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pubmed-article:9592058pubmed:abstractTextNoribogaine is formed in vivo by the O-demethylation of the indole alkaloid ibogaine. We report here that noribogaine acts as a full agonist at the mu-opioid receptor. Noribogaine-stimulated guanylyl 5'gamma-[35S]thio]triphosphate ([35S]GTPgammaS) was studied in rat thalamic membranes to measure activation of guanine nucleotide binding proteins (G-proteins) in the presence of excess GDP. Noribogaine caused a 170% increase above basal [35S]GTPgammaS binding at sub-micromolar effective concentrations (EC50) in a naloxone-sensitive manner, confirming that this effect was an opioid receptor-mediated process. The level of intrinsic activity for noribogaine in these assays was comparable to the full agonists DAMGO and morphine. In contrast, ibogaine had no significant effect on [35S]GTPgammaS binding over a similar concentration range. The efficacy of noribogaine as a full mu-opioid agonist may explain ibogaine's ability to block the acute signs of opiate withdrawal and its suppressive effects on morphine self-administration.lld:pubmed
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pubmed-article:9592058pubmed:articleTitleNoribogaine stimulates naloxone-sensitive [35S]GTPgammaS binding.lld:pubmed
pubmed-article:9592058pubmed:affiliationDepartment of Neurology, University of Miami School of Medicine, FL 33136, USA.lld:pubmed
pubmed-article:9592058pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:9592058pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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