Annexin V-heparin oligosaccharide complex suggests heparan sulfate-mediated assembly on cell surfaces

被引：99

作者：

Capila, I

Hernaiz, MJ

Mo, YD

Mealy, TR

Campos, B

Dedman, JR

Linhardt, RJ

Seaton, BA ^{[1
]}

机构：

[1] Boston Univ, Sch Med, Dept Physiol & Biophys, Boston, MA 02118 USA

[2] Univ Iowa, Dept Chem & Biochem Engn, Iowa City, IA 52242 USA

[3] Univ Cincinnati, Coll Med, Dept Cellular & Mol Physiol, Cincinnati, OH 45220 USA

[4] Univ Iowa, Div Med & Nat Prod Chem, Dept Chem, Iowa City, IA 52242 USA

来源：

STRUCTURE | 2001年 / 9卷 / 01期

关键词：

D O I：

10.1016/S0969-2126(00)00549-9

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：

Background: Annexin V, an abundant anticoagulant protein, has been proposed to exert its effects by self-assembling into highly ordered arrays on phospholipid membranes to form a protective anti-thrombotic shield at the cell surface. The protein exhibits very high-affinity calcium-dependent interactions with acidic phospholipid membranes, as well as specific binding to glycosaminoglycans (GAGs) such as heparin and heparan sulfate, a major component of cell surface proteoglycans. At present, there is no structural information to elucidate this interaction or the role it may play in annexin V function at the cell surface.

引用

页码：57 / 64

页数：8

共 44 条

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