Partial characterization of leukocyte binding molecules on endothelial cells induced by minimally oxidized LDL.

Treatment of rabbit aortic endothelial cells, human umbilical vein endothelial cells, and human aortic endothelial cells for 4 hours with minimally oxidized low-density lipoprotein (MM-LDL) induced the adhesion of monocytes but not neutrophils or lymphocytes to these cells. This induction was blocked by inhibitors of glycoprotein synthesis (cycloheximide and tunicamycin), and binding was abolished by treatment of cells with low levels of trypsin, suggesting that the binding molecule(s) is a protein. There was no increase in binding of antibodies to E-selectin, vascular cell adhesion molecule-1 (VCAM-1), or intercellular adhesion molecule-1 (ICAM-1) after treatment of cells with MM-LDL. Treatment of endothelial cells with Fab fragments of antibody to monocyte chemotactic protein-1 or to fibronectin did not block monocyte binding. Several sugars (lactose-1-phosphate, maltose-1-phosphate, and N-acetylglucosamine) inhibited monocyte binding to cells treated with MM-LDL, but binding was not blocked by mannose-6-phosphate, fructose-6-phosphate, glucose-1-phosphate, or glucose-6-phosphate. EDTA or EGTA treatment inhibited binding, which was restored by adding either calcium or magnesium. We conclude that the binding of monocytes to endothelial cells induced by a 4-hour treatment with MM-LDL is caused by a binding molecule(s) other than E-selectin, VCAM-1, or ICAM-1 and that carbohydrate chains on the monocytes or the endothelium play a role in binding.