Characterization of the oligosaccharide moiety of VIP receptor from the human pancreatic cell line BxPC-3.
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 M(r) = 68,200 glycoprotein, consisting of a M(r) = 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.
Fabre
C
C
Institut de Chimie Biologique, CNRS URA 202, Université de Provence, Marseille, France.
el Battari
A
A
Bellan
C
C
Pasqualini
E
E
Marvaldi
J
J
Lombardo
D
D
Luis
J
J
D000230:Adenocarcinoma / Q000737:chemistry*; D006023:Glycoproteins / Q000737:chemistry*; D006801:Humans; D009844:Oligosaccharides / Q000032:analysis; D010190:Pancreatic Neoplasms / Q000737:chemistry*; D011869:Radioligand Assay; D018005:Receptors, Vasoactive Intestinal Peptide / Q000737:chemistry*; D014407:Tumor Cells, Cultured
D006023:Glycoproteins; D009844:Oligosaccharides; D018005:Receptors, Vasoactive Intestinal Peptide