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Biochem Biophys Res Commun. 1994 Apr 29;200(2):769-76.

Human intestinal VIP receptor: cloning and functional expression of two cDNA encoding proteins with different N-terminal domains.

Author information

  • 1Unité de Neuroendocrinologie et Biologie Cellulaire Digestives, Institut National de la Santé et de la Recherche Médicale, Unité 410, Faculté de Médecine Xavier Bichat, Paris, France.

Abstract

We describe here two human VIP receptor cDNA clones isolated from a jejunal epithelial cell cDNA library. The hIVR8 cDNA encodes a human VIP receptor consisting of 460 amino acids and has seven putative transmembrane domains like other G protein-coupled receptors. When expressed in COS-7 cells, hIVR8 conferred specific [125I]VIP binding sites (dissociation constant = 0.6 nM) with displacement patterns characteristic of the human common VIP/PACAP receptor, i.e., VIP = PACAP-27 > PACAP-38 > helodermin > growth hormone-releasing factor = peptide methionineamide > secretin. It also conferred stimulation of cAMP production by VIP (half-maximal stimulation for 0.5 nM peptide). Another clone, hIVR5, encodes a 495 amino acid VIP receptor-related protein exhibiting 100% homology with the functional VIP receptor (hIVR8) over the 428 amino acids at the C-terminus but a completely divergent 67 amino acid N-terminal domain. When expressed in COS-7 cells, this VIP receptor-related protein does not bind 125I-VIP, although it is normally addressed at the plasma membrane as assessed by immunofluorescence studies.

PMID:
8179610
[PubMed - indexed for MEDLINE]
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