Tanaka A
Third Department of Internal Medicine, Tokyo Medical and Dental University.
Nihon Rinsho. 1999 Dec;57(12):2711-6.
Unique candidate receptor membrane binding proteins, MBP 200 and 235, were identified in human monocyte-macrophages. The MBP binds and internizes chylomicrons, triglyceride (TG)-rich VLDL, and VLDL devoid of apo E, but not acetyl LDL, via a domain in apo B48. The MBP is named apo B48 receptor because the receptor-binding domain is within apo B48. The apo B48 receptor differs from the scavenger receptor family and LDL receptor family because it does not bind acetyl LDL and it binds VLDL devoid of apo E by an apo E-independent mechanism. Immunohisto-chemical studies indicate colocalization of anti-apo B48 receptor Ab and monocyte-macrophage specific Ab in human atherosclerotic lesion foam cells. This suggests that apo B48 receptor may contribute to foam cell formation and atherosclerosis in abnormal state with elevated TG-rich lipoproteins.
在人类单核细胞 - 巨噬细胞中鉴定出了独特的候选受体膜结合蛋白MBP 200和235。MBP通过载脂蛋白B48中的一个结构域结合并内化乳糜微粒、富含甘油三酯（TG）的极低密度脂蛋白（VLDL）以及不含载脂蛋白E的VLDL，但不结合乙酰化低密度脂蛋白（acetyl LDL）。由于受体结合结构域位于载脂蛋白B48内，因此该MBP被命名为载脂蛋白B48受体。载脂蛋白B48受体不同于清道夫受体家族和低密度脂蛋白受体家族，因为它不结合乙酰化低密度脂蛋白，并且通过不依赖载脂蛋白E的机制结合不含载脂蛋白E的VLDL。免疫组织化学研究表明，抗载脂蛋白B48受体抗体与单核细胞 - 巨噬细胞特异性抗体在人类动脉粥样硬化病变泡沫细胞中共定位。这表明在富含TG的脂蛋白升高的异常状态下，载脂蛋白B48受体可能有助于泡沫细胞的形成和动脉粥样硬化。
