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.
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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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© 2008 Springer Science + Business Media, LLC
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Jacobsen, B., Kjaergaard, M., Gårdsvoll, H., Ploug, M. (2008). Structure and Inhibition of the Urokinase-Type Plasminogen Activator Receptor. In: Edwards, D., Høyer-Hansen, G., Blasi, F., Sloane, B.F. (eds) The Cancer Degradome. Springer, New York, NY. https://doi.org/10.1007/978-0-387-69057-5_34
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DOI: https://doi.org/10.1007/978-0-387-69057-5_34
Publisher Name: Springer, New York, NY
Print ISBN: 978-0-387-69056-8
Online ISBN: 978-0-387-69057-5
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