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.
引用
收藏
页码：836 / 839
页数：4
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