Chloride ions preferentially mask high-affinity GABA binding sites.
Chloride ions (Cl-) act to regulate the appearance of gamma-aminobutyric acid (GABA) binding sites in synaptic membranes from bovine retinas. Scatchard analysis indicates that the presence of Cl- results in a preferential decrease (85%) in the number of high-affinity binding sites, with no statistically significant change in the affinity (KD) of either the high- or low-affinity sites. The finding that the appearance of this binding site is altered by the presence of Cl- may indicate that Cl- acts, either directly or indirectly, to regulate the appearance, and hence function, of the high-affinity GABA receptor.
D000818:Animals; D000838:Anions; D002417:Cattle; D002712:Chlorides / Q000494:pharmacology*; D011963:Receptors, GABA-A / Q000187:drug effects / Q000378:metabolism*; D012160:Retina / Q000378:metabolism*; D013570:Synaptic Membranes / Q000378:metabolism*; D005680:gamma-Aminobutyric Acid / Q000378:metabolism
D000838:Anions; D002712:Chlorides; D011963:Receptors, GABA-A; D005680:gamma-Aminobutyric Acid