Formation of oxidized HDL in atherosclerotic foci.
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We obtained a monoclonal antibody 9F 5-3 a against oxidative high-density lipoprotein (HDL) modified with CuSO4. In addition, we have examined the epitope of 9F 5-3 a and the localization of oxidized HDL (oxHDL) in atheromatous plaque. The 9F 5-3 a was reacted strongly with oxHDL and to a lesser degree with oxidized low-density lipoprotein (oxLDL) and native LDL. No reactivity was found with native HDL. Furthermore, the cross-linkage of apolipoprotein A-I and/or apolipoprotein A-II was accelerated by HDL oxidation, and the crosslinked apolipoprotein forms (32, 60, 90, 120 and 200-kDas) were selectively recognized by the 9F 5-3 a antibody. OxHDL particles reacting with the 9F 5-3 a antibody were localized histochemically in the luminal side of intima of atheromatous plaques in human abdominal aortae. Using a ligand receptor assay for oxHDL, a major 130-kDa band was detected in cultured human aortic endothelial cells. These results suggested that oxHDL particles and its putative binding protein were present in atheromatous plaques and endothelial cells, respectively.
- 日本電気泳動学会の論文
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