Axelsson I, Berman I, Pita J C
J Biol Chem. 1983 Jul 25;258(14):8915-21.
Proteoglycans are considered to be important for the mechanical properties of articular cartilage and growth plate and for the regulation of calcification of growth plate. We have used ultracentrifugation, gel chromatography, and electron microscopy to characterize and compare proteoglycans isolated from rabbit articular cartilage, uncalcified growth plate, and calcified cartilage. We found that proteoglycans from articular cartilage were more resistant to extraction than were proteoglycans from uncalcified growth plate and calcified cartilage. Long term neutral decalcification of calcified cartilage resulted in degraded proteoglycans. The chondroitin sulfate chains from all three tissues had similar size distribution. Gel chromatography and electron microscopy of proteoglycan monomers suggested that those from uncalcified growth plate were largest, those from articular cartilage intermediate, and those from calcified cartilage smallest. Proteoglycan aggregates from articular cartilage were longer than those from uncalcified growth plate. Both biochemical and quantitative electron microscopic data suggested the existence in mineralizing cartilage of at least two different sized populations of proteoglycan aggregates.
蛋白聚糖被认为对关节软骨和生长板的力学性能以及生长板钙化的调节很重要。我们使用超速离心、凝胶色谱和电子显微镜来表征和比较从兔关节软骨、未钙化生长板和钙化软骨中分离出的蛋白聚糖。我们发现，关节软骨中的蛋白聚糖比未钙化生长板和钙化软骨中的蛋白聚糖更难提取。钙化软骨的长期中性脱钙导致蛋白聚糖降解。来自所有三种组织的硫酸软骨素链具有相似的大小分布。蛋白聚糖单体的凝胶色谱和电子显微镜显示，未钙化生长板中的最大，关节软骨中的居中，钙化软骨中的最小。关节软骨中的蛋白聚糖聚集体比未钙化生长板中的更长。生化和定量电子显微镜数据均表明，矿化软骨中存在至少两种不同大小的蛋白聚糖聚集体群体。
