Urokinase plasminogen activator surface receptor (uPAR)

Urokinase plasminogen activator surface receptor (uPAR), encoded by the PLAUR gene, is a multidomain glycoprotein anchored to the cell membrane via a glycosylphosphatidylinositol (GPI) anchor[1][2]. It is the high-affinity receptor for urokinase-type plasminogen activator (uPA) and focuses plasminogen activation at the cell surface, facilitating localized pericellular proteolysis for processes including tissue remodeling, cell migration, and invasion. uPAR consists of three LU domains and belongs to the LU gene superfamily. It directly interacts with uPA, vitronectin, integrins, and is involved in key cellular events such as cell adhesion, migration, and signal transduction. uPAR is upregulated in many solid tumors, especially at invasive fronts, and elevated uPAR or soluble uPAR is associated with poor prognosis and increased metastasis risk. Soluble uPAR serves as a circulating biomarker for inflammation and a variety of diseases. While many experimental strategies for targeting uPAR have been developed, including imaging agents and cytotoxic modalities, no direct uPAR-targeted therapies are currently approved[1][2][4].

Other names

PLAURCD87UPARU-PARURKRMO3Monocyte activation antigen Mo3Urokinase-type plasminogen activator receptorurokinase receptoru-plasminogen activator receptor form 2suPAR (soluble form)

Inhibition of uPAR blocks plasminogen activation and downstream proteolysis, cell migration, and invasion; antibodies and peptide antagonists can prevent ligand binding or cell-surface localization; cytotoxic strategies target uPAR-expressing cells for elimination[2].