The plasminogen activator, urokinase receptor (PLAUR, also known as uPAR), is a glycosylphosphatidylinositol (GPI)-anchored cell surface protein that plays a key role in extracellular matrix degradation, cell adhesion, migration, and signaling. It binds urokinase-type plasminogen activator (uPA), facilitating the conversion of plasminogen to plasmin, a protease critical for fibrinolysis and tissue remodeling. PLAUR is implicated in pathological processes such as cancer metastasis, inflammation, and fibrosis due to its role in promoting cell invasion and angiogenesis.
PLAUR antibodies are tools or therapeutic agents designed to target this receptor. Research-grade antibodies are widely used to study PLAUR expression in tumors or inflammatory diseases, correlating its levels with disease progression and prognosis. Therapeutically, anti-PLAUR antibodies aim to inhibit uPA-PLAUR interaction, blocking downstream proteolytic and signaling pathways (e.g., MAPK, PI3K/Akt) to suppress tumor growth or inflammatory damage. Some monoclonal antibodies, like ATN-658. have shown preclinical efficacy in cancer models. Challenges include optimizing specificity to avoid off-target effects and addressing PLAUR's complex roles in both physiological and pathological contexts. Current studies also explore PLAUR as a biomarker for targeted therapy or imaging in oncology.