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      Coexistence of GABAA and GABAB receptors on Aδ and C primary afferents

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          Most cited references 19

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          3H-baclofen and 3H-GABA bind to bicuculline-insensitive GABA B sites in rat brain.

           N Bowery,  D. Hill (1981)
          The presence of a novel receptor for the neurotransmitter gamma-aminobutyric acid (GABA) on peripheral autonomic nerve terminals and in mammalian brain slices has been described recently. This receptor differs from the classical GABA site as it is unaffected by recognized GABA antagonists such as bicuculline and is not sensitive to the majority of accepted GABA-mimetics such as 3-aminopropanesulphonic acid (3-APS) or isoguvacine. We propose to designate the classical site as the GABA A and the novel site as the GABA B receptor. The beta-p-chlorophenyl derivative of GABA, baclofen, is stereospecifically active at the GABA B site whereas it is devoid of activity at the classical GABA A3 site. We now report that high-affinity saturable binding of 3H-baclofen and 3H-GABA to the GABA B site can be detected in fragments of crude synaptic membranes prepared from rat brain. The results support the concept of a novel GABA receptor within the mammalian brain and show that GABA and baclofen can compete for the same recognition site.
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            Bicuculline, an antagonist of GABA and synaptic inhibition in the spinal cord of the cat.

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              Intracellular Ca2+ activates a fast voltage-sensitive K+ current in vertebrate sympathetic neurones.

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                Author and article information

                Journal
                British Journal of Pharmacology
                Wiley
                00071188
                February 1984
                February 1984
                July 19 2012
                : 81
                : 2
                : 327-333
                Article
                10.1111/j.1476-5381.1984.tb10082.x
                © 2012

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