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Intercellular adhesion molecule 2 (ICAM-2) is a type I transmembrane glycoprotein that belongs to the immunoglobulin superfamily and functions as a cell adhesion molecule. It is constitutively expressed on the endothelium, platelets, lymphocytes, and monocytes. ICAM-2 is a ligand for the integrin LFA-1 (lymphocyte function-associated antigen 1, CD11a/CD18), playing critical roles in immune surveillance, leukocyte recirculation, and antigen-specific immune responses. Its extracellular domain contains two Ig-like domains, which mediate integrin binding, particularly via a critical glutamic acid residue (Glu-37) that coordinates with Mg²⁺ in the LFA-1 binding pocket. Additionally, ICAM-2 is involved in spermatid adhesion in the testis, contributing to spermatogenesis, and may have roles in cancer and inflammation by mediating immune cell interactions and migration. Note: ICAM-2 is closely related to other ICAM family members (e.g., ICAM-1, ICAM-3), but its specific roles and therapeutic targeting are less established than ICAM-1. No significant misspellings or major correctness issues were found in the provided name and aliases.
Drugs or antibodies could block ICAM-2/LFA-1 interaction, thereby inhibiting leukocyte adhesion, migration, or immune activation
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