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Aim:The interactions of selectins and their ligands initiate the process of leuko-cyte migrating into inflamed tissue.P-selectin glycoprotein ligand 1 (PSGL-1) isthe best characterized ligand of selectins,and has been demonstrated to mediatethe adhesion of leukocytes to all three selectins in vivo.PSGL-1 not only func-tions as an anchor molecule to capture the leukocytes to the activated endothelialcells by its interaction with selectins,but also transduces the signals to activateleukocytes.Our present work aimed to investigate the mechanism by whichPSGL-1-mediated signal activates neutrophils and enhances the adhesion to theendothelial cells.Methods:We detected the effects of the engagement of PSGL-1with monoclonal antibodies (mAb) or P-selectin on the adhesion of neutrophils tothe recombinant intercellular adhesion molecule-1 (ICAM-1),and on the expres-sion of β_2-integrin.Additionally,the role of cytoskeleton in these process wasstudied by using inhibitor cytochalasin B.Results:The engagement of PSGL-Iincreased the expression of β_2-integrin on the surface of neutrophils and en-hanced the adhesion of neutrophils to the recombinant ICAM-1.mAb againstCD18 impaired the adhesion of PSGL-1-engaged neutrophils to ICAM-1.Moreover,the inhibitor cytochalasin B largely blocked the increase of CD 18 expression aswell as the adhesion of PSGL-1-engaged neutrophils to ICAM-1.Conclusion:The PSGL-1-transduced signals can enhance β_2-integrin-involved adhesion ofneutrophils to the recombinant ICAM-1,and this process depends on the dynam-ics of cytoskeleton.
Aim: The interactions of selectins and their ligands to the process of leuko-cyte migrating into inflamed tissue. P-selectin glycoprotein ligand 1 (PSGL-1) is the most characterized ligand of selectins, and has been demonstrated to mediate the adhesion of leukocytes to all three selectins in vivo. PSGL-1 not only func-tions as an anchor molecule to capture the leukocytes to the activated endothelial cells by its interaction with selectins, but also transduces the signals to activate leukocytes. Our present work aimed to investigate the mechanism by which PSGL- 1-mediated signal activates neutrophils and enhances the adhesion to the endothelial cells. Methods: We detected the effects of the engagement of PSGL-1 with monoclonal antibodies (mAb) or P-selectin on the adhesion of neutrophils tothe recombinant intercellular adhesion molecule-1 (ICAM -1), and on the expres-sion of β_2-integrin. Additionally, the role of cytoskeleton in these process was constructed by using inhibitor cytochalasin B. Results: The engagement of PSGL-Iincreased the expression of β_2-integrin on the surface of neutrophils and en-hanced the adhesion of neutrophils to the recombinant ICAM-1.mAb againstCD18 impaired the adhesion of PSGL-1-engaged neutrophils to ICAM-1.Moreover, the inhibitor cytochalasin B substantially blocked the increase of CD 18 expression aswell as the adhesion of PSGL-1-engaged neutrophils to ICAM-1. Conlusion: The PSGL-1-transduced signals can enhance β_2-integrin-involved adhesion ofneutrophils to the recombinant ICAM -1, and this process depends on the dynam-ics of cytoskeleton.