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- W3177185087 abstract "Plasminogen activator inhibitor-1 (PAI-1), a member of the serpin family of proteins, circulates in blood in a complex with vitronectin (VN). In the extracellular matrix, VN exists as an oligomer with altered conformation. Although the binding of PAI-1 to VN has typically been thought to follow a 1:1 stoichiometry, our lab has gathered substantial evidence to support a 2:1 stoichiometry of PAI-1 binding to VN. This two-site binding model involves an extended binding interface and leads to the oligomerization of VN. We thereby propose 1) the formation of this dual binding interface is necessary for the oligomerization of VN; 2) these oligomeric forms of VN associate more with matrix components; and 3) the oligomeric PAI-1/vitronectin complexes promote cell binding. In this study, we have used mutant forms of PAI-1 to show that disruption of the second-site interaction leads to less efficient oligomerization of VN. We have also shown that PAI-1-mediated oligomeric forms of VN exhibit increased association with specific matrix components, including Collagen-IV and Heparan Sulfate proteoglycan (HSPG). Such association promotes cellular binding to the matrix. Thus, we have characterized one of the protease-independent features of PAI-1, which affects the assembly and function of matrix-associated VN." @default.
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- W3177185087 date "2009-04-01" @default.
- W3177185087 modified "2023-09-23" @default.
- W3177185087 title "An Extended Binding Interface Spanning Two Sites for Interaction with PAI‐1 Alters the Function of Vitronectin in the Extracellular Matrix" @default.
- W3177185087 doi "https://doi.org/10.1096/fasebj.23.1_supplement.677.8" @default.
- W3177185087 hasPublicationYear "2009" @default.
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