Monoglucosylated glycans in the secreted human complement component C3: implications for protein blosynthesis and structure

被引：41

作者：

Crispin, MDM

Ritchie, GE

Critchley, AJ

Morgan, BP

Wilson, IA

Dwek, RA

Sim, RB

Rudd, PM

机构：

[1] Univ Oxford, Dept Biochem, Oxford Glycobiol Inst, Oxford OX1 3QU, England

[2] Scripps Res Inst, Dept Mol Biol, La Jolla, CA 92037 USA

[3] Univ Wales Coll Cardiff, Coll Med, Dept Med Biochem & Immunol, Cardiff CF14 4XN, S Glam, Wales

[4] Scripps Res Inst, Skaggs Inst Chem Biol, La Jolla, CA 92037 USA

[5] Univ Oxford, Dept Biochem, MRC, Immunochem Unit, Oxford OX1 3QU, England

来源：

FEBS LETTERS | 2004年 / 566卷 / 1-3期

关键词：

complement component C3; glycosylation; monoglucosylation; calnexin; calreticulin;

D O I：

10.1016/j.febslet.2004.04.045

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：

The monoglucosylated oligomannose N-linked oligosaccharide (Glc(1) Man(9) GlcNAc(2)) is a retention signal for the calnexin-calreticulin quality control pathway in the endoplasmic reticulum. We report here the presence of such monoglucosylated N-glycans on the human complement serum glycoprotein C3. This finding represents the first report of monoglucosylated glycans on a human serum glycoprotein from non-diseased individuals. The presence of the glucose moiety in 5% of the human C3 glycoprotein suggests that this glycosylation site is sequestered within the protein and is consistent with previous studies identifying a cryptic conglutinin binding site on C3 that becomes exposed upon its conversion to iC3b. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：270 / 274

页数：5

共 45 条

[1] THE PREPARATION AND CHARACTERIZATION OF MONOCLONAL-ANTIBODIES TO HUMAN-COMPLEMENT COMPONENT C8 AND THEIR USE IN PURIFICATION OF C8 AND C8 SUBUNITS [J].