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- W2012089924 abstract "The binding of (3H)muscimol and (3H)GABA to thoroughly-washed subcellular particles prepared from “neurone-enriched” and astroblast primary cultures of rat brain was examined in Na+-free, Tris-citrate medium using a centrifugation assay. Competition for binding sites by excess (10−3 and 10−5M) unlabelled GABA provided estimates of “specific” binding. With 6.2 nM labelled ligand in the medium, about 37 f-moles (3H)GABA/mg protein and about 220 f-moles (3H)muscimol/mg protein were bound to particles of neurone-enriched cultures. Over a concentration range of 6.2–62 nM, (3H)muscimol binding had KB≈9 nM, BMAX≈270 f-moles/mg protein. Neither (3H)GABA nor (3H)muscimol was bound to particles prepared from cultured astroblasts of neonatal rat brain or from C6 glioma cells. (3H)Muscimol binding to particles of neurone-enriched cultures was potently inhibited by muscimol itself, GABA, isoguvacine, and 3-aminopropanesulfonic acid, and less potently inhibited by bicuculline-methobromide. β-Alanine and β-proline also had some inhibitory effect, whereas (±) nipecotic acid, L-2,4-diaminobutyric acid and picrotoxin were relatively inactive (IC501̆ mM). A similar binding of (3H)GABA and (3H)muscimol occurred to particles of a neurone-enriched culture of mouse brain. Electron-microscopic examination of neurone-enriched cultures did not reveal synaptic connections. Thus, GABA-receptors are present on neuronal membranes before the formation of most synapses. This binding of (3H)muscimol and of (3H)GABA that occurs to neuronal, but not to glial, membranes might serve as a useful “neuronal marker”." @default.
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- W2012089924 date "1980-01-01" @default.
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- W2012089924 title "Receptors for (3H)muscimol and for (3H)GABA in neurone-enriched cultures" @default.
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