O-mannosyl glycans in mammals

被引：107

作者：

Endo, T ^{[1
]}

机构：

[1] Tokyo Metropolitan Inst Gerontol, Dept Glycobiol, Itabashi Ku, Tokyo 1730015, Japan

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS | 1999年 / 1473卷 / 01期

关键词：

glycoprotein; dystroglycan; O-mannosyl glycan; laminin; sialic acid;

D O I：

10.1016/S0304-4165(99)00182-8

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：

Most proteins within living organisms contain glycans. Glycan structures can modulate the biological properties and functions of glycoproteins. The major glycans of glycoproteins can be classified into two groups, N-glycans and O-glycans, according to their glycan-peptide linkage regions. Developments in glycobiology have revealed a new type of glycosidic linkage to the peptide portion, the O-mannosyl linkage, in mammals, while so far it had been thought to be specific to yeast, This review will give an outline of the O-mannosyl glycans of mammalian glycoproteins. Since one of the most well known O-mannosyl-modified mammalian glycoproteins is dystroglycan, the functional aspects of the O-mannosyl glycan of dystroglycan will be described to help understand this new glycobiological field. (C) 1999 Elsevier Science B.V. All rights reserved.

引用

页码：237 / 246

页数：10

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