How vitronectin binds PAI-1 to modulate fibrinolysis and cell migration

  title={How vitronectin binds PAI-1 to modulate fibrinolysis and cell migration},
  author={Aiwu Zhou and James A. Huntington and Navraj S. Pannu and Robin W. Carrell and Randy J Read},
  journal={Nature Structural Biology},
The interaction of the plasma protein vitronectin with plasminogen activator inhibitor-1 (PAI-1) is central to human health. Vitronectin binding extends the lifetime of active PAI-1, which controls hemostasis by inhibiting fibrinolysis and has also been implicated in angiogenesis. The PAI-1–vitronectin binding interaction also affects cell adhesion and motility. For these reasons, elevated PAI-1 activities are associated both with coronary thrombosis and with a poor prognosis in many cancers… CONTINUE READING

From This Paper

Figures, tables, and topics from this paper.
80 Citations
32 References
Similar Papers


Publications citing this paper.
Showing 1-10 of 80 extracted citations


Publications referenced by this paper.
Showing 1-10 of 32 references

Crystal structure of the extracellular segment of integrin α V β 3 in complex with an ArgGlyAsp ligand

  • J.-P. Xiong
  • Science
  • 2002

Kinetic analysis of the interaction between vitronectin and the urokinase receptor

  • Y. Okumura
  • J . Biol . Chem .
  • 2002

The proor antiangiogenic effect of plasminogen activator inhibitor 1 is dose dependent

  • L. Devy
  • FASEB J .
  • 2002

Clinical relevance of the plasminogen activator inhibitor type 1 — a multifaceted proteolytic factor

  • N. Harbeck
  • Onkologie
  • 2001

Similar Papers

Loading similar papers…