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Further characterization of neuropeptide Y receptor subtypes using centrally truncated analogs of neuropeptide Y: evidence for subtype- differentiating effects on affinity and intrinsic efficacy

MC Michel, W Gaida, AG Beck-Sickinger, HA Wieland, H Doods, H Durr, G Jung and G Schnorrenberg

Department of Medicine, University of Essen, Germany.

Previous attempts to classify neuropeptide Y receptor subtypes suffered from relying only on carboxyl-terminal analogs and fragments of neuropeptide Y. We have tested the potency and affinity of chemically different compounds, i.e., centrally truncated analogs of neuropeptide Y, in three Y1-like (Ca2+ mobilization in HEL cells, blood pressure increases in pithed rats, and 125I-neuropeptide Y binding in SK-N-MC cells) and two Y2-like (125I-neuropeptide Y binding to rabbit kidney membranes and presynaptic inhibition in rat vas deferens) model systems of neuropeptide Y receptors. Our data confirm the concept of two major subclasses of neuropeptide Y receptors, with some centrally truncated neuropeptide Y analogs having high affinity for Y2-like and low affinity for Y1-like neuropeptide Y receptors. Some of the truncated neuropeptide Y analogs are antagonists at Y1-like receptors and (possibly partial) agonists at Y2-like receptors. Our data also indicate that amino acid residues distal from the amino- and carboxyl- terminal ends of the peptide may subtype-selectively affect affinity and intrinsic efficacy of peptide agonists at neuropeptide Y receptors.

Volume 42, Issue 4, pp. 642-648, 10/01/1992
Copyright © 1992 by American Society for Pharmacology and Experimental Therapeutics




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Copyright © 1992 by the American Society for Pharmacology and Experimental Therapeutics