Molecular pharmacology and structure of VPAC Receptors for VIP and PACAP (Q28200901)

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12 November 2019

review article

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title

Molecular pharmacology and structure of VPAC Receptors for VIP and PACAP (English)

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12 November 2019

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12 November 2019

M Laburthe

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12 November 2019

language of work or name

English

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publication date

1 October 2002

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12 November 2019

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12 November 2019

volume

108

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12 November 2019

issue

2-3

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12 November 2019

page(s)

165-173

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Vasoactive intestinal peptide

12 November 2019

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VIP and PACAP: very important in pain?

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VIP and PACAP in pain and inflammation

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Interactions of glucagon, gut glucagon, vasoactive intestinal polypeptide and secretin with liver and fat cell plasma membranes: binding to specific sites and stimulation of adenylate cyclase

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Interaction of Gila monster venom with VIP receptors in intestinal epithelium of human

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Interaction of GRF with VIP receptors and stimulation of adenylate cyclase in rat and human intestinal epithelial membranes. Comparison with PHI and secretin

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Interaction of PHM, PHI and 24-glutamine PHI with human VIP receptors from colonic epithelium: comparison with rat intestinal receptors.

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Pituitary adenylate cyclase activating polypeptide (PACAP) and its receptors: neuroendocrine and endocrine interaction

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Receptors for VIP, PACAP, secretin, GRF, glucagon, GLP-1, and other members of their new family of G protein-linked receptors: structure-function relationship with special reference to the human VIP-1 receptor

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Molecular identification of receptors for vasoactive intestinal peptide in rat intestinal epithelium by covalent cross-linking. Evidence for two classes of binding sites with different structural and functional properties

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Selective photolabeling of high and low affinity binding sites for vasoactive intestinal peptide (VIP): evidence for two classes of covalent VIP-receptor complexes in intestinal cell membranes

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Molecular analysis of vasoactive intestinal peptide receptors. A comparison with receptors for VIP-related peptides

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Functional expression and tissue distribution of a novel receptor for vasoactive intestinal polypeptide

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Cloning and functional expression of a human neuroendocrine vasoactive intestinal peptide receptor

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

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The VIP2 receptor: molecular characterisation of a cDNA encoding a novel receptor for vasoactive intestinal peptide

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Molecular cloning and functional characterization of a human VIP receptor from SUP-T1 lymphoblasts

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Cloning and functional characterization of the human vasoactive intestinal peptide (VIP)-2 receptor

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LNB-TM7, a group of seven-transmembrane proteins related to family-B G-protein-coupled receptors

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Secretin and vasoactive intestinal peptide receptors: members of a unique family of G protein-coupled receptors

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Cloning and expression of the human vasoactive intestinal peptide receptor

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RDC1 may not be VIP receptor

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Characterization of the RDC1 gene which encodes the canine homolog of a proposed human VIP receptor. Expression does not correlate with an increase in VIP binding sites

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7 January 2021

Two receptors for vasoactive intestinal polypeptide with similar specificity and complementary distributions

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7 January 2021

The human vasoactive intestinal peptide receptor: molecular identification by covalent cross-linking in colonic epithelium

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7 January 2021

Glycosylation of VIP receptors: a molecular basis for receptor heterogeneity.

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Stable expression of the recombinant human VIP1 receptor in clonal Chinese hamster ovary cells: pharmacological, functional and molecular properties.

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Vasoactive intestinal peptide (VIP)1 receptor. Three nonadjacent amino acids are responsible for species selectivity with respect to recognition of peptide histidine isoleucineamide.

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Development of high affinity selective VIP1 receptor agonists

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Identification of key residues for interaction of vasoactive intestinal peptide with human VPAC1 and VPAC2 receptors and development of a highly selective VPAC1 receptor agonist. Alanine scanning and molecular modeling of the peptide

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Creation of a selective antagonist and agonist of the rat VPAC(1) receptor using a combinatorial approach with vasoactive intestinal peptide 6-23 as template

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Different vasoactive intestinal polypeptide receptor domains are involved in the selective recognition of two VPAC(2)-selective ligands

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7 January 2021

The long-acting vasoactive intestinal polypeptide agonist RO 25-1553 is highly selective of the VIP2 receptor subclass

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7 January 2021

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7 January 2021

VIP activates G(s) and G(i3) in rat alveolar macrophages and G(s) in HEK293 cells transfected with the human VPAC(1) receptor

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7 January 2021

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7 January 2021

The pituitary adenylate cyclase activating polypeptide (PACAP I) and VIP (PACAP II VIP1) receptors stimulate inositol phosphate synthesis in transfected CHO cells through interaction with different G proteins

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7 January 2021

Differential activation of phospholipase D by VPAC and PAC1 receptors

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7 January 2021

Alternate coupling of receptors to Gs and Gi in pancreatic and submandibular gland cells

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7 January 2021

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

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7 January 2021

Interaction of cA-kinase and cG-kinase in mediating relaxation of dispersed smooth muscle cells

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7 January 2021

Differential regulation of phospholipase A2 (PLA2)-dependent Ca2+ signaling in smooth muscle by cAMP- and cGMP-dependent protein kinases. Inhibitory phosphorylation of PLA2 by cyclic nucleotide-dependent protein kinases

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7 January 2021

Vasoactive intestinal peptide prevents excitotoxic cell death in the murine developing brain

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7 January 2021

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.

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7 January 2021

Tryptophan 67 in the human VPAC(1) receptor: crucial role for VIP binding

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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.

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7 January 2021

Mutagenesis of N-glycosylation sites in the human vasoactive intestinal peptide 1 receptor. Evidence that asparagine 58 or 69 is crucial for correct delivery of the receptor to plasma membrane

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7 January 2021

The human VPAC1 receptor: three-dimensional model and mutagenesis of the N-terminal domain

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7 January 2021

Aspartate 196 in the first extracellular loop of the human VIP1 receptor is essential for VIP binding and VIP-stimulated cAMP production

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7 January 2021

A disulfide bond between conserved cysteines in the extracellular loops of the human VIP receptor is required for binding and activation

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Uncovering molecular mechanisms involved in activation of G protein-coupled receptors

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Two basic residues of the h-VPAC1 receptor second transmembrane helix are essential for ligand binding and signal transduction

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7 January 2021

The C-terminus ends of secretin and VIP interact with the N-terminal domains of their receptors

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Critical contributions of amino-terminal extracellular domains in agonist binding and activation of secretin and vasoactive intestinal polypeptide receptors. Studies of chimeric receptors

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7 January 2021

Properties of chimeric secretin and VIP receptor proteins indicate the importance of the N-terminal domain for ligand discrimination

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7 January 2021

Construction of chimeras between human VIP1 and secretin receptors: identification of receptor domains involved in selectivity towards VIP, secretin, and PACAP

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7 January 2021

Molecular mapping of epitopes involved in ligand activation of the human receptor for the neuropeptide, VIP, based on hybrids with the human secretin receptor

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7 January 2021

Vasoactive Intestinal Polypeptide and Pituitary Adenylate Cyclase-Activating Polypeptide Receptor Chimeras Reveal Domains That Determine Specificity of Vasoactive Intestinal Polypeptide Binding and Activation

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7 January 2021

Domains determining agonist selectivity in chimaeric VIP2 (VPAC2)/PACAP (PAC1) receptors

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7 January 2021

Vasoactive intestinal polypeptide VPAC1 and VPAC2 receptor chimeras identify domains responsible for the specificity of ligand binding and activation

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7 January 2021

Vasoactive intestinal peptide modification at position 22 allows discrimination between receptor subtypes

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7 January 2021

10.1016/S0167-0115(02)00099-X

Identifiers

DOI

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12220741%20AND%20SRC:MED&resulttype=core&format=json

12 November 2019

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12220741%20AND%20SRC:MED&resulttype=core&format=json