GABAA receptor: subunit expression in Xenopus oocytes and localization of receptor mRNAs in rat brain

Malherbe, Pari; Richards, J. G.; Séquier, J. M.; Mathews, Salima; Draguhn, Andreas; Möhler, Hanns

doi:10.1007/978-3-642-74155-5_8

Cited by 1 publication

(1 citation statement)

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“…The a-subunit of the GABA/BZR from bovine [6] and rat brain [16,17] is believed to consist of a large extracellular N-terminus followed by four transmembrane regions (Ml-M4) and a short extracellular C-terminus region. The main BZbinding protein (53 kDa) in pig brain seems to share homologies with the bovine and rat cysubunits as shown by its size.…”

Section: Discussionmentioning

confidence: 99%

Photolabeled tryptic degradation products of benzodiazepine‐binding proteins are glycopeptides Implications for localization of cleavage sites

Schmitz¹,

Reichelt²,

Möhler³

1989

FEBS Letters

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Crude synaptic membranes of avian and mammalian brain tissue were photolabeled with the benzodiazepine-receptor ligand PH]flunitrazepam and subsequently treated extensively with trypsin followed by incubation with endoglycosidase F. SDS-polyacrylamide gel electrophoresis and fluorography revealed that the final tryptic degradation product of 25 kDa in both pigeon and calf brain is deglycosylated in two steps. These results were confirmed by immunoblots of similarly pretreated membranes of pig brain using the a-subunit-specific monoclonal antibody bd-24. Benzodiazepine-receptor binding and its enhancement by GABA are largely retained after trypsinization. Based on the proposed transmembrane topology for the a-subunits of the GABA/benzodiazepine receptor, we suggest that the large N-terminal domain of benzodiazepine-binding proteins is protected against tryptic cleavage.

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Section: Discussionmentioning

confidence: 99%