C. Fabre et al., CHARACTERIZATION OF THE OLIGOSACCHARIDE MOIETY OF VIP RECEPTOR FROM THE HUMAN PANCREATIC-CELL LINE BXPC-3, Peptides, 14(6), 1993, pp. 1331-1338
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 [I-125]VIP or [I-125]N-AcPACAP27
binding and in stimulating cAMP production was typical of the human V
IP receptor. By combining affinity labeling with glycosidase treatment
s, we have characterized the VIP receptor as a M(r) = 68,200 glycoprot
ein. consisting of a M(r) = 39,300 polypeptide core with at least thre
e N-linked oligosaccharide chains. In addition, our results revealed t
he presence of a low amount of sialic acid residues in the carbohydrat
e moiety of receptor.