Molecular pharmacology and structure of VPAC Receptors for VIP and PACAP

Molecular pharmacology and structure of VPAC Receptors for VIP and PACAP VIP and PACAP are two prominent neuropeptides which share two common G protein-coupled receptors VPAC1 and VPAC2 while PACAP has an additional specific receptor PAC1. This paper reviews the present knowledge regarding three aspects of VPAC receptors including: (i) receptor specificity towards natural VIP-related peptides and pharmacology of synthetic agonists or antagonists; (ii) receptor signaling; (iii) molecular basis of ligand-receptor interaction as determined by site-directed mutagenesis, construction of receptor chimeras and structural modeling. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Regulatory Peptides Elsevier

Molecular pharmacology and structure of VPAC Receptors for VIP and PACAP

Regulatory Peptides, Volume 108 (2) – Oct 15, 2002

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Publisher
Elsevier
Copyright
Copyright © 2002 Elsevier Science B.V.
ISSN
0167-0115
eISSN
1873-1686
DOI
10.1016/S0167-0115(02)00099-X
Publisher site
See Article on Publisher Site

Abstract

VIP and PACAP are two prominent neuropeptides which share two common G protein-coupled receptors VPAC1 and VPAC2 while PACAP has an additional specific receptor PAC1. This paper reviews the present knowledge regarding three aspects of VPAC receptors including: (i) receptor specificity towards natural VIP-related peptides and pharmacology of synthetic agonists or antagonists; (ii) receptor signaling; (iii) molecular basis of ligand-receptor interaction as determined by site-directed mutagenesis, construction of receptor chimeras and structural modeling.

Journal

Regulatory PeptidesElsevier

Published: Oct 15, 2002

References

  • Pharmaceutical VIP: prospects and problems
    Gozes, I.; Fridkinb, M.; Hill, J.M.
  • Cloning and functional characterization of the human vasoactive intestinal peptide (VIP)-2 receptor
    Adamou, J.E.; Aiyar, N.; Van Horn, S.
  • Secretin and vasoactive intestinal peptide receptors: members of a unique family of G protein-coupled receptors
    Ulrich, C.D.; Holtmann, M.; Miller, L.J.
  • Development of selective agonists and antagonists for the human vasoactive intestinal polypeptide VPAC(2) receptor
    Moreno, D.; Gourlet, P.; De Neef, P.
  • VIP activates G(s) and G(i3) in rat alveolar macrophages and G(s) in HEK293 cells transfected with the human VPAC(1) receptor
    Shreeve, S.M.; Sreedharan, S.P.; Hacker, M.P.
  • Selective expression of vasoactive intestinal peptide (VIP)2/pituitary adenylate cyclase-activating polypeptide (PACAP)3 receptors in rabbit and guinea pig gastric and tenia coli smooth muscle cells
    Teng, B.; Murthy, K.S.; Kuemmerle, J.F.
  • Interaction of cA-kinase and cG-kinase in mediating relaxation of dispersed smooth muscle cells
    Murthy, K.S.; Makhlouf, G.M.
  • Highly conserved aspartate 68, tryptophane 73 and glycine 109 in the N-terminal extracellular domain of the human VIP receptor are essential for its ability to bind VIP
    Couvineau, A.; Gaudin, P.; Maoret, J.J.
  • Tryptophan 67 in the human VPAC(1) receptor: crucial role for VIP binding
    Nicole, P.; Maoret, J.J.; Couvineau, A.
  • Mutational analysis of cysteine residues within the extracellular domains of the human vasoactive intestinal peptide (VIP) 1 receptor identifies seven mutants that are defective in VIP binding
    Gaudin, P.; Couvineau, A.; Maoret, J.J.
  • Aspartate 196 in the first extracellular loop of the human VIP1 receptor is essential for VIP binding and VIP-stimulated cAMP production
    Du, K.; Nicole, P.; Couvineau, A.
  • The C-terminus ends of secretin and VIP interact with the N-terminal domains of their receptors
    Gourlet, P.; Vilardaga, J.P.; De Neef, P.
  • Properties of chimeric secretin and VIP receptor proteins indicate the importance of the N-terminal domain for ligand discrimination
    Vilardaga, J.P.; De Neef, P.; Di Paolo, E.
  • Molecular mapping of epitopes involved in ligand activation of the human receptor for the neuropeptide, VIP, based on hybrids with the human secretin receptor
    Olde, B.; Sabirsh, A.; Owman, C.
  • Vasoactive intestinal peptide modification at position 22 allows discrimination between receptor subtypes
    Gourlet, P.; Vandermeers-Piret, M.C.; Rathe, J.

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