Inflammation
Lp(a) carries the inflammatory chemokine MCP-1 in human plasma via oxidized phospholipids, a mechanistic study (J Lipid Res 2013)
Original title: MCP-1 binds to oxidized LDL and is carried by lipoprotein(a) in human plasma
This study examined whether monocyte chemoattractant protein-1 (MCP-1), a key chemokine in vascular inflammation, binds oxidized LDL (OxLDL) and Lp(a). OxLDL bound MCP-1 and retained its ability to recruit monocytes, an interaction abolished by mutating two basic amino acids (Arg-18, Lys-19) in MCP-1 and blocked by the antibody E06, which targets oxidized phospholipids (OxPLs). Since OxPLs are carried by Lp(a) in human plasma, the researchers found wild-type but not mutant MCP-1 bound Lp(a) in human plasma, an interaction also blocked by E06, and Lp(a) isolated from human plasma contained endogenous MCP-1 capable of inducing monocyte migration. The findings show both OxLDL and Lp(a) bind MCP-1 via oxidized phospholipids, potentially modulating monocyte trafficking during atherogenesis.
Original abstract
Lipoprotein oxidation plays an important role in pathogenesis of atherosclerosis. Oxidized low density lipoprotein (OxLDL) induces profound inflammatory responses in vascular cells, such as production of monocyte chemoattractant protein-1 (MCP-1) [chemokine (C-C motif) ligand 2], a key chemokine in the initiation and progression of vascular inflammation. Here we demonstrate that OxLDL also binds MCP-1 and that the OxLDL-bound MCP-1 retains its ability to recruit monocytes. A human MCP-1 mutant in which basic amino acids Arg-18 and Lys-19 were replaced with Ala did not bind to OxLDL. The MCP-1 binding to OxLDL was inhibited by the monoclonal antibody E06, which binds oxidized phospholipids (OxPLs) in OxLDL. Because OxPLs are carried by lipoprotein(a) [Lp(a)] in human plasma, we tested to determine whether Lp(a) binds MCP-1. Recombinant wild-type but not mutant MCP-1 added to human plasma bound to Lp(a), and its binding was inhibited by E06. Lp(a) captured from human plasma contained MCP-1 and the Lp(a)-associated endogenous MCP-1 induced monocyte migration. These results demonstrate that OxLDL and Lp(a) bind MCP-1 in vitro and in vivo and that OxPLs are major determinants of the MCP-1 binding. The association of MCP-1 with OxLDL and Lp(a) may play a role in modulating monocyte trafficking during atherogenesis.
Summary written by lp-a.org from the published abstract; figures as published. Page updated 18 August 2026. Methods.