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Structure and Inhibition of the Urokinase-Type Plasminogen Activator Receptor

  • Benedikte Jacobsen
  • Magnus Kjaergaard
  • Henrik Gårdsvoll
  • Michael Ploug

Abstract

The urokinase-type plasminogen activator receptor (uPAR/CD87) is a glycolipid-anchored receptor that is involved in focalizing plasminogen activation to the cell surface due to its high-affinity binding to the urokinase-type plasminogen activator (uPA). This chapter describes recent accomplishments in the molecular understanding of the structural biology of uPAR and its interactions with the cognate ligands, uPA and vitronectin. Furthermore, the structural basis for the pharmacological inhibition of uPAR by monoclonal antibodies, recombinant fusion proteins, and synthetic peptide antagonists are discussed. These compounds may prove valuable as drug candidates in combined intervention strategies targeting tumor invasion and metastasis.

Keywords

Plasminogen Activator Plasminogen Activation Urokinase Plasminogen Activator Peptide Antagonist Urokinase Plasminogen Activator Receptor 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Abbreviations

ANS

8-anilino-1 -naphthalene sulfonate

ATF

Amino-terminal fragment

GFD

Growth factor-like domain

GPI

Glycosylphosphatidylinositol

LU

Ly-6/uPAR

mAb

Monoclonal antibody

PNH

Paroxysmal nocturnal hemoglobinuria

SMB

Somatomedin B

tPA

Tissue-type plasminogen activator

uPA

Urokinase-type plasminogen activator

uPAR

uPA receptor

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Copyright information

© Springer Science + Business Media, LLC 2008

Authors and Affiliations

  • Benedikte Jacobsen
    • 1
  • Magnus Kjaergaard
    • 1
  • Henrik Gårdsvoll
    • 1
  • Michael Ploug
    • 1
  1. 1.Finsen Laboratory Section 3735Copenhagen Biocenter, RigshospitaletCopenhagen NDenmark

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