Pathophysiology of secretary form of VLDL receptor

体内和体外研究表明，VLDL受体结合富tg脂蛋白（TGRL）而不结合LDL，并且即使LDL受体结合TGRL和LDL，也作为外周脂蛋白受体发挥作用。两种VLDL受体蛋白（1型和2型）通过不同的剪接机制产生。我们发现缺乏o -连接糖结构域的2型VLDL受体对TGRL的亲和力低于1型VLDL受体。1型VLDL受体在单核-巨噬细胞分化和生长过程中主要表达。将2型VLDL受体分泌到培养基中，建立了测定人VLDL受体秘书形态（sVLDL-R）的方法。糖尿病患者sVLDL-R水平高于健康对照组。

In vivo and in vitro studies have shown that the VLDL receptor bind TG-rich lipoprotein (TGRL) but not LDL and function as a peripheral lipoprotein receptor even though the LDL receptor bind both TGRL and LDL. Two VLDL receptor proteins (type1 and type2) are produced by alternative splicing mechanism. We elucidated that type2 VLDL receptor lacking the O-linked sugar domain bound lower affinity for TGRL than type1 VLDL receptor. Type1 VLDL receptor was expressed predominantly during monocyte-macrophage differentiation and growth. Type2 VLDL receptor was secreted into medium and we established the method for measurement of human secertary form of VLDL receptor (sVLDL-R). Level of human sVLDL-R in diabetes was higher than healthy control.