10 research outputs found
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Differential localization of two alternatively spliced GABA-A receptor gamma2-subunit messenger RNSs in the chick brain
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Distribution of the GABA-A receptor alpha1- and gamma2-subunit messenger RNAs in chick brain
We have used sequence-specific oligonucleotide probes and in situ hybridisation histochemistry to examine the distribution of the GABAA receptor alpha 1- and gamma 2-subunit mRNAs in serial sections of 1-day-old chick brain. Both transcripts are present together, at high levels, in many brain regions. Differences are found, however, in the relative amounts of these mRNAs in two isthmic nuclei of the optic lobe, the deep cerebellar nuclei, and the dorsal thalamus. We therefore conclude that while the alpha 1 and gamma 2 subunits predominantly occur together in the same receptor complex, they may also be found separately in other GABAA receptor subtypes
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Molecular biology of (gamma-aminobutyric acid)A receptors: multiple approaches to the study of functional domains
No abstract available
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The chicken GABA(A) receptor alpha1 subunit - cDNA sequence and localization of the corresponding messenger RNA
We report the sequence of a complementary DNA (cDNA) that encodes the chicken GABA(A) receptor alpha-1 subunit, which is extremely homologous to mammalian alpha-1 subunits. The distribution of alpha-1 subunit transcripts is shown to correlate mainly, but not completely, with the previously-reported pattern of benzodiazepine type I (BZI) binding sites in the avian brain. These results suggest that the alpha-1 subunit may not necessarily be restricted to receptors having BZI pharmacology
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The chicken GABA-A receptor - cDNA cloning and structural analysis of the Alpha 1-subunit gene promoter
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The structure and expression of the GABAA receptor as deduced by molecular genetic studies
It is well established that the inhibitory neurotransmitter γ-aminobutyric acid (GABA) mediates many of its effects by binding to the GABAA receptor, which is present on the majority of mammalian brain neurons (Enna, 1983), resulting in the opening of an integral chloride channel. This receptor has considerable pharmaceutical importance as it contains binding sites for anti-convulsant (barbiturates), anxiogenic (β-carbolines) and convulsant (picrotoxin) drugs (reviewed in Turner and Whittle, 1983; Olsen and Venter, 1986). Although it is known that anxiolytic agents such as benzodiazepines also bind to the GABAA receptor, there exists a population of benzodiazepine-insensitive receptors (Study and Barker, 1981; Unnerstall etal., 1981; de Bias etal., 1988). Our understanding of the molecular structure and function of this receptor complex has been greatly increased by the application of recombinant DNA methodology and the subsequent cloning and expression of cDNA clones that encode its constituent subunits. This chapter will review these advances and describe some recent results arising from the use of the cloned sequences
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Genes for the GABA(A) receptor subunit types and their expression
No abstract available