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• W1916809719 endingPage "54" @default.
• W1916809719 startingPage "945" @default.
• W1916809719 abstract "Previous studies have indicated that inorganic and organic cations can markedly affect parameters of the function of the N-methyl-D-aspartate receptor ionophore complex. As these effects may involve modulation of agonist binding, the purpose of our study was to investigate the stimulatory effect of mono- and divalent cations on binding properties of glutamate/N-methyl-D-aspartate recognition sites on the N-methyl-D-aspartate receptor complex, using [3H]CGP 39653 as the specific ligand for these sites. In well-washed membranes from rat brain, [3H]CGP 39653 binding sites were present at two affinity states when assayed at 10 mM HEPES-KOH buffer. About 75% of these sites were in a low-affinity state (Kd = 210 +/- 30 nM) although 25% were in a high-affinity state (Kd = 6.4 +/- 0.4 nM). Addition of mono- or divalent cations to the incubation medium stimulated [3H]CGP 39653 binding, measured at a radioligand concentration of 4 nM. Maximal increases in binding were to approximately 230 and 400% of control, in the presence of mono- and divalent cations, respectively. Values of EC50 for stimulation were 5 to 7 mM for monovalent cations and 0.2 to 0.4 mM for divalent cations. At these concentrations, cations increased the Bmax for the high-affinity population of [3H]CGP 39653 sites and decreased the Bmax for low-affinity ones. These findings suggest that, like spermidine, inorganic cations stimulate binding by converting [3H]CGP 39653 binding sites from the low- to high-affinity state." @default.
• W1916809719 created "2016-06-24" @default.
• W1916809719 creator A5019337347 @default.
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• W1916809719 date "1997-08-01" @default.
• W1916809719 modified "2023-09-23" @default.
• W1916809719 title "Two affinity states of N-methyl-D-aspartate recognition sites: modulation by cations." @default.
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• W1916809719 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/9262362" @default.
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