Purification of the human THP-1 monocyte-macrophage triglyceride-rich lipoprotein receptor.
Purification of the human THP-1 monocyte-macrophage triglyceride-rich lipoprotein receptor.
复制标题
纯化人 THP-1 单核巨噬细胞富含甘油三酯的脂蛋白受体。
DOI：
10.1006/bbrc.1995.1687
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发表时间：
1995
期刊：
影响因子：
--
通讯作者：
Bradley,WA
中科院分区：
文献类型：
--
作者：
Ramprasad,MP;Li,R;Gianturco,SH;Bradley,WA
此前，我们报道了人血传播和THP-1单核巨噬细胞具有载脂蛋白E-和脂蛋白脂酶不依赖的、高亲和力的特异性结合部位，用于摄取和降解高甘油三酯的极低密度脂蛋白和血浆乳糜粒，不同于低密度脂蛋白受体基因家族和乙酰低密度脂蛋白受体(Gianturco等人，J.Lipid Res.35：1674-1687,1994)。配基印迹分析确定两个细胞表面结构相关的膜结合蛋白是MR∼200 kDa和MR∼235 kDa的候选受体，它们在还原时被转化为具有中等迁移率的单一配体结合物种。我们现在报道一种从培养的∼-1单核细胞中纯化减少的候选受体蛋白的THP1200倍。
Previously we reported that human blood-borne and THP-1 monocyte-macrophages have an apolipoprotein E- and lipoprotein lipase-independent, high affinity, specific binding site for the uptake and degradation of hypertriglyceridemic VLDL and plasma chylomicrons distinct from the LDL receptor gene family and the acetyl LDL receptor (Gianturco et al., J. Lipid Res. 35:1674-1687, 1994). Ligand blot analyses identified two cell-surface, structurally related membrane binding proteins as receptor candidates of Mr∼200 kDa and Mr∼235 kDa which are converted into a single ligand binding species of intermediate mobility upon reduction. We now report a ∼1200-fold purification of the reduced candidate receptor protein from cultured THP-1 monocytes.