Lecithin-cholesterol acyltransferase (LCAT) as a plasma glycoprotein: an overview

被引:13
|
作者
Lima, VLM
Coelho, LCBB
Kennedy, JF
Owen, JS
Dolphin, PJ
机构
[1] UCL Royal Free & Univ Coll, Sch Med, Dept Med, London NW3 2PF, England
[2] Dalhousie Univ, Dept Biochem & Mol Biol, Lipoprotein Res Grp, Halifax, NS B3H 4H7, Canada
[3] Univ Birmingham, Sch Chem, Birmingham Carbohydrate & Prot Technol Grp, Birmingham B15 2TT, W Midlands, England
[4] Univ Fed Pernambuco, Dept Bioquim, BR-50670420 Recife, PE, Brazil
关键词
cholesterol; lipoproteins; N-glycosylation; serum glycoprotein; site-directed mutagenesis;
D O I
10.1016/j.carbpol.2003.09.005
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
This article reviews recent major efforts towards understanding the importance of carbohydrate chains for the physiological functioning of lecithin-cholesterol acyltransferase (LCAT), the plasma enzyme which esterifies cholesterol. The assembly of oligosaccharide chains in protein backbones is the most extensive of all the post-translational modifications, and can play a crucial role in protein folding, oligomer assembly and secretion, in regulating biological activity, as well as in clearance of glycoproteins from the bloodstream. Here, we describe modifications in LCAT-linked carbohydrate structures, arising from site-directed mutagenesis or from use of drugs and specific enzymes, which modify either the structure or the assembly of LCAT glycans, and evaluate how these help define their involvement in and importance to enzyme secretion, stability and activity. (C) 2003 Elsevier Ltd. All rights reserved.
引用
收藏
页码:179 / 191
页数:13
相关论文
共 50 条