Ramprasad M P, Li R, Gianturco S H, Bradley W A
University of California at San Diego, USA.
Biochem Biophys Res Commun. 1995 May 16;210(2):491-7. doi: 10.1006/bbrc.1995.1687.
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 M(r) approximately 200 kDa and M(r) approximately 235 kDa which are converted into a single ligand binding species of intermediate mobility upon reduction. We now report a approximately 1200-fold purification of the reduced candidate receptor protein from cultured THP-1 monocytes.
此前我们报道过，人血源性细胞以及THP-1单核细胞 - 巨噬细胞具有一个载脂蛋白E和脂蛋白脂肪酶非依赖性、高亲和力、特异性结合位点，用于摄取和降解高甘油三酯血症的极低密度脂蛋白（VLDL）和血浆乳糜微粒，该位点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，《脂质研究杂志》35:1674 - 1687，1994）。配体印迹分析确定了两种细胞表面、结构相关的膜结合蛋白作为受体候选物，分子量约为200 kDa和235 kDa，还原后转化为单一的具有中间迁移率的配体结合物种。我们现在报道从培养的THP-1单核细胞中对还原后的候选受体蛋白进行了约1200倍的纯化。
