Different Vasoactive Intestinal Polypeptide Receptor Domains Are Involved in the Selective Recognition of Two VPAC2-Selective Ligands

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Vol. 56, Issue 6, 1280-1287, December 1999

Different Vasoactive Intestinal Polypeptide Receptor Domains Are Involved in the Selective Recognition of Two VPAC₂-Selective Ligands

Maria G. Juarranz, Jean Van Rampelbergh, Philippe Gourlet, Philippe De Neef, Johnny Cnudde, Patrick Robberecht, and Magali Waelbroeck

Department of Biochemistry and Nutrition, Faculty of Medicine, Université Libre de Bruxelles, Brussels, Belgium

A vasoactive intestinal polypeptide (VIP) analog, acylated on the amino-terminal histidine by hexanoic acid (C₆-VIP), behavedas a VPAC₂ preferring agonist in binding and functional studieson human VIP receptors, and radioiodinated C₆-VIP was a suitableligand for binding studies on wild-type and chimeric receptors.We evaluated the properties of C₆-VIP, its analog AcHis¹-VIP, and the VPAC₂-selective agonist Ro 25-1553 on the wild-typeVPAC₁ and VPAC₂ receptors and on the chimeric receptors exchangingthe different domains between both receptors. VIP had a normalaffinity and efficacy on the chimeras starting with the amino-terminalVPAC₂ receptor sequence. The binding and functional profile ofthese chimeric receptors suggested that the high affinity of Ro25-1553 for VPAC₂ receptors is supported by the amino-terminalextracellular domain, whereas the ability to prefer C₆-VIP overVIP is supported by the VPAC₂ fifth transmembrane (TM5)-EC₃ receptordomain. These results further support the hypothesis that thecentral and carboxyl-terminal regions of the peptide (modifiedin RO 25-1553) recognize the extracellular amino-terminal regiondomain, whereas the amino-terminal VIP amino acids bind to theTM receptor core. VIP had a reduced affinity and efficacy on theN-VPAC₁/VPAC₂ and on the N $right-arrow$ EC₂-VPAC₁/VPAC₂ chimeric receptors.C₆-VIP behaved as a high-affinity agonist on these constructions.The antagonists [AcHis¹,D-Phe²,Lys¹⁵,Arg¹⁶,Leu²⁷]VIP(3-7)/GRF(8-27) and VIP(5-27) had comparable affinities forthe wild-type receptors and for the two latter chimeras, supportingthe hypothesis that these chimeras were properly folded but unableto reach the high-agonist-affinity, active receptor conformationin response to VIPbinding.

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