Characterization of the binding of different conformational forms of plasminogen activator inhibitor-1 to vitronectin. Implications for the regulation of pericellular proteolysis.

@article{Lawrence1997CharacterizationOT,
  title={Characterization of the binding of different conformational forms of plasminogen activator inhibitor-1 to vitronectin. Implications for the regulation of pericellular proteolysis.},
  author={Daniel A Lawrence and Shanthi Palaniappan and Steingrimur Stefansson and Steven T Olson and A M Francis-Chmura and Joseph D. Shore and David Ginsburg},
  journal={The Journal of biological chemistry},
  year={1997},
  volume={272 12},
  pages={7676-80}
}
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… CONTINUE READING