Abstract
This review focuses on HDL function in modulating LDL oxidation and LDL-induced inflammation. Dysfunctional HDL has been identified in animal models and humans with chronic inflammatory diseases including atherosclerosis. The loss of antiinflammatory function correlated with a loss of function in reverse cholesterol transport. In animal models and perhaps in humans, dysfunctional HDL can be improved by apoA-I mimetic peptides that bind oxidized lipids with high affinity.
Highlights
This review focuses on HDL function in modulating LDL oxidation and LDL-induced inflammation
We reported that cultures of human aortic endothelial cells and smooth muscle cells could oxidize LDL even in the presence of antioxidant containing serum inducing the cells to produce monocyte chemoattractant-1 (MCP-1) [6]
HDL-associated enzymes was reduced in rabbits and humans during the course of an acute phase reaction, resulting in HDL that increased cell-mediated LDL oxidation and increased MCP-1 production
Summary
This review focuses on HDL function in modulating LDL oxidation and LDL-induced inflammation. HDL-associated enzymes was reduced in rabbits and humans during the course of an acute phase reaction, resulting in HDL that increased cell-mediated LDL oxidation and increased MCP-1 production. We reported [10] that apolipoprotein (apo)A-I and an apoA-I peptide mimetic removed seeding molecules from human LDL, rendering the LDL resistant to oxidation by human artery wall cells.
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