通过干扰分泌-再摄取途径实现小硫酸皮肤素蛋白聚糖II的细胞外积累。
Extracellular accumulation of small dermatan sulphate proteoglycan II by interference with the secretion-recapture pathway.
作者信息
Schmidt G, Hausser H, Kresse H
机构信息
Institute of Physiological Chemistry and Pathobiochemistry, University of Münster, Federal Republic of Germany.
出版信息
Biochem J. 1990 Mar 1;266(2):591-5.
Human skin fibroblasts were metabolically labelled in the presence of affinity-purified antibodies against the core protein of small dermatan sulphate proteoglycan II. The treatment resulted in a dose- and time-dependent accumulation of this proteoglycan in the culture medium, with a 2-3-fold increase found within an experimental period of 4 h. The presence of antibodies was without influence on the rate of biosynthesis of the proteoglycan. However, proteoglycan-antibody complexes were inefficiently endocytosed. Addition of unlabelled proteoglycan, which served as a competitor for uptake, similarly led to an accumulation of newly formed [35S]sulphate-labelled proteoglycans. Proteoglycan accumulation also occurred as a consequence of its binding to collagen fibrils which were physically separated from the cell layer. Together, these results establish the quantitative importance of the secretion-recapture pathway of small dermatan sulphate proteoglycan II in cultured fibroblasts.
在存在针对小硫酸皮肤素蛋白聚糖II核心蛋白的亲和纯化抗体的情况下，对人皮肤成纤维细胞进行代谢标记。该处理导致这种蛋白聚糖在培养基中呈剂量和时间依赖性积累，在4小时的实验期内发现增加了2至3倍。抗体的存在对蛋白聚糖的生物合成速率没有影响。然而，蛋白聚糖-抗体复合物的内吞作用效率低下。添加未标记的蛋白聚糖作为摄取的竞争物，同样导致新形成的[35S]硫酸盐标记的蛋白聚糖积累。蛋白聚糖的积累也是其与从细胞层物理分离的胶原纤维结合的结果。总之，这些结果确立了小硫酸皮肤素蛋白聚糖II在培养的成纤维细胞中的分泌-再捕获途径的定量重要性。
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