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肝内皮细胞和库普弗细胞上清道夫受体对修饰低密度脂蛋白的结合特性

Binding characteristics of scavenger receptors on liver endothelial and Kupffer cells for modified low-density lipoproteins.

作者信息

De Rijke Y B, Biessen E A, Vogelezang C J, van Berkel T J

机构信息

Division of Biopharmaceutics, Leiden-Amsterdam Center for Drug Research (LACDR), Sylvius Laboratories, University of Leiden, The Netherlands.

出版信息

Biochem J. 1994 Nov 15;304 ( Pt 1)(Pt 1):69-73. doi: 10.1042/bj3040069.

Abstract

Previous studies showed that both endothelial and Kupffer cells contain specific recognition sites of oxidized low-density lipoprotein (OxLDL), in addition to recognition sites which recognize OxLDL and acetylated LDL (AcLDL). We have determined the binding characteristics of the recognition sites for OxLDL on Kupffer cells and endothelial cells (OxLDL-specific binding-site) in comparison to the recognition site for AcLDL on endothelial cells, which recognizes both AcLDL and OxLDL (Ac/OxLDL binding site). The capacity of Kupffer cells to bind OxLDL (Bmax. = 779 ng of 125I-OxLDL/mg of cell protein; Kd = 6 micrograms/ml) was comparable to the binding-capacity of endothelial cells (Bmax. = 803 ng of 125I-OxLDL/mg of cell protein; Kd = 5 micrograms/ml). The effect of net charge of modified LDL on its affinity for the recognition sites on Kupffer and endothelial cells was evaluated using competition studies. The affinity of AcLDL for the Ac/OxLDL binding site was greatly increased from 460 micrograms/ml to 4 micrograms/ml with increasing extent of modification and thus net charge. The Ac/OxLDL binding-site on endothelial cells also displayed an increased affinity towards LDL with an increasing degree of oxidation. The affinity of OxLDL for the Ac/OxLDL binding-site appeared to be about 4-fold higher than that of AcLDL with a similar extent of modification. At higher degrees of oxidation of LDL, the affinity for the OxLDL-specific site on endothelial and Kupffer cells was also strongly enhanced; the OxLDL-specific binding-site possesses a higher affinity for mildly oxidized LDL as compared with the Ac/OxLDL binding-site. It is concluded that recognition of OxLDL by both the OxLDL-specific binding-site and the Ac/OxLDL binding-site on liver endothelial and Kupffer cells depends on the net negative charge of modified LDL. The similarity in binding pattern of these binding sites makes it likely that the newly described 95 kD OxLDL binding protein on Kupffer cells [Y. B. De Rijke and Th. J. C. van Berkel, J. Biol. Chem. (1994), 269, 824-827] contains a recognition site with similar structural elements as described earlier for scavenger receptors.

摘要

先前的研究表明,除了能识别氧化型低密度脂蛋白(OxLDL)和乙酰化低密度脂蛋白(AcLDL)的识别位点外,内皮细胞和库普弗细胞都含有氧化型低密度脂蛋白的特异性识别位点。我们已经确定了库普弗细胞和内皮细胞上氧化型低密度脂蛋白识别位点(OxLDL特异性结合位点)的结合特性,并与内皮细胞上能识别乙酰化低密度脂蛋白和氧化型低密度脂蛋白的乙酰化/氧化型低密度脂蛋白结合位点(Ac/OxLDL结合位点)进行了比较。库普弗细胞结合氧化型低密度脂蛋白的能力(Bmax. = 779 ng 125I-OxLDL/mg细胞蛋白;Kd = 6微克/毫升)与内皮细胞的结合能力相当(Bmax. = 803 ng 125I-OxLDL/mg细胞蛋白;Kd = 5微克/毫升)。使用竞争研究评估了修饰低密度脂蛋白的净电荷对其与库普弗细胞和内皮细胞上识别位点亲和力的影响。随着修饰程度以及净电荷的增加,乙酰化低密度脂蛋白对Ac/OxLDL结合位点的亲和力从460微克/毫升大幅增加到4微克/毫升。内皮细胞上的Ac/OxLDL结合位点对氧化程度增加的低密度脂蛋白也表现出更高的亲和力。在相似的修饰程度下,氧化型低密度脂蛋白对Ac/OxLDL结合位点的亲和力似乎比乙酰化低密度脂蛋白高约4倍。在更高的低密度脂蛋白氧化程度下,其对内皮细胞和库普弗细胞上OxLDL特异性位点的亲和力也显著增强;与Ac/OxLDL结合位点相比,OxLDL特异性结合位点对轻度氧化的低密度脂蛋白具有更高的亲和力。结论是,肝内皮细胞和库普弗细胞上的OxLDL特异性结合位点和Ac/OxLDL结合位点对氧化型低密度脂蛋白的识别取决于修饰低密度脂蛋白的净负电荷。这些结合位点结合模式的相似性表明,库普弗细胞上新描述的95 kD氧化型低密度脂蛋白结合蛋白[Y. B. De Rijke和Th. J. C. van Berkel,《生物化学杂志》(1994年),269,824 - 827]包含一个具有与先前描述的清道夫受体相似结构元件的识别位点。

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