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AMS Software Home Photo Studio 3.15 Serial Key – photofreevedownload.comLow density lipoprotein-derived phospholipase A2 activity prevents monocyte-endothelial interaction via inhibition of E-selectin-mediated endothelial cell adhesion.
Phospholipase A2 (PLA2) enzymes are reported to regulate lipoprotein metabolism and atherosclerosis. We investigated a potential role of the PLA2 isoform lipoprotein-associated PLA2 (Lp-PLA2) in monocyte-endothelial interactions and atherogenesis. We found that lipoprotein-free Lp-PLA2 (Lp-PLA2(0)) at nanomolar concentrations prevented monocyte adhesion to human umbilical vein endothelial cells, which was accompanied by inhibition of E-selectin-mediated endothelial cell adhesion (ICAM-1-mediated cell adhesion). Co-incubation of Lp-PLA2(0) and lipoprotein, both at high micromolar concentrations, resulted in potentiation of both monocyte adhesion and E-selectin-mediated cell adhesion. The protective effect of Lp-PLA2(0) was not observed in the presence of the free fatty acid oleate, but was found to be dose-dependent. No appreciable changes in E-selectin expression, monocyte adhesion receptor expression, and intracellular Ca(2+) mobilization were detected following stimulation of endothelial cells by Lp-PLA2(0) or oleate. Lp-PLA2(0) and oleate also did not affect endothelial cell proliferation or apoptosis. The protective effect of Lp-PLA2(0) was accompanied by decreased cell proliferation, induced premature senescence, and marked alterations in cell morphology. Our data suggest that Lp-PLA2(0) may be useful to prevent monocyte adhesion, inflammation, and atherogenesis, thereby contributing to the prevention of cardiovascular diseases.Q:
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