on February 22, 2007
Published online before print February 22, 2007, doi: 10.1161/ATVBAHA.107.140442
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Submitted on July 17, 2006
Accepted on February 6, 2007
P-Selectin Glycoprotein Ligand-1 Is Expressed on Endothelial Cells and Mediates Monocyte Adhesion to Activated Endothelium
Paula da Costa Martins ;
From the Department of Experimental Immunohematology (P.d.C.M., J.v.G., J.-J.Z.), Sanquin Research; the Department of Molecular Cell Biology and Immunology (J.-J.G.-V., M.F.-B., P.L.H.), VU Medical Center; the Department of Medical Biochemistry (J.V.v.T., A.J.H.), Academical Medical Center; the Department of Physiology (C.B.), VU Medical Center; and the Department of Immunohematology and Blood Transfusion (J.-J.Z.), Leiden University Medical Center, Leiden, The Netherlands.
* To whom correspondence should be addressed. E-mail: j.j.zwaginga{at}lumc.nl.
Objective--The purpose of this study was to investigate the presence and functionality of P-selectin glycoprotein ligand-1 (PSGL-1) on activated endothelial cells (ECs).
Methods and Results--We show here that PSGL-1 is expressed at the mRNA and protein levels in umbilical vein and microvascular ECs. Furthermore, this endothelial PSGL-1 (ePSGL-1) is functional and mediates adhesion of monocytes or platelet-monocyte complexes (PMCs) to the activated endothelium in a flow model. ePSGL-1 expression was not affected by treating ECs with inflammatory stimuli (tumor necrosis factor 
, interleukin-1
, thrombin, or histamine). However, the functional binding capacity of ePSGL-1 to monocytes or P-selectin/Fc chimera significantly increased by stimulation of the ECs with TNF. By means of a siRNA approach to specifically knock-down the genes involved in the glycosylation of PSGL-1 we could show that tumor necrosis factor -induced glycosylation of ePSGL-1 is critical for its binding capacity.
Conclusion--Our results show that ECs express functional PSGL-1 which mediates tethering and firm adhesion of monocytes and platelets to inflamed endothelium.
Key words: P-selectin glycoprotein ligand-1 • monocyte adhesion • platelet-monocyte complexes • endothelium • glycosylation
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