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XB-ART-25567
EMBO J 1990 Oct 01;910:3261-7. doi: 10.1002/j.1460-2075.1990.tb07525.x.
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Structural and functional characterization of the gamma 1 subunit of GABAA/benzodiazepine receptors.

Ymer S , Draguhn A , Wisden W , Werner P , Keinänen K , Schofield PR , Sprengel R , Pritchett DB , Seeburg PH .


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The GABAA receptor gamma 1 subunit of human, rat and bovine origin was molecularly cloned and compared with the gamma 2 subunit in structure and function. Both gamma subunit variants share 74% sequence similarity and are prominently synthesized in often distinct areas of the central nervous system as documented by in situ hybridization. When co-expressed with alpha and beta subunits in Xenopus oocytes and mammalian cells, the gamma variants mediate the potentiation of GABA evoked currents by benzodiazepines and help generate high-affinity binding sites for these drugs. However, these sites show disparate pharmacological properties which, for receptors assembled from alpha 1, beta 1 and gamma 1 subunits, are characterized by the conspicuous loss in affinity for neutral antagonists (e.g. flumazenil) and negative modulators (e.g. DMCM). These findings reveal a pronounced effect of gamma subunit variants on GABAA/benzodiazepine receptor pharmacology.

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Species referenced: Xenopus
Genes referenced: gabarap

References [+] :
Adler, Evidence for gamma-aminobutyric acid modulation of ovarian hormonal effects on luteinizing hormone secretion and hypothalamic catecholamine activity in the female rat. 1986, Pubmed