AnxA2

Annexin A2 (AnxA2, ANXA2) is a Ca²⁺-dependent phospholipid-binding protein that participates in membrane organization, exocytosis, endocytosis, cell migration, proliferation, and cytoskeletal remodeling, establishing a central role in cellular homeostasis and membrane dynamics^[1][2][3]. Mechanistically, AnxA2 functions at the interface between membranes and the actin cytoskeleton, where it promotes actin remodeling and coordinates membrane-associated trafficking processes that are required for cell polarization and structural organization^[2][3]. At the cell surface, AnxA2 forms a heterotetrameric complex with S100A10 (p11) and contributes to plasminogen activation and fibrinolytic regulation, linking membrane signaling to extracellular proteolytic activity and vascular homeostasis^[4][5][6]. Therefore, AnxA2 is closely associated with biological processes including fibrinolysis, inflammation, tissue repair, membrane repair, and matrix remodeling^[5][6][7]. In disease settings, dysregulated AnxA2 expression or activity has been reported in vascular disorders, inflammatory diseases, kidney diseases, acute promyelocytic leukemia, and multiple cancers, where it influences inflammatory signaling, thrombosis-related pathways, and cellular invasion programs^[5][6][1][8]. Compared with related annexin family members, AnxA2 is distinguished by its well-characterized interaction with S100A10 and its prominent role in cell-surface plasmin generation, providing functional specialization within the annexin protein family^[4][9]. For experimental applications, AnxA2-targeting antibodies and other inhibitory strategies have been widely employed to investigate fibrinolysis, vascular biology, inflammation, membrane repair, and tumor-associated mechanisms, supporting its value as a mechanistic research target^[5][7][8].