Immunological properties of apoB-containing lipoprotein particles in human atherosclerotic arteries.

In this study, we have documented immunochemical properties of apolipoprotein (apo) B-containing particles (LpB) extracted from human atherosclerotic lesions obtained during vascular reconstructive surgery of patients. These properties were compared to those of particles purified from corresponding atherosclerotic plasma and healthy control plasma. LpB immunoreactivities were tested in solid phase competitive binding radioimmunoassays using five anti-apoB monoclonal antibodies (MAb) for which epitopes have been previously located on the protein. The regions encompassed amino acids 405 to 539 (MAb B1), 1854 to 1879 (MAb B4), 3506 (MAb BA11), and 4355 (MAb BL3). The fifth antibody (MAb BL5) recognizes a conformationally expressed epitope. LpB from lesions presented a significantly decreased immunoreactivity as compared to LpB from respective plasma except for the epitope recognized by MAb BA11 located precisely in the low density lipoprotein (LDL) receptor binding site. The accessibility of the four sequential epitopes was similar on LpB from atherosclerotic and healthy plasma while it was decreased for the conformational one in LpB from atherosclerotic samples. These altered immunoreactivities were not related to changes in chemical composition of LpB as this was quite comparable in all preparations. With regard to electronegativity, apoB fragmentation, immunological accessibility, and size distribution of the particles, changes seem to increase in the following order from healthy plasma, atherosclerotic plasma, and the corresponding lesions. The results confirm some structural characteristics of oxidatively modified particles from human atherosclerotic lesions and to a lesser degree from respective plasma, but more specifically demonstrate a global conformational change in LpB from lesions, this change being perhaps initiated in the plasma.