Integrin beta-3 and P-selectin (CD61 and CD62P)

Platelet glycoproteins CD61 (Integrin beta-3) and CD62P (P-selectin) are distinct cell surface proteins that play essential roles in platelet function, hemostasis, and inflammatory responses. CD61 is a key component of the Integrin alpha-IIb/beta-3 complex (GPIIb/IIIa), which undergoes a conformational change upon platelet activation to bind fibrinogen and mediate platelet aggregation [1]. CD62P is a cell adhesion molecule stored in the alpha-granules of platelets and Weibel-Palade bodies of endothelial cells; it is expressed on the cell surface upon activation to facilitate the rolling and attachment of leukocytes [2]. In clinical practice, CD61 is a primary therapeutic target for anti-thrombotic drugs such as abciximab and eptifibatide, which are used to prevent clotting during percutaneous coronary interventions [3]. CD62P is the target of crizanlizumab, a monoclonal antibody used to reduce the frequency of vaso-occlusive crises in patients with sickle cell disease by preventing platelet-leukocyte-endothelial interactions [4]. Both proteins are also widely utilized as flow cytometry biomarkers to monitor platelet activation levels in various cardiovascular and inflammatory conditions [5]. Because these molecules represent two distinct protein families—integrins and selectins—they are often studied together to provide a comprehensive view of platelet activation status.

Other names

Integrin subunit beta 3ITGB3GPIIIaPlatelet membrane glycoprotein IIIaP-selectinSELPGMP-140PADGEMGranule membrane protein 140CD61 antigenCD62P antigen

CD61-targeted drugs act as antagonists of the glycoprotein IIb/IIIa receptor, preventing the binding of fibrinogen and von Willebrand factor to activated platelets to inhibit aggregation [1, 3]. CD62P-targeted drugs are monoclonal antibodies that block P-selectin interactions with P-selectin glycoprotein ligand-1 (PSGL-1) on leukocytes, thereby preventing cell-cell adhesion and vaso-occlusion [2, 4].