The VLDL receptor plays a key role in the metabolism of postprandial remnant lipoproteins

The VLDL receptor plays a key role in the metabolism of postprandial remnant lipoproteins
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DOI:
10.1016/j.cca.2019.05.004
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发表时间:
2019-08-01
影响因子:
5
通讯作者:
Takahashi, Sadao
Takahashi, Sadao
中科院分区:
医学3区
文献类型:
--
作者:
Nakajima, Katsuyuki;Tokita, Yoshiharu;Takahashi, Sadao

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根据脂蛋白颗粒及其受体的特性,提出了一个新的概念来解释餐后残余脂蛋白的代谢过程。用免疫分离法研究了残脂蛋白(RLP)的特性。大多数的餐后脂蛋白增加脂肪摄入后被证明是极低密度脂蛋白残留物,而不是乳糜微粒(CM)残留物,基于显着高比例的载脂蛋白B100/载脂蛋白B48的RLP和载脂蛋白B48和载脂蛋白B100的颗粒大小的高度相似性,在6小时内平行波动脂肪摄入后。VLDL受体是作为富含TG的脂蛋白代谢的受体而发现的,位于骨骼肌、脂肪组织等外周组织中,但肝脏没有餐后极低密度脂蛋白颗粒强烈结合并内化到表达极低密度脂蛋白受体的细胞中。与RLP中存在的VLDL受体结合的配体,如LPL和Lp(a)。VLDL残余物中各种特异性配体的存在可增强与VLDL受体结合的能力,VLDL受体主要起向外周组织递送能量的作用,但当过量和/或持续地保留在血浆中时,也是致动脉粥样硬化性疾病的致病因素。
A new concept to account for the process of postprandial remnant lipoprotein metabolism is proposed based on the characteristics of lipoprotein particles and their receptors. The characteristics of remnant lipoprotein (RLP) were investigated using an immuno-separation method. The majority of the postprandial lipoproteins increased after fat intake was shown to be VLDL remnants, not chylomicron (CM) remnants, based on the significantly high ratio of apoB100/apoB48 in the RLP and the high degree of similarity in the particle size of the apoB48 and apoB100 carrying lipoproteins, which fluctuate in parallel during a 6 h period after fat intake. The VLDL receptor was discovered as a receptor for TG-rich lipoprotein metabolism and is located in peripheral tissues such as skeletal muscle, adipose tissue, etc., but not in the liver. Postprandial VLDL particles are strongly bound and internalized into cells expressing the VLDL receptor. Ligands that bind to VLDL receptor, such as LPL and Lp(a), present in RLP. The presence of various specific ligands in VLDL remnants may enhance the capacity for binding to the VLDL receptor, which play the role primarily for energy delivery to the peripheral tissues, but is also a causal factor in atherogenic diseases when excessively and/or continuously remained in plasma.