| 摘要 |
Inflammatory recruitment of leukocytes is governed by dynamic interactions of integrins with endothelial immunglobulin superfamily (IgSF) proteins. We have identified the IgSF member junctional adhesion molecule-1 (JAM-1) as a ligand of the beta2 integrin lymphocyte function-associated antigen-1 (LFA-1). Under static and physiologic flow conditions, JAM-1 contributed to LFA-1-dependent transendothelial migration of T cells and neutrophils, and also to LFA-1-mediated arrest of T cells triggered by chemokines on endothelium co-stimulated with cytokines to re-distribute JAM-1 from the tight junctions. Transfectants expressing JAM-1 supported LFA-1-mediated adhesion of leukocytes which required the membrane-proximal Ig-like domain 2 of JAM-1. Thus, JAM-1 is a counter-receptor for LFA-1 ideally situated to guide and control transmigration during leukocyte recruitment.
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