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Effect of Guanine Nucleotides on Dopaminergic Agonist and Antagonist Affinity for [ 3 H]Sulpiride Binding Sites in Rat Striatal Membrane Preparations
Author(s) -
Freedman S. B.,
Poat Judith A.,
Woodruff G. N.
Publication year - 1982
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1982.tb12530.x
Subject(s) - sulpiride , gtp' , chemistry , dopaminergic , agonist , cyclase , dopamine receptor , dopamine , benzamide , adenylate kinase , antagonist , spiperone , guanine , pharmacology , biochemistry , medicine , endocrinology , nucleotide , receptor , stereochemistry , biology , enzyme , gene
[ 3 H]Sulpiride bound to rat striatal membrane preparations with a saturable, high affinity component. This binding was displaced potently by dopamine antagonists (both classic neuroleptics and the benzamide, sulpiride) and less potently by dopamine agonists. GTP and its stable analogue Gpp(NH)p did not affect [ 3 H]sulpiride binding to the membranes but altered the affinity for dopaminergic agonists. This effect was specific in that antagonist binding was not affected and only GTP, GDP, and Gpp(NH)p produced the effect. Similar alterations in ligand binding affinity caused by guanine nucleotides have been observed for binding sites linked to an adenylate cyclase. Such an interpretation for the case of [ 3 H]sulpiride is contrary to suggestions that sulpiride labels only those dopamine receptors that are not cyclase linked.