Monocyte adhesion to activated aortic endothelium: role of L-selectin and heparan sulfate proteoglycans
| Autor: | N. Monai, Olivier Spertini, Y. Tardy, L. Gluffre, Marc Schapira, A.-S. Cordey |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 1997 |
| Předmět: |
Monocyte adhesion
Endothelium Immunology Perlecan Biology Ligands Heparan Sulfate Proteoglycans Monocytes Article 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine Cell Adhesion medicine Animals Humans Immunology and Allergy L-Selectin Cell adhesion Aorta Cells Cultured 030304 developmental biology 0303 health sciences Heparinase Monocyte Cell Biology Heparin Molecular biology Cell biology Sialic acid Endothelial stem cell Kinetics medicine.anatomical_structure chemistry Biochemistry 030220 oncology & carcinogenesis Aortic endothelium biology.protein cardiovascular system Cytokines Cattle Proteoglycans L-selectin Endothelium Vascular Heparitin Sulfate Animals Aorta Cattle Cell Adhesion/drug effects Cells Cultured Cytokines/pharmacology Endothelium Vascular/drug effects/*physiology Heparan Sulfate Proteoglycans Heparitin Sulfate/*physiology Humans Kinetics L-Selectin/biosynthesis/*physiology Ligands Monocytes/drug effects/*physiology Proteoglycans/*physiology 030215 immunology medicine.drug |
| Zdroj: | Journal of Cell Biology, vol. 136, no. 4, pp. 945-956 The Journal of Cell Biology |
| Popis: | This study examines the role of L-selectin in monocyte adhesion to arterial endothelium, a key pathogenic event of atherosclerosis. Using a nonstatic (rotation) adhesion assay, we observed that monocyte binding to bovine aortic endothelium at 4 degrees C increased four to nine times upon endothelium activation with tumor necrosis factor (TNF)-alpha. mAb-blocking experiments demonstrated that L-selectin mediates a major part (64 +/- 18%) of monocyte attachment. Videomicroscopy experiments performed under flow indicated that monocytes abruptly halted on 8-h TNF-alpha-activated aortic endothelium, approximately 80% of monocyte attachment being mediated by L-selectin. Flow cytometric studies with a L-selectin/IgM heavy chain chimeric protein showed calcium-dependent L-selectin binding to cytokine-activated and, unexpectedly, unactivated aortic cells. Soluble L-selectin binding was completely inhibited by anti-L-selectin mAb or by aortic cell exposure to trypsin. Experiments with cycloheximide, chlorate, or neuraminidase showed that protein synthesis and sulfate groups, but not sialic acid residues, were essential for L-selectin counterreceptor function. Moreover, heparin lyases partially inhibited soluble L-selectin binding to cytokine-activated aortic cells, whereas a stronger inhibition was seen with unstimulated endothelial cells, suggesting that cytokine activation could induce the expression of additional ligand(s) for L-selectin, distinct from heparan sulfate proteoglycans. Under flow, endothelial cell treatment with heparinase inhibited by approximately 80% monocyte attachment to TNF-alpha-activated aortic endothelium, indicating a major role for heparan sulfate proteoglycans in monocyte-endothelial interactions. Thus, L-selectin mediates monocyte attachment to activated aortic endothelium, and heparan sulfate proteoglycans serve as arterial ligands for monocyte L-selectin. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|