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首页> 外文OA文献 >Structure and interactions of proteoglycans in the extracellular matrix produced by cultured human fibroblasts.
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Structure and interactions of proteoglycans in the extracellular matrix produced by cultured human fibroblasts.

机译：蛋白聚糖在培养的人成纤维细胞产生的细胞外基质中的结构和相互作用。

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Subconfluent cultures of human embryonic skin fibroblasts were labelled with [35S]sulphate for 3 days, after which cell-free extracellular matrix was isolated. A chondroitin sulphate proteoglycan (CSPG) and a heparan sulphate proteoglycan (HSPG) were purified from the matrix. Chromatography on Sepharose CL-2B gave peak Kav. values of 0.35 and 0.38 respectively for the CSPG and the HSPG. The polysaccharide chains released from the two PGs were of similar size (Kav. 0.50 on Sepharose CL-4B). Approx. 50% of the CSPG showed affinity for hyaluronic acid (HA). However, it differed immunologically from the HA-aggregating CSPG of human articular cartilage, and had a larger core protein (apparent molecular mass 290 kDa) than had the cartilage PG. Neither metabolically [35S]sulphate-labelled PGs, isolated from the medium of fibroblast cultures, nor chemically 3H-labelled polysaccharides (HA, CS, HS and heparin) were incorporated into the extracellular matrix when added to unlabelled cell cultures. These results indicate that the matrix PGs are not derived from the PGs present in the medium and that an interation between polysaccharide chains and matrix components is not sufficient for incorporation of PGs into the matrix. Incubation of cell-free 35S-labelled matrix with unlabelled polysaccharides did not lead to the release of any 35S-labelled material, supporting this conclusion. Furthermore, so-called 'link proteins' were not present in the fibroblast cultures, indicating that the CSPGs were anchored in the matrix in a manner different from the link-stabilized association of CSPG with HA in chondrocyte matrix. The identification of a proteinase, secreted by fibroblasts in culture, that after activation with heparin has the ability to release 35S-labelled PGs from the matrix may also indicate that the core proteins are important for the association of the PGs to the matrix.
机译：用[35S]硫酸盐标记人类胚胎皮肤成纤维细胞的亚融合培养物3天，然后分离出无细胞的细胞外基质。从基质中纯化硫酸软骨素蛋白聚糖（CSPG）和硫酸乙酰肝素蛋白聚糖（HSPG）。在琼脂糖凝胶CL-2B上进行色谱分离，得到峰Kav。 CSPG和HSPG的值分别为0.35和0.38。从两个PG释放的多糖链具有相似的大小（琼脂糖凝胶CL-4B上的Kav.0.50）。大约50％的CSPG对透明质酸（HA）表现出亲和力。但是，它在免疫学上不同于人关节软骨的HA聚合CSPG，并且比软骨PG具有更大的核心蛋白（表观分子量290 kDa）。从成纤维细胞培养液中分离出的代谢性[35S]硫酸盐标记的PG，或化学3H标记的多糖（HA，CS，HS和肝素）均未添加到未标记的细胞培养物中。这些结果表明基质PG不是衍生自培养基中存在的PG，并且多糖链和基质组分之间的相互作用不足以将PG掺入基质中。将无细胞的35S标记的基质与未标记的多糖一起孵育不会导致任何35S标记的物质的释放，支持此结论。此外，成纤维细胞培养物中不存在所谓的“连接蛋白”，这表明CSPG以不同于软骨细胞基质中CSPG与HA的链接稳定缔合的方式锚定在基质中。由肝中的成纤维细胞分泌的蛋白酶的鉴定表明，用肝素激活后具有从基质中释放35S标记的PG的能力，这也可能表明核心蛋白对于PG与基质的缔合很重要。

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