PLAUR (plasminogen activator, urokinase receptor) functions as a cell surface receptor that binds urokinase plasminogen activator and plays crucial roles in proteolysis, cell signaling, and pathological processes. The protein localizes plasmin formation and mediates proteolysis-independent signal transduction effects 1. PLAUR demonstrates significant clinical relevance across multiple diseases. In cancer, it promotes metastasis and anoikis resistance in gastric cancer through transcriptional activation by TCF7L2 1. In hepatocellular carcinoma, PLAUR+ neutrophils drive immunotherapy resistance by creating an immunosuppressive tumor microenvironment through CD8+ T cell exclusion 2. The receptor also facilitates wound healing, being upregulated during reepithelialization processes 3. In thrombotic diseases, PLAUR+ neutrophils exhibit thrombolytic properties and contribute to thrombus resolution through a pro-resolving monocyte-neutrophil axis 4. Additionally, PLAUR signaling promotes chr19 pruritus in skin diseases like atopic dermatitis through TLR2-OSM pathways 5, and serves as a diagnostic marker for atherosclerosis progression 6. The gene shows cell-specific expression patterns regulated by endothelial-specific enhancer elements 7, making it a promising therapeutic target across diverse pathological conditions.