Integrin alpha subunit (ITGA)

Integrin alpha subunits are type I transmembrane glycoprotein receptors that pair noncovalently with integrin beta subunits to form integrin heterodimers. These receptors are fundamental to cell-extracellular matrix and cell-cell adhesion, influencing cell survival, migration, proliferation, and immune cell trafficking[1][2][3][4][5][7][8][9]. Structurally, the α subunit contains a seven-bladed β-propeller domain, often with a ~200 amino acid inserted (I) domain involved in ligand recognition (collagens, cell-adhesion molecules)[1][2][5][6][9]. There are 18 distinct α subunits in mammals, each defining the ligand specificity and biological function of the resulting integrin. Integrin α subunits are widely implicated in diseases involving abnormal cell adhesion or migration, including cancer, inflammation, and autoimmune disorders[5][9]. Therapeutics targeting these subunits/blocking integrin function are approved or in late-stage clinical trials for conditions such as multiple sclerosis, Crohn’s disease, and acute coronary syndromes. Safety concerns largely relate to immune suppression and hemostatic disturbance, reflecting the central evolutionary role of integrins in tissue architecture and immune surveillance[5].

Other names

CD antigens (e.g., CD49a-f, CD11a/c, CD41)VLA1-6 (for "Very Late Antigen")gene names ITGA1-11ITGALITGAMITGAVITGA2BITGAXITGAEITGAD

Inhibition of integrin/ligand binding (blocks adhesion and migration) Interference with intracellular signaling downstream of integrins Induction of cell detachment or apoptosis Blockade of immune cell transmigration