Myeloperoxidase binds to low‐density lipoprotein: potential implications for atherosclerosis

FEBS Letters

Stocker, Roland¹  Frei, Balz¹  McCall, Mark R.¹  Myzak, Melinda C.¹  Carr, Anitra C.¹ 

[1] Linus Pauling Institute, Oregon State University, 571 Weniger Hall, Corvallis, OR 97331-6512, USA

关键词: Atherosclerosis;    Low-density lipoprotein;    Myeloperoxidase;    Plasma;    ApoB;    apolipoprotein B-100;    HRP;    horseradish peroxidase;    LDL;    low-density lipoprotein;    LPO;    lactoperoxidase;    MPO;    myeloperoxidase;    TMB;    tetramethylbenzidine;    VLDL;    very low-density lipoprotein;   

DOI  :  10.1016/S0014-5793(00)02227-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Myeloperoxidase (MPO), an abundant heme enzyme released by activated phagocytes, catalyzes the formation of a number of reactive species that can modify low-density lipoprotein (LDL) to a form that converts macrophages into lipid-laden or ‘foam’ cells, the hallmark of atherosclerotic lesions. Since MPO has been shown to bind to a number of different cell types, we investigated binding of MPO to LDL. Using the precipitation reagents phosphotungstate or isopropanol, MPO co-precipitated with LDL, retaining its catalytic activity. The association of MPO with LDL was confirmed using native gel electrophoresis. MPO was also found to co-precipitate with apolipoprotein B-100-containing lipoproteins in whole plasma. No precipitation of MPO was observed in lipoprotein-deficient plasma, and there was a dose-dependent increase in precipitation following addition of LDL to lipoprotein-deficient plasma. Binding of MPO to LDL could potentially enhance site-directed oxidation of the lipoprotein and limit scavenging of reactive oxygen species by antioxidants.

【 授权许可】

Unknown