Snowden J M
Biochim Biophys Acta. 1982 Apr 21;703(1):21-5. doi: 10.1016/0167-4838(82)90005-x.
The effects of proteoglycans/glycosaminoglycans on the thermal stability of in vivo assembled collagen fibrils have been examined. The shrinkage temperature of tendon collagen was found to be linearly dependent on the concentration of chondroitin sulphate in the surrounding fluid. Enzymic pretreatment of articular cartilage, to reduce its glycosaminoglycan content, resulted in decreased stability of the collagen present. The stability of the collagen in hyaluronidase-treated cartilage was found to be higher when measured in a solution of chondroitin sulphate (30 g/dl) than in buffer alone. The results of this study demonstrate that the proteoglycans stabilize collagen fibrils in tissues such as articular cartilage.
已对蛋白聚糖/糖胺聚糖对体内组装胶原纤维热稳定性的影响进行了研究。发现肌腱胶原的收缩温度与周围液体中硫酸软骨素的浓度呈线性相关。对关节软骨进行酶预处理以降低其糖胺聚糖含量，会导致其中存在的胶原稳定性降低。当在硫酸软骨素溶液（30 g/dl）中测量时，发现经透明质酸酶处理的软骨中胶原的稳定性高于仅在缓冲液中的稳定性。本研究结果表明，蛋白聚糖可稳定关节软骨等组织中的胶原纤维。
