Etipathogenesis of osteoarthritis and cartilage proteoglycan.

对关节软骨中的蛋白多糖进行了形态学、生化和免疫学研究。短句来源cmd/cmd小鼠的骨骺软骨在遗传上不能合成软骨特征蛋白多糖，但在<II型>胶原合成中正常，光镜和电镜下观察其结构，发现胶原原纤维明显异常，如胶原原纤维直径增加，出现周期性带状图案，并形成束状。这些结果表明，软骨特征蛋白多糖（软骨PG）通常限制胶原原纤维的横向生长，并影响体内胶原原纤维的形成。体外培养的cmd/cmd软骨细胞产生结节，细胞外基质明显减少。免疫荧光染色显示，突变细胞的结节在缺乏软骨PG和<II型>胶原沉积不均匀和减少方面与正常细胞不同。将正常小鼠软骨或群鼠软骨肉瘤制备的软骨PG外源性添加到培养基中，将其完全纳入结节的细胞外基质中，同时纠正<II型>胶原的异常分布模式。透明质酸或十糖会干扰软骨PG与基质的结合。结果表明，完整的软骨PG需要特异性并入软骨细胞结节中，并进一步表明软骨PG在基质大分子的组装中起调节作用。

The research includes morphological, biochemical and immunological work about the proteoglycan in articular cartilage.Light and electron microscopic observations on the structure of epiphyseal cartilages in the cmd/cmd mice, which had genetically failed to synthesize cartilage-characteristic proteoglycan but were normal in type <II> collagen synthesis, showed apparent abnormalities of collagen fibrils: e.g. increase in the diameter, appearance of periodic banding patterns and bundle-formation of collagen fibrils. These findings suggest that cartilage-characteristic proteoglycan (Cartilage PG) normally limits the lateral growth of collagen fibrils and affects collagen fibrillogenesis in vivo.Chondrocytes from the cmd/cmd cartilage cultured in vitro produced nodules with greatly reduced extracellular matrix. Immunofluorescence staining revealed that the nodules of mutant cells differed from the normal in lacking cartilage PG and in uneven and reduced deposition of type <II> collagen. Exogenously added cartilage PG prepared from either normal mouse cartilage or Swarm rat chondrosarcoma to the culture medium was incorporated exclusively into the extracellular matrices of the nodules, with a concurrent correction of the abnormal distribution pattern of type <II> collagen. The incorporation of cartilage PG into the matrix was disturbed by hyaluronic acid or decasaccharide.The results indicate that the intact from of cartilage PG is required for specific incorporation into the chondrocyte nodules, and further suggest that cartilage PG plays a regulatory role in the assembly of the matrix macromolecules.