Investigating the effect of VEGF glycosylation on glycosaminoglycan binding and protein unfolding

被引：30

作者：

Brandner, B

Kurkela, R

Vihko, P

Kungl, AJ ^{[1
]}

机构：

[1] Graz Univ, Inst Pharmaceut Sci, A-8010 Graz, Austria

[2] Oulu Univ, Bioctr Oulu, FIN-90014 Oulu, Finland

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2006年 / 340卷 / 03期

关键词：

growth factor; heparin; heparan sulfate;

D O I：

10.1016/j.bbrc.2005.12.079

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：

VEGF(165) binding to endothelial cells is potentiated by glycosaminoglycans (GAGs). Here, we have investigated the impact of VEGF(165) N-glycosylation on GAG binding. Although glycosylated VEGF(165) bound to heparin with only slightly higher affinity than non-glycosylated VEGF(165), the natural ligand heparan sulfate induced a conformational change only in the glycosylated protein. Unfolding studies of the VEGF proteins indicated a stabilising effect of heparin on the growth factor structure. (c) 2005 Elsevier Inc. All rights reserved.

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收藏

页码：836 / 839

页数：4

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