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VPAC1 receptor binding site: Contribution of photoaffinity labeling approach
Neuropeptides, 2010The vasoactive intestinal peptide (VIP) is a prominent 28 aminoacid neuropeptide with wide distribution in both central and peripheral nervous systems, where it plays important regulatory role in many physiological processes. VIP has a large spectrum of biological functions including exocrine secretions, hormone release, foetal development, immune ...
A, Couvineau +3 more
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PACAP and its receptor VPAC1 regulate megakaryocyte maturation: therapeutic implications
Blood, 2008Megakaryocytes and platelets express the Gs-coupled VPAC1 receptor, for which the pituitary adenylyl cyclase–activating peptide (PACAP) and the vasointestinal peptide (VIP) are agonists. We here demonstrate a regulatory role for VPAC1 signaling during megakaryopoiesis. A total of 2 patients with trisomy 18p with PACAP overexpression and transgenic mice
Kathleen, Freson +7 more
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Ontogeny of PAC1-R and VPAC1-R in the frog, Rana esculenta
Peptides, 2007The distribution of pituitary adenylate cyclase-activating polypeptide (PACAP) and PACAP receptors in the brain of amphibians has been previously described. In the present study, we have investigated the ontogeny of the selective PACAP receptor, PAC1-R, and the PACAP-vasoactive intestinal polypeptide (VIP) mutual receptor, VPAC1-R, in frog embryos by ...
M. CIARLO +4 more
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Characterization of Intestinal and Pancreatic Dysfunction in VPAC1-Null Mutant Mouse
Pancreas, 2011These studies examined the effect of homozygous deletion of vasoactive intestinal peptide receptor type 1 (VPAC1) on development and function of intestines and pancreas.Genetically engineered VPAC1-null mutant mice were monitored for growth, development, and glucose homeostasis.
Dorit, Fabricius +11 more
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VPAC1 Expression Is Regulated by FXR Agonists in the Human Gallbladder Epithelium *
Hepatology, 2005Abstract Vasoactive intestinal peptide receptor-1 (VPAC1) is the high-affinity receptor of vasoactive intestinal peptide (VIP), a major regulator of bile secretion. To better define the level at which VPAC1 stimulates bile secretion, we examined its expression in the different cell types ...
Nicolas, Chignard +6 more
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Evidence for Multiple Rat VPAC1 Receptor States with Different Affinities for Agonists
Cellular Signalling, 1999We compare the binding properties of [125I-VIP] and [125I]-Ro 25 1553 to VPAC1 receptors, expressed in stably transfected CHO cells. [125I]-VIP labelled two VPAC1 receptor states, while [125I]-Ro 25 1553 labelled selectively a limited number of high-affinity receptors.
Busto, Rebeca +4 more
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Peptides, 2004
C-terminally truncated human VPAC(1) receptors were constructed and stably transfected in Chinese hamster ovary (CHO) cells. Selected clones expressing comparable receptor densities were studied for ligand's binding properties, basal and stimulated adenylate cyclase activity. The wild-type (1-457) receptor served as reference. The binding properties of
Vertongen, Pascale +4 more
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C-terminally truncated human VPAC(1) receptors were constructed and stably transfected in Chinese hamster ovary (CHO) cells. Selected clones expressing comparable receptor densities were studied for ligand's binding properties, basal and stimulated adenylate cyclase activity. The wild-type (1-457) receptor served as reference. The binding properties of
Vertongen, Pascale +4 more
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Annals of the New York Academy of Sciences, 2006
Abstract: The human VPAC1 receptor for VIP and PACAP is a class II Gprotein–coupled receptor (GPCR).The N‐terminal ectodomain of the VPAC1 receptor plays a crucial role in VIP binding. Photoaffinity experiments clearly indicated that the 6–28 part of VIP physically interacts with the N‐terminal ectodomain. Construction of a 3D model of the N‐terminal
Alain, Couvineau +6 more
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Abstract: The human VPAC1 receptor for VIP and PACAP is a class II Gprotein–coupled receptor (GPCR).The N‐terminal ectodomain of the VPAC1 receptor plays a crucial role in VIP binding. Photoaffinity experiments clearly indicated that the 6–28 part of VIP physically interacts with the N‐terminal ectodomain. Construction of a 3D model of the N‐terminal
Alain, Couvineau +6 more
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Development of Selective Ligands for Pac1, Vpac1 and Vpac2 Receptors
2003At the time of its isolation, purification and sequencing in 1970-1972 by Said and Mutt (Said and Mutt, 1972;Mutt and Said, 1974), VIP was the third identified member of a peptide group that included secretin (Mutt et al, 1970) and glucagon (Bromer et al, 1957).
P. Robberecht +3 more
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Biochemical and Biophysical Research Communications, 2010
Vasoactive intestinal peptide (VIP) is a 28-amino acid peptide widely expressed in the body and binding three types of receptors: VPAC(1)-R, VPAC(2)-R and PAC(1)-R. Based on beneficial effects of VIP and VPAC(1)-R agonists in mouse models of several chronic inflammatory disorders, we hypothesized that activation of VIP receptors would prevent ...
Yuri, Sheikine +8 more
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Vasoactive intestinal peptide (VIP) is a 28-amino acid peptide widely expressed in the body and binding three types of receptors: VPAC(1)-R, VPAC(2)-R and PAC(1)-R. Based on beneficial effects of VIP and VPAC(1)-R agonists in mouse models of several chronic inflammatory disorders, we hypothesized that activation of VIP receptors would prevent ...
Yuri, Sheikine +8 more
openaire +2 more sources

