Abstract
THE leukocyte adhesion molecule LFA-1 mediates a wide range of lymphocyte, monocyte, natural killer cell, and granulocyte interactions with other cells in immunity and inflammation1,2. LFA-1 (CD 1 la/CD 18) is a receptor for intercellular adhesion molecule 1 (ICAM-1, CD54), a surface molecule which is constitu-tively expressed on some tissues and induced on others in inflammation3–5. Induction of ICAM-1 on epithelial cells, endothelial cells and fibroblasts mediates LFA-1-dependent adhesion of lymphocytes4,6,7. Several lines of evidence have suggested the existence of a second LFA-1 ligand: homotypic adhesion of one cell line was inhibited by a monoclonal antibody to LFA-1, but not by one to ICAM-18; there exists an LFA-1-dependent, ICAM-1-indepen-dent pathway of adhesion to endothelial cells6; and also, there are some types of target cells in which LFA-1-dependent T-lymphocyte adhesion and lysis are independent of ICAM-19. We have cloned this second ligand, designated ICAM-2, using a novel method for identifying ligands of adhesion molecules. ICAM-2 is an integral membrane protein with two immunoglobulin-like domains, whereas ICAM-1 has five10,11. Remarkably, ICAM-2 is much more closely related to the two most N-terminal domains of ICAM-1 (34% identity) than either ICAM-1 or ICAM-2 is to other members of the immunoglobulin superfamily, demonstrating the existence of a subfamily of immunoglobulin-like ligands that bind the same integrin receptor.
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Staunton, D., Dustin, M. & Springer, T. Functional cloning of ICAM-2, a cell adhesion ligand for LFA-1 homologous to ICAM-1. Nature 339, 61–64 (1989). https://doi.org/10.1038/339061a0
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DOI: https://doi.org/10.1038/339061a0
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