Mild oxidation of lipoproteins increases their affinity for surfaces covered by heparan sulfate and lipoprotein lipase

被引:33
作者
Makoveichuk, E [1 ]
Lookene, A
Olivecrona, G
机构
[1] Umea Univ, Dept Med Biochem & Biophys, S-90187 Umea, Sweden
[2] Russian Acad Med Sci, Inst Expt Med, Dept Biochem, St Petersburg, Russia
[3] Estonian Acad Sci, Inst Chem Phys & Biophys, Tallinn, Estonia
关键词
surface plasmon resonance technique; THP-I monocyte-derived macrophages;
D O I
10.1006/bbrc.1998.9596
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Lipoprotein lipase (LPL) is present in cells involved in development of atherosclerosis (endothelial cells, smooth muscle cells, and macrophages). A direct involvement of LPL in atherogenesis has been suggested. Previously we used the surface plasmon resonance technique to study the interaction of lipoproteins with surfaces covered by heparan sulfate proteoglycans (HSPG) and LPL [A. Lookene et al. (1997) Biochemistry 36, 5267-5275], The binding was much increased by the presence of LPL. Here we demonstrate that mild oxidation of low-density-lipoprotein (LDL) and very-low-density lipoprotein (VLDL) in vitro increases their binding to surfaces covered by HSPG; and LPL, while extensive oxidation decreases it. Similar results were obtained with a lipid emulsion (Intralipid), indicating that oxidation-induced changes of the lipid part could explain the effects. LPL increased binding and uptake of the mildly oxidized (compared to nonoxidized) LDL by THP-I monocyte-derived macrophages, Our studies indicate that LPL has the highest affinity for mildly oxidized LDL and support its involvement in development of atherosclerosis, (C) 1998 Academic Press.
引用
收藏
页码:703 / 710
页数:8
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