P-selectin glycoprotein ligand-1 is expressed on endothelial cells and mediates monocyte adhesion to activated endothelium

Paula Da Costa Martins, Juan Jesús García-Vallejo, Johannes V. Van Thienen, Mar Fernandez-Borja, Janine M. Van Gils, Cora Beckers, Anton J. Horrevoets, Peter L. Hordijk, Jaap Jan Zwaginga*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

Abstract

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 α, interleukin-1β, 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 TNFα. 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 α-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.

Original languageEnglish
Pages (from-to)1023-1029
Number of pages7
JournalArteriosclerosis, Thrombosis, and Vascular Biology
Volume27
Issue number5
DOIs
Publication statusPublished - May 2007

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