ITGA2B encodes integrin alpha-IIb, which heterodimerizes with beta-3 (ITGB3) to form the glycoprotein IIb/IIIa platelet receptor 1. This integrin recognizes RGD sequences in fibrinogen, fibronectin, and other extracellular matrix proteins, mediating rapid platelet aggregation essential for hemostasis 1. Upon activation, ITGA2B:ITGB3 facilitates platelet-platelet interactions through soluble fibrinogen binding, physically plugging vascular defects. The complex also mediates heterotypic cell adhesion with erythrocytes via ICAM4 binding. Loss-of-function mutations in ITGA2B cause Glanzmann thrombasthenia, an autosomal recessive bleeding disorder characterized by severe mucocutaneous hemorrhage due to defective platelet aggregation 1. Conversely, rare gain-of-function mutations in ITGA2B produce macrothrombocytopenia with increased platelet size 2. Emerging evidence suggests ITGA2B participates in non-hemostatic functions: under hypoxic conditions, ITGA2B upregulates IL-6 through ILK/NF-κB signaling and disrupts mitochondrial function, potentially contributing to high-altitude myocardial injury 3. Additionally, posttranslational modifications of ITGA2B can generate neoantigens driving autoimmunity in ankylosing spondylitis 4, and ITGA2B appears implicated in Alzheimer's disease neuropathology 5.