SERPINE1 (plasminogen activator inhibitor-1) is a serine protease inhibitor with dual roles in fibrinolysis regulation and cell biology. As the primary inhibitor of tissue-type plasminogen activator (tPA) and urokinase-type plasminogen activator (uPA), SERPINE1 regulates fibrinolysis and controls blood clot degradation 1. Beyond protease inhibition, SERPINE1 independently regulates cell migration, keratinocyte migration during wound repair, and cellular senescence 1. In cancer pathology, SERPINE1 emerges as a critical driver of progression across multiple malignancies. In gastric cancer, SERPINE1 promotes metastasis through anoikis resistance via PI3K/AKT and EMT signaling, while facilitating M2 macrophage polarization and CD8+ T-cell suppression 2. SERPINE1 overexpression correlates with advanced disease stages and poor prognosis 3. Therapy-induced senescent tumor cells secrete SERPINE1-enriched extracellular vesicles that promote colorectal cancer progression through NF-κB p65 nuclear translocation 4. In gastric cancer, SERPINE1 mediates exosomal let-7g-5p transfer to macrophages, driving M2 polarization via JAK2/STAT3 activation 5. Conversely, targeting SERPINE1 with inhibitors or miR-486-5p enhances angiogenesis and wound healing in diabetic contexts 6. These findings position SERPINE1 as both a prognostic biomarker and therapeutic target in cancer and vascular disease.