Cation dependence of opioid receptor binding supports theory on membrane-mediated receptor selectivity.
A quantitative analysis of the binding of dynorphin A-(1-9)-nonapeptide to the opioid Kappa-receptors of the guinea pig cerebellum [Paterson et al. (1986) Proc. Natl. Acad. Sci. U.S.A. 83, 6216-6220] shows that changes in electrostatic surface accumulation of the ligand fully account for the observed suppression of binding by a series of univalent and divalent salts. Binding to mu- and delta-receptors, on the other hand, is subject to additional ion-specific effects. These observations support the membrane locations for the receptor sites proposed by the "membrane compartments" theory for opioid receptor selection.
D000465:Algorithms; D000818:Animals; D002531:Cerebellum / Q000378:metabolism; D004399:Dynorphins / Q000378:metabolism*; D006168:Guinea Pigs; D008566:Membranes / Q000378:metabolism; D010446:Peptide Fragments / Q000378:metabolism*; D011957:Receptors, Opioid / Q000378:metabolism*; D017465:Receptors, Opioid, delta; D017473:Receptors, Opioid, kappa; D017450:Receptors, Opioid, mu
D010446:Peptide Fragments; D011957:Receptors, Opioid; D017465:Receptors, Opioid, delta; D017473:Receptors, Opioid, kappa; D017450:Receptors, Opioid, mu; D004399:Dynorphins; C040238:dynorphin A (1-9)