Heparin binding domain in vitronectin is required for oligomerization and thus enhances integrin mediated cell adhesion and spreading

被引：28

作者：

Chillakuri, Chandramouli R. ^{[1
]}

Jones, Celine ^{[1
]}

Mardon, Helen J. ^{[1
]}

机构：

[1] Univ Oxford, John Radcliffe Hosp, Nuffield Dept Obstet & Gynaecol, Womens Ctr, Oxford OX3 9DU, England

来源：

FEBS LETTERS | 2010年 / 584卷 / 15期

基金：

英国医学研究理事会;

关键词：

Vitronectin; Integrin; Oligomerization; Extracellular matrix; Cell adhesion; Heparin binding domain; SOMATOMEDIN-B DOMAIN; PROTEIN VITRONECTIN; HUMAN-PLASMA; IDENTIFICATION; MIGRATION;

D O I：

10.1016/j.febslet.2010.06.023

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：

Vitronectin is a multi-functional protein found predominantly as a monomer in blood and as an oligomer in the extracellular matrix. We have dissected the minimal regions of vitronectin protein needed for effective integrin dependent cell adhesion and spreading. A fragment of vitronectin containing the RGD integrin binding site showed similar binding affinity as that of full vitronectin protein to purified integrin alpha v beta 3 but had diminished cell adhesion and spreading function in vivo. We demonstrate that the oligomeric state of the protein is responsible for this effect. We provide compelling evidence for the involvement of the heparin binding domain of vitronectin in the oligomerization process and show that such oligomerization reinforces the activity of vitronectin in cell adhesion and spreading. Structured summary: MINT-7905703: Vn (uniprotkb:P04004) and Vn (uniprotkb:P04004) bind (MI:0407) by molecular sieving (MI:0071) (C) 2010 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.

引用

页码：3287 / 3291

页数：5