Characterization of a Novel VPAC(1) Selective Agonist and Identification of the Receptor Domains Implicated in the Carboxyl-terminal Peptide Recognition

Overview

Journal Br J Pharmacol

Publisher Wiley

Specialty Pharmacology

Date 2000 Jun 24

PMID 10864888

Citations 5

Authors

J Van Rampelbergh

M G Juarranz

J Perret

A Bondue

R M Solano

C Delporte

P De Neef

P Robberecht

M Waelbroeck

Affiliations

Soon will be listed here.

Abstract

Vasoactive Intestinal Polypeptide (VIP) interacts with a high affinity to two subclasses of G protein coupled receptors named VPAC(1) and VPAC(2), and has a 3 - 10 fold preference for VPAC(1) over VPAC(2) receptors. Selective ligands for each receptor subclass were recently described. [R(16)]-PACAP (1 - 23) and [L(22)]-VIP are two selective VPAC(1) agonists. Chimaeric human VPAC(2)-VPAC(1) recombinant receptors expressed in CHO cells were used to identify the receptor domains implicated in these two selective ligands recognition. The VPAC(2) preference for [R(16)]-PACAP (1 - 27) over [R(16)]-PACAP (1 - 23) did not require the receptor's NH(2)-terminus domain but involved the whole transmembrane domain. In contrast, the selectivity of [L(22)]-VIP depended only on the presence of the NH(2) terminus and EC(2) domains of the VPAC(1) receptor. The present data support the idea that in the GPCR-B family of receptors the different selective ligands require different domains for their selectivity, and that the peptides carboxyl terminal sequence (amino acids 24 - 27) folds back on the transmembrane receptor domain, close to the peptides, aminoterminus.

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