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

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

Research output: Contribution to journal › Article › peer-review

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 language	English
Journal	Blood
Volume	96
Issue number	11 PART I
Publication status	Published - 2000
Externally published	Yes

ASJC Scopus subject areas

Hematology

Cite this

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

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, ",

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year = "2000",

language = "English",

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journal = "Blood",

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publisher = "American Society of Hematology",

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T1 - Urokinase receptor (upar/cd87) is a genuine ligand for integrins and mediates cell-cell interaction

AU - Tarui, Takehiko

AU - Mazar, Andrew P.

AU - Cines, Douglas B.

AU - Takada, Yoshikazu

PY - 2000

Y1 - 2000

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AB - 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,

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

Abstract

ASJC Scopus subject areas

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