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首页> 外文期刊>Biochemistry >Remnant high density lipoprotein(2) particles produced by hepatic lipase display high-affinity binding and increased endocytosis into a human hepatoma cell line (HEPG(2))
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Remnant high density lipoprotein(2) particles produced by hepatic lipase display high-affinity binding and increased endocytosis into a human hepatoma cell line (HEPG(2))

机译：肝脂肪酶产生的残留高密度脂蛋白（2）颗粒显示出高亲和力结合，并增加了人类肝癌细胞系（HEPG（2））的内吞作用

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We had previously shown that hepatic lipase plays a prominent role in promoting the generation of pre-beta HDL particles from triglyceride rich HDL2, leaving an a-HDL particle of decreased size that was named "remnant HDL2" [Barrans, A., et al. (1994) J. Biol. Chem. 269, 11572-11577]. Interestingly, this remnant HDL2 was rapidly cleared by the liver, suggesting a particularly high affinity of those remnant HDL2 for liver cells. In the present study, we attempted to characterize the interaction of remnant HDL2 with HepG(2) cells, as compared to those of native triglyceride rich HDL2. Two main observations were made. First, while triglyceride rich HDL2 particles were able to bind only the low-affinity binding sites, the remaining particle generated after hepatic lipase lipolysis the remnant HDL2 was further able to bind to the high-affinity binding sites. Competition experiments indicate that these two remnant HDL2 binding sites were the same as the two HDL3 binding sites previously described [Barbaras, R., et al. (1994) Biochemistry 33, 2335-2340]. This is the first observation on the remodelling dependence of HDL binding onto hepatocytes. Second, following binding on those two binding sites, the remnant HDL2 were faster internalized and in higher amounts than the native triglyceride rich HDL2. All together, these observations suggest that the continuous remodeling of HDL induces different binding and internalization characteristics of the HDL particles and that the high-affinity HDL binding sites might trigger the internalization of apo HDL through the low-affinity binding sites. [References: 21]
机译：先前我们已经表明，肝脂肪酶在促进富含甘油三酸酯的HDL2产生pre-βHDL颗粒方面起着重要作用，留下了尺寸减小的α-HDL颗粒，称为“残余HDL2” [Barrans，A.等。 （1994）J.Biol。化学269，11572-11577]。有趣的是，这种残留的HDL2被肝脏迅速清除，表明这些残留的HDL2对肝细胞的亲和力特别高。在本研究中，我们试图表征与富含甘油三酸酯的HDL2相比，残留的HDL2与HepG（2）细胞的相互作用。进行了两个主要观察。首先，尽管富含甘油三酸酯的HDL2颗粒只能结合低亲和力的结合位点，但在肝脂肪酶脂解后，残留的HDL2产生的剩余颗粒还可以与高亲和力的结合位点结合。竞争实验表明，这两个残余的HDL2结合位点与先前描述的两个HDL3结合位点相同[Barbaras，R.，et al。 （1994）Biochemistry 33，2335-2340]。这是关于HDL结合对肝细胞的重塑依赖性的首次观察。其次，在这两个结合位点上结合后，残留的HDL2的内在化速度更快，且含量高于天然的富含甘油三酸酯的HDL2。总之，这些观察结果提示HDL的连续重塑诱导了HDL颗粒的不同结合和内在化特征，并且高亲和力HDL结合位点可能通过低亲和力结合位点触发载脂蛋白HDL的内在化。 [参考：21]

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