Glycosylation of Tetraspanin Tspan-1 at Four Distinct Sites Promotes Its Transition Through the Endoplasmic Reticulum

被引:16
|
作者
Scholz, Claus-Juergen [2 ]
Sauer, Georg
Deissler, Helmut [1 ]
机构
[1] Univ Ulm, Sch Med, Dept Obstet & Gynaecol, D-89075 Ulm, Germany
[2] Univ Wurzburg, IZKF Lab Microarray Applicat, D-97070 Wurzburg, Germany
来源
PROTEIN AND PEPTIDE LETTERS | 2009年 / 16卷 / 10期
关键词
Tetraspanins; glycosylation; ovarian carcinoma cells; EGFP fusion proteins; DIFFERENTIALLY EXPRESSED GENES; MOLECULAR MARKERS; BREAST-CANCER; IDENTIFICATION; ANTIGEN; PROTEIN; PROFILES; ADENOCARCINOMA; SUPERFAMILY; PROGRESSION;
D O I
10.2174/092986609789071234
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
We showed that Tspan-1, a tetraspanin overexpressed in many human cancers, harbours oligosaccharides at all four potential N-glycosylation sites. Its most abundant form contained only mannose-rich sugar chains but two distinct glycosylation sites could also contain complex carbohydrates. Glycosylation seemed to be required for correct folding and subsequent transition through the endoplasmic reticulum.
引用
收藏
页码:1244 / 1248
页数:5
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