Integrin subunit alpha X (ITGAX)

Integrin subunit alpha X (ITGAX, also known as CD11c) is an **integrin alpha chain** that dimerizes with the beta 2 chain (ITGB2) to form the integrin alpha X beta 2 complex (also known as complement receptor 4, CR4)[1][2][4]. This leukocyte-specific receptor mediates cell-cell interactions and adhesion, particularly during inflammatory responses[2][4]. It plays a critical role in the phagocytosis of complement-coated particles, chemotaxis, and monocyte/neutrophil adhesion to the endothelium[1][2]. CD11c is highly expressed on human dendritic cells, as well as monocytes, macrophages, neutrophils, and some B cells, and is widely used as a **marker for dendritic cells** and to aid classification in hematologic malignancies such as hairy cell leukemia[2][4]. ITGAX also participates in angiogenesis and is involved in immune modulation and leukocyte recruitment[1][4][6]. The only approved drug that directly targeted ITGAX is efalizumab, a monoclonal antibody withdrawn from the market due to safety concerns related to immunosuppression and risk of infection[4].

Other names

CD11cIntegrin alpha-XLeukocyte adhesion glycoprotein p150,95 alpha chainLeukocyte adhesion receptor p150,95CD11 antigen-like family member CLeu M5Complement component 3 receptor 4 subunitMyeloid membrane antigenITAXp150,95 alpha chain

Antibody targeting leads to inhibition of integrin-mediated cell adhesion and migration[4]