. Considering the dominant role of the GluR-B subunit in determining the divalent ion permeability of the receptor, it is likely that most GABAergic neurons express AMPA receptor channels with different calcium permeabilities.