Urokinase receptor (upar/cd87) is a genuine ligand for integrins and mediates cell-cell interaction

Takehiko Tarui, Andrew P. Mazar, Douglas B. Cines, Yoshikazu Takada

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Abstract

The receptor for urokinase-type plasminogen activator (uPAR/CD87) is a 35-65 K Mr glycoprotein composed of 283 amino acid residues. It is anchored to the plasma membrane by a glycosyl phosphatidylinositol (GPI)-linkage. Binding of urokinase-type plasminogen activator (uPA) to its receptor, uPAR, regulates cellular adhesion, migration, and tumor cell invasion. It has been proposed that uPAR forms cis-interactions with integrins as an associated protein, and transduces proliferative or migratory signals to cells upon binding of uPA. However, it is still unclear how GPI-anchored uPAR, which lacks a transmembrane structure, mediates signal transduction. We found that recombinant soluble human uPAR (suPAR) synthesized in CHO cells specifically binds to recombinant human integrins a4βl,

Original languageEnglish
JournalBlood
Volume96
Issue number11 PART I
Publication statusPublished - 2000
Externally publishedYes

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ASJC Scopus subject areas

  • Hematology

Cite this

Tarui, T., Mazar, A. P., Cines, D. B., & Takada, Y. (2000). Urokinase receptor (upar/cd87) is a genuine ligand for integrins and mediates cell-cell interaction. Blood, 96(11 PART I).