Interaction of small dermatan sulfate proteoglycan from fibroblasts with fibronectin.
Interaction of small dermatan sulfate proteoglycan from fibroblasts with fibronectin.
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DOI：
10.1083/jcb.104.6.1683
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发表时间：
1987-06
期刊：
影响因子：
--
通讯作者：
Kresse H
中科院分区：
文献类型：
--
作者：
Schmidt G;Robenek H;Harrach B;Glössl J;Nolte V;Hörmann H;Richter H;Kresse H
使用免疫金标记将小硫酸皮肤素蛋白聚糖 (DS-PG) 的核心蛋白定位在培养的人成纤维细胞表面。 4℃时，DS-PG核心蛋白均匀分布在细胞表面。在 37 摄氏度时，金颗粒要么以簇的形式重新排列，要么仍然与原纤维结合在一起。双标记免疫细胞化学表明 DS-PG 核心蛋白和纤连蛋白在原纤维中共同分布。在酶联免疫吸附测定中，成纤维细胞分泌物中的 DS-PG 及其核心蛋白与纤连蛋白的结合发生在 pH 7.4 和生理离子强度下。可以结合比完整蛋白多糖更大量的核心蛋白。纤连蛋白肽在 COOH 末端附近含有肝素结合结构域，或含有肝素结合 NH2 末端，是唯一与 DS-PG 和核心蛋白相互作用的片段。肝素和硫酸皮肤素的竞争和替代实验表明肝素和 DS-PG 核心蛋白存在相邻的结合位点。据推测，硫酸乙酰肝素蛋白聚糖和 DS-PG 可能与纤连蛋白竞争性相互作用。
Immunogold labeling was used to localize the core protein of small dermatan sulfate proteoglycan (DS-PG) on the surface of cultured human fibroblasts. At 4 degrees C, DS-PG core protein was uniformly distributed over the cell surface. At 37 degrees C, gold particles either became rearranged in form of clusters or remained associated with fibrils. Double-label immunocytochemistry indicated the co- distribution of DS-PG core protein and fibronectin in the fibrils. In an enzyme-linked immunosorbent assay, binding of DS-PG from fibroblast secretions and of its core protein to fibronectin occurred at pH 7.4 and at physiological ionic strength. Larger amounts of core protein than of intact proteoglycan could be bound. Fibronectin peptides containing either the heparin-binding domain near the COOH-terminal end or the heparin-binding NH2 terminus were the only fragments interacting with DS-PG and core protein. Competition and replacement experiments with heparin and dermatan sulfate suggested the existence of adjacent binding sites for heparin and DS-PG core protein. It is hypothesized that heparan sulfate proteoglycans and DS-PG may competitively interact with fibronectin.