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Integrin subunit alpha L (ITGAL), also known as CD11A, forms a heterodimeric complex with the beta-2 integrin (CD18/ITGB2) to make lymphocyte function-associated antigen 1 (LFA-1), a critical leukocyte cell surface receptor. LFA-1 mediates firm adhesion between leukocytes and other cells via binding to intercellular adhesion molecules (ICAM-1, -2, -3, -4) and is essential for immune cell trafficking, activation, cytotoxic function, and migration across the endothelium. Its central role in immune cell recruitment and activation underpins its function in inflammatory responses, host defense, and tumor immune surveillance. Altered expression and function of ITGAL are implicated in diseases such as autoimmune disorders, cancer, chronic inflammation, and immunodeficiency[1][2][3].
Inhibition of leukocyte adhesion and migration by blocking LFA-1/ICAM interaction Modulation of immune cell activation and infiltration
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