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Several positively charged epitopes on the surface of CXCL8 involved in the binding of the major components of endothelial glycocalyx, sulfated glycosaminoglycans (GAGs).In the present study, we aimed to test the hypothesis that the surface GAGs — heparan sulfate (HS) is a crucial prerequisite for enhancement of endothelial cell migration by CXCL8, and to explore its underlying mechanism by detecting the changes in expression of Rho-GTPases and in the organization of actin cytoskeleton after enzymatic removal of HS on human umbilical vein endothelial cells (HUVECs) by using heparinase III.Our results revealed that the reduction of wound area by CXCL8 was greatly attenuated by removal of HS. The upregulations of Rho-GTPases, including Cdc42, Rac1, and RhoA by CXCL8 were suppressed by removal of HS . The polymerization and polarization of actin cytoskeleton, and the increasing of stress fibers by CXCL8 were also abolished by heparinase III. Taken together, our results demonstrated an essential role of HS in mediating CXCL8-induced endothelial cell migration, and highlighted the biological relevance of the CXCL8 and GAGs interactions in endothelial cell migration.
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