CARTILAGE OLIGOMERIC MATRIX PROTEIN AND THROMBOSPONDIN-1 - PURIFICATION FROM ARTICULAR-CARTILAGE, ELECTRON-MICROSCOPIC STRUCTURE, AND CHONDROCYTE BINDING
CARTILAGE OLIGOMERIC MATRIX PROTEIN AND THROMBOSPONDIN-1 - PURIFICATION FROM ARTICULAR-CARTILAGE, ELECTRON-MICROSCOPIC STRUCTURE, AND CHONDROCYTE BINDING
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DOI：
10.1111/j.1432-1033.1994.tb19070.x
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发表时间：
1994-08-01
期刊：
影响因子：
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通讯作者：
PAULSSON, M
中科院分区：
文献类型：
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作者：
DICESARE, PE;MORGELIN, M;PAULSSON, M
从正常牛关节软骨中分离纯化了软骨低聚基质蛋白(COMP)和凝血酶敏感蛋白1(TSP1)。纯化方案中的关键步骤是用含EDTA的缓冲液选择性萃取。通过肝素亲和层析实现了这两个分子的最终分离。经过旋转阴影和负染后的电子显微镜观察到的颗粒显示出与其原型分子相似的结构；对于COMP，来自于大鼠软骨肉瘤；对于TSP1，来自于血小板。研究了原代牛软骨细胞与纯化的基质蛋白的粘附性。细胞附着在COMP上，但不附着在结构上相关的TSP1上，表明这些蛋白在软骨中具有独立的功能。
Cartilage oligomeric matrix protein (COMP) and thrombospondin 1 (TSP1) were purified in a native form from normal bovine articular cartilage. The key step in the purification scheme was selective extraction with EDTA-containing buffer. Final separation of these two molecules was achieved by heparin affinity chromatography. Particles viewed by electron microscopy after rotary shadowing and negative staining revealed structures similar to their prototype molecules; from the Swarm rat chondrosarcoma for COMP, or from platelets for TSP1. Attachment of primary bovine chondrocytes to purified matrix proteins was investigated. Cells attached to COMP but not to the structurally related TSP1 indicating separate functions for these proteins in cartilage.