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      Chemokines trigger immediate beta2 integrin affinity and mobility changes: differential regulation and roles in lymphocyte arrest under flow.

      Immunity

      Time Factors, Antigens, CD18, metabolism, Cell Adhesion, Cell Membrane, Cell Movement, physiology, Cells, Cultured, Chemokine CCL19, Chemokine CCL21, Chemokine CXCL12, Chemokines, CC, pharmacology, Chemokines, CXC, Endopeptidases, Animals, Endothelium, Vascular, Humans, Intercellular Adhesion Molecule-1, Lymphocyte Function-Associated Antigen-1, Lymphocytes, cytology, drug effects, Mice, Models, Biological, Peyer's Patches, Phosphatidylinositol 3-Kinases

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          Abstract

          Chemokines trigger rapid integrin-dependent lymphocyte arrest to vascular endothelium. We show that the chemokines SLC, ELC, and SDF-1alpha rapidly induce lateral mobility and transient increase of affinity of the beta2 integrin LFA-1. Inhibition of phosphatidylinositol 3-OH kinase (PI(3)K) activity blocks mobility but not affinity changes and prevents lymphocyte adhesion to ICAM-1 immobilized at low but not high densities, suggesting that mobility enhances the frequency of encounters between high-affinity integrin and ligand but that at higher ligand density affinity changes are sufficient for arrest. Thus, chemokines trigger, through distinct signaling pathways, both a high-affinity state and lateral mobility of LFA-1 that can coordinately determine the vascular arrest of circulating lymphocytes under physiologic conditions.

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          11163192

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