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  • Title: Agonist and antagonist interactions with D1 dopamine receptors: agonist-induced masking of D1 receptors depends on intrinsic activity.
    Author: O'Boyle KM, Waddington JL.
    Journal: Neuropharmacology; 1992 Feb; 31(2):177-83. PubMed ID: 1532443.
    Abstract:
    The effects of agonist and antagonist compounds on the equilibrium binding of the D1 antagonist ligand [3H]SCH 23390 were examined in membranes from the striatum of the rat. The antagonist SK&F 83566 interacted with D1 receptors in the manner of a competitive antagonist, causing a decrease in the affinity of the binding of [3H]SCH 23390, without altering the maximum number of binding sites (Bmax). The interaction of agonist compounds with the D1 receptor appeared to be more complex. The drug SK&F 75670, a weak partial agonist, also acted competitively at D1 sites. However, agonists with moderate (SK&F 38393, CY 208-243) or full (dopamine) intrinsic activity to stimulate adenylate cyclase, interacted with D1 binding sites in a mixed competitive/non-competitive manner, causing both a decrease in ligand affinity and a decrease in Bmax. The benzazepine analogue, which also has full agonist activity, SK&F 82958, only caused a reduction in Bmax. Furthermore, there was a positive relationship between the intrinsic activity of agonists and the magnitude of the reductions in Bmax which they induced. In the presence of the GTP analogue, Gpp(NH)p, CY 208-243 no longer caused an apparent reduction in the number of receptors. These data suggests that the apparent loss of D1 receptors, induced by agonists, may result from an interaction with a guanine-nucleotide sensitive, high affinity agonist binding site and that the degree of interaction with this site depends on the intrinsic D1 activity of the agonist.
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