Antipsychotics lack alpha 1A/B adrenoceptor subtype selectivity in the rat.
Article Details
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Cahir M, King DJ
Antipsychotics lack alpha 1A/B adrenoceptor subtype selectivity in the rat.
Eur Neuropsychopharmacol. 2005 Mar;15(2):231-4.
- PubMed ID
- 15695070 [ View in PubMed]
- Abstract
The alpha1A- and alpha1B-adrenoceptor affinity of the typical (chlorpromazine, haloperidol, pimozide, thioridazine and trifluoperazine) and atypical (clozapine, olanzapine, quetiapine, risperidone and sertindole) antipsychotics was determined by competition binding at alpha1A- and alpha1B-adrenoceptors in rat submaxillary gland and liver. Although all antipsychotics bound to both subtypes with relatively high affinity (K(i)s<74 nM), none were selective (>10-fold). Comparison with published dopamine D2 receptor affinities suggests that antipsychotic blockade of alpha1A- and/or alpha1B-adrenoceptors may contribute to the antipsychotic activity of all the atypical and several of the typical antipsychotics examined.
DrugBank Data that Cites this Article
- Drug Targets
Drug Target Kind Organism Pharmacological Action Actions Acepromazine Alpha-1A adrenergic receptor Protein Humans UnknownAntagonistDetails Acepromazine Alpha-1B adrenergic receptor Protein Humans UnknownAntagonistDetails Chlorpromazine Alpha-1A adrenergic receptor Protein Humans YesAntagonistDetails Chlorpromazine Alpha-1B adrenergic receptor Protein Humans YesAntagonistDetails Thioproperazine Alpha-1A adrenergic receptor Protein Humans YesAntagonistDetails Thioproperazine Alpha-1B adrenergic receptor Protein Humans YesAntagonistDetails Thioridazine Alpha-1A adrenergic receptor Protein Humans YesAntagonistDetails Thioridazine Alpha-1B adrenergic receptor Protein Humans YesAntagonistDetails Trifluoperazine Dopamine D2 receptor Protein Humans YesAntagonistDetails