Oram J F, Brinton E A, Bierman E L
J Clin Invest. 1983 Nov;72(5):1611-21. doi: 10.1172/JCI111120.
Cultured human skin fibroblasts and human arterial smooth muscle cells possess high-affinity binding sites specific for high density lipoproteins (HDL). Results from the present study demonstrate that binding of HDL to these sites is up-regulated in response to cholesterol loading of cells. When fibroblasts or smooth muscle cells were preincubated with nonlipoprotein cholesterol, cellular binding of 125I-HDL3 was enhanced severalfold. This enhancement was sustained in the presence of cholesterol but was readily reversed when cells were exposed to cholesterol-free medium. The stimulatory effect of cholesterol treatment was prevented by cycloheximide, suggesting the involvement of protein synthesis. Kinetic analysis of HDL3 binding showed that prior exposure to cholesterol led to an induction of high-affinity binding sites on the cell surface. In the up-regulated state, the apparent dissociation constant (Kd) of these sites was approximately 2 micrograms protein/ml. Competition studies indicated that the HDL binding sites recognized either HDL3 or HDL2 but interacted weakly with low density lipoprotein (LDL). Exposure of cells to lipoprotein cholesterol in the form of LDL also enhanced HDL binding by a process related to delivery of sterol into cells via the LDL receptor pathway. Enhancement of HDL binding to fibroblasts by either nonlipoprotein cholesterol or LDL was associated with an increased cell cholesterol content, a suppressed rate of cholesterol synthesis, decreased LDL receptor activity, and an enhanced rate of cholesterol ester formation. A comparison of HDL3 binding with the effects of HDL3 on cholesterol transport from cells revealed similar saturation profiles, implying a link between the two processes. Thus, cultured human fibroblasts and human arterial smooth muscle cells appear to possess specific receptors for HDL that may function to facilitate cholesterol removal from cells.
培养的人皮肤成纤维细胞和人动脉平滑肌细胞具有对高密度脂蛋白(HDL)特异的高亲和力结合位点。本研究结果表明,HDL与这些位点的结合会因细胞的胆固醇负荷而上调。当成纤维细胞或平滑肌细胞与非脂蛋白胆固醇预孵育时,125I-HDL3的细胞结合增强了数倍。这种增强在有胆固醇存在时持续存在,但当细胞暴露于无胆固醇培养基中时则很容易逆转。胆固醇处理的刺激作用被放线菌酮阻止,提示蛋白质合成参与其中。HDL3结合的动力学分析表明,预先暴露于胆固醇会导致细胞表面高亲和力结合位点的诱导。在上调状态下,这些位点的表观解离常数(Kd)约为2微克蛋白质/毫升。竞争研究表明,HDL结合位点识别HDL3或HDL2,但与低密度脂蛋白(LDL)的相互作用较弱。细胞暴露于LDL形式的脂蛋白胆固醇也通过与通过LDL受体途径将固醇输送到细胞中的过程相关的方式增强了HDL结合。非脂蛋白胆固醇或LDL增强HDL与成纤维细胞的结合与细胞胆固醇含量增加、胆固醇合成速率受抑制、LDL受体活性降低以及胆固醇酯形成速率增强有关。HDL3结合与HDL3对细胞胆固醇转运的影响的比较显示出相似的饱和曲线,这意味着这两个过程之间存在联系。因此,培养的人成纤维细胞和人动脉平滑肌细胞似乎具有HDL的特异性受体,其可能起到促进胆固醇从细胞中清除的作用。