[HTML][HTML] Characterization of the binding of different conformational forms of plasminogen activator inhibitor-1 to vitronectin: implications for the regulation of pericellular …
DA Lawrence, S Palaniappan, S Stefansson… - Journal of Biological …, 1997 - ASBMB
Plasminogen activator inhibitor type 1 (PAI-1), the primary physiologic inhibitor of
plasminogen activation, is associated with the adhesive glycoprotein vitronectin (Vn) in
plasma and the extracellular matrix. In this study we examined the binding of different
conformational forms of PAI-1 to both native and urea-purified vitronectin using a solid-
phase binding assay. These results demonstrate that active PAI-1 binds to urea-purified Vn
with approximately 6-fold higher affinity than to native Vn. In contrast, inactive forms of PAI-1 …
plasminogen activation, is associated with the adhesive glycoprotein vitronectin (Vn) in
plasma and the extracellular matrix. In this study we examined the binding of different
conformational forms of PAI-1 to both native and urea-purified vitronectin using a solid-
phase binding assay. These results demonstrate that active PAI-1 binds to urea-purified Vn
with approximately 6-fold higher affinity than to native Vn. In contrast, inactive forms of PAI-1 …