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Characterization of the oligosaccharide moiety of VIP receptor from the human pancreatic cell line BxPC-3 |
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| Authors: | Catherine Fabre, Assou El Battari, Catherine Bellan, Eric Pasqualini, Jacques Marvaldi, Dominique Lombardo,Jos Luis |
| Affiliation: | * Institut de Chimie Biologique, CNRS URA 202, Université de Provence, 3 place Victor Hugo, 13331, Marseille cedex 3, France † Faculté de Médecine, INSERM U260, 27 Bd Jean Moulin, 13385, Marseille cedex 5, France |
| Abstract: | The human pancreatic cell line BxPC-3 displays two classes of binding sites with high and low affinity for VIP. The order of potency of VIP-related peptides in inhibiting either [125I]VIP or [125I]N-AcPACAP27 binding and in stimulating cAMP production was typical of the human VIP receptor. By combining affinity labeling with glycosidase treatments, we have characterized the VIP receptor as a Mr = 68,200 glycoprotein, consisting of a Mr = 39,300 polypeptide core with at least three N-linked oligosaccharide chains. In addition, our results revealed the presence of a low amount of sialic acid residues in the carbohydrate moiety of receptor. |
| Keywords: | Vasoactive intestinal peptide VIP receptor PACAP Glycosylation Carbohydrate chains Pancreatic cancer |
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