GLYCOSYLATION OF VIP RECEPTORS - A MOLECULAR-BASIS FOR RECEPTOR HETEROGENEITY

被引：20

作者：

FABRE, C

ELBATTARI, A

KARAMANOS, Y

COUVINEAU, A

SALOMON, R

LABURTHE, M

MARVALDI, J

PICHON, J

LUIS, J

机构：

[1] UNIV AIX MARSEILLE 1,INST CHIM BIOL,CNRS,URA 202,3 PL VICTOR HUGO,F-13331 MARSEILLE 3,FRANCE

[2] UNIV LIMOGES,INST BIOTECHNOL,F-87060 LIMOGES,FRANCE

[3] UNIV PARIS 07,INSERM,U239,F-75018 PARIS,FRANCE

来源：

PEPTIDES | 1993年 / 14卷 / 03期

关键词：

VASOACTIVE INTESTINAL PEPTIDE; VIP; VIP RECEPTOR; GLYCOSYLATION; SIZE HETEROGENEITY; PROTEIN CORE; AFFINITY LABELING; GLYCOHYDROLASES; PNGASE-F; GLYCANASE; NEURAMINIDASE;

D O I：

10.1016/0196-9781(93)90136-5

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 I-125-VIP-labeled components with molecular weights ranging from M, = 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.

引用

页码：483 / 489

页数：7

共 35 条

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