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J Kuhse

Publications and source records attributed to J Kuhse.

38 records · Page 3Linked to original sources
PubMed1990

A single amino acid exchange alters the pharmacology of neonatal rat glycine receptor subunit.

Agonist activation of the inhibitory glycine receptor (GlyR) in the adult vertebrate CNS is efficiently antagonized by the alkaloid strychnine. Here, we describe a novel rat GlyR alpha subunit cDNA (alpha 2*) that generates chloride channels of low strychnine sensitivity upon expression in Xenopus oocytes. Comparison with the highly homologous human alpha 2 polypeptide and site-directed mutagenesis identified a single amino acid exchange at position 167 that causes the altered pharmacology of alpha 2* receptors. Amplification by the polymerase chain reaction revealed a strong decrease in alpha 2* mRNA abundancy during postnatal spinal cord development. These data indicate that alpha 2* represents a ligand binding subunit of the previously identified neonatal GlyR isoform of low strychnine affinity.

Amino Acid Sequence↗
PubMedDate not supplied

Differential expression of glycine receptor subunits in the retina of the rat: a study using immunohistochemistry and in situ hybridization.

Immunohistochemistry and in situ hybridization were used to study the distribution of glycine receptor (GlyR) subunits and the GlyR-associated protein gephyrin in the rat retina. Monoclonal antibodies against the alpha and beta subunits of the GlyR and gephyrin showed a strong punctate labeling pattern in the inner plexiform layer. Glycine receptor mRNAs were found in the inner nuclear layer and the ganglion cell layer. The alpha 1 subunit mRNA is predominantly present in the outer half of the INL and on some but not all ganglion cells. GlyR alpha 2 subunit mRNA is predominantly present in the inner half of the INL and on nearly all cells in the ganglion cell layer. GlyR alpha 3-, GlyR beta-, and gephyrin-mRNAs are present in the entire INL and in cells in the ganglion cell layer. The differential expression of glycine receptor subunits indicates a functional diversity of glycine receptors in the retina.

Animals↗