Localization of a Vitronectin Binding Region of Plasminogen Activator Inhibitor-1
1995 ◽
Vol 73
(05)
◽
pp. 829-834
◽
Keyword(s):
SummaryThe PAI-1 binding site for VN was studied using two independent methods. PAI-1 was cleaved by Staph V8 protease, producing 8 fragments, only 2 of which bound to [125I]-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 and 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.
1993 ◽
Vol 70
(02)
◽
pp. 301-306
◽
1998 ◽
Vol 80
(12)
◽
pp. 942-948
◽
2006 ◽
Vol 24
(18_suppl)
◽
pp. 14596-14596
2008 ◽
Vol 100
(12)
◽
pp. 1014-1020
◽
2016 ◽
Vol 116
(12)
◽
pp. 1032-1040
◽
2007 ◽
Vol 98
(08)
◽
pp. 296-303
◽