Glycosylation of VIP receptors: a molecular basis for receptor heterogeneity.
Apparent molecular weights of VIP-binding proteins differ greatly according to species and to tissue. In this study, we used plasma membranes from various species (human, rat, pig) and tissues (melanoma, intestine, liver), which display major 125I-VIP-labeled components with molecular weights ranging from M(r) = 51,800 to 66,800. With the exception of porcine receptor, the various VIP receptors had similar apparent molecular weights after removal of their N-linked carbohydrates. In addition to differences in the amount of asparagine-linked glycans, our results also revealed differences in the composition of the oligosaccharide chains, which can also account for the heterogeneity in the molecular weights of the VIP receptor.
Institut de Chimie Biologique, CNRS URA 202, Université de Provence, Marseille, France.
C
C
Fabre
A
A
el Battari
Y
Y
Karamanos
A
A
Couvineau
R
R
Salomon
M
M
Laburthe
J
J
Marvaldi
J
J
Pichon
J
J
Luis
D000818:Animals; D006026:Glycoside Hydrolases; D006031:Glycosylation; D006801:Humans; D007422:Intestines / Q000737:chemistry* / Q000166:cytology; D008099:Liver / Q000737:chemistry*; D008545:Melanoma; D008970:Molecular Weight; D009844:Oligosaccharides / Q000032:analysis; D051381:Rats; D011964:Receptors, Gastrointestinal Hormone / Q000737:chemistry*; D018005:Receptors, Vasoactive Intestinal Peptide; D013552:Swine; D014407:Tumor Cells, Cultured; D014660:Vasoactive Intestinal Peptide
D009844:Oligosaccharides; D011964:Receptors, Gastrointestinal Hormone; D018005:Receptors, Vasoactive Intestinal Peptide; D014660:Vasoactive Intestinal Peptide; D006026:Glycoside Hydrolases