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

研究成果: 雜誌貢獻 › 文章

摘要

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,

原文	英語
期刊	Blood
卷	96
發行號	11 PART I
出版狀態	已發佈 - 2000
對外發佈	Yes

指紋

ASJC Scopus subject areas

Hematology

引用此

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).

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

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指紋

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