LOCALIZATION OF A VITRONECTIN BINDING REGION OF PLASMINOGEN-ACTIVATOR INHIBITOR-1

被引：0
|
作者：
PADMANABHAN, J [1 ]
SANE, DC [1 ]
机构：
[1] WAKE FOREST UNIV, BOWMAN GRAY SCH MED, DEPT INTERNAL MED, WINSTON SALEM, NC 27157 USA
来源：
THROMBOSIS AND HAEMOSTASIS | 1995年 / 73卷 / 05期
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D O I：
暂无
中图分类号：
R5 [内科学];
学科分类号：
1002 ; 100201 ;
摘要：
The PAI-1 binding site for VN was studied using two independent methods. PAI-1 was cleaved by Staph V8 protease, producing 8 frag ments, only 2 of which bound to [I-125]-VN. These fragments were predicted to overlap between residues 91-130. Since PAI-2 has structural homology to PAI-1, but does not bind to vitronectin, chimeras of PAI-1 acid PAI-2 were constructed. Four chimeras, containing PAI-1 residues 1-70, 1-105, 1-114, and 1-167 were constructed and expressed in vitro. PAI-1, PAI-2, and all of the chimeras retained inhibitory activity for t-PA, but only the chimera containing PAI-1 residues 1-167 formed a complex with VN. Together, these results predict that the VN binding site of PAI-1 is between residues 115-130.
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页码：829 / 834
页数：6
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