Plasmodium falciparum-infected erythrocytes and oxidized low-density lipoprotein bind to separate domains of CD36
Plasmodium falciparum-infected erythrocytes and oxidized low-density lipoprotein bind to separate domains of CD36
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DOI：
10.1086/314897
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发表时间：
1999-08-01
影响因子：
6.4
通讯作者：
Kain, KC
中科院分区：
文献类型：
--
作者：
Crandall, I;Guy, RA;Kain, KC
红细胞的细胞粘附恶性疟原虫（pRBC）感染的红细胞（红细胞）对内皮细胞的作用以及巨噬细胞对氧化低密度脂蛋白（oxLDL）的摄取均部分由糖蛋白受体CD 36介导。通过使用表达人CD 36的中国仓鼠卵巢细胞检测脂蛋白和pRBC竞争人CD 36受体的相互作用，OxLDL竞争性抑制pRBC与CD 36的粘附，但天然LDL和高密度脂蛋白不抑制。CD 36中的赖氨酸残基的修饰抑制oxLDL和pRBC结合;然而，只有oxLDL结合受到受体碘化的抑制，只有pRBC结合受到pH变化和受体还原的影响。此外，pRBC/CD 36相互作用的肽抑制剂不影响oxLDL结合。这些结果表明，虽然oxLDL竞争性抑制pRBC的粘附，这些配体与CD 36受体上的不同结构域相互作用。
The cytoadherence of erythrocytes (red blood cells) infected with Plasmodium falciparum (pRBCs) to endothelial cells and the uptake of oxidized low-density lipoprotein (oxLDL) by macrophages are both mediated, in part, by the glycoprotein receptor CD36, The interaction of lipoproteins and pRBCs competing for the human CD36 receptor was examined by use of Chinese hamster ovary cells expressing human CD36, OxLDL competitively inhibits the adherence of pRBCs to CD36, but native LDL and high-density lipoprotein do not. Modification of Lys residues in CD36 inhibits both oxLDL and pRBC binding; however, only oxLDL binding is inhibited by receptor iodination, and only pRBC binding is influenced by pH variations and receptor reduction. Furthermore, peptide inhibitors of the pRBC/CD36 interaction do not influence oxLDL binding. These results suggest that, although oxLDL competitively inhibits the adherence of pRBCs, these ligands interact with distinct domains on the CD36 receptor.