Chandrasekhar S, Laurie G W, Cannon F B, Martin G R, Kleinman H K
Proc Natl Acad Sci U S A. 1986 Jul;83(14):5126-30. doi: 10.1073/pnas.83.14.5126.
In cartilage, type II collagen is present as thin, short, randomly oriented fibrils. In vitro, however, type II collagen forms fibrils of large diameter, indicating that additional factors may be involved in the regulation of collagen fibril formation. We have examined extracts of a cartilage-producing tumor for the presence of collagen-binding proteins. In addition to fibronectin and link protein, a Mr 54,000 protein was found to bind to collagen fibrils as well as to native and denatured type II collagen. Immunological studies using antibody against the protein indicate that it is a cartilage matrix protein, not present in bone or in several other tissues. In vitro studies show that the Mr 54,000 protein in combination with cartilage proteoglycan decreases the rate of type II fibril formation and causes the fibrils to be of small diameter (24 +/- 8 nm). These studies indicate that complexes between collagen and proteoglycans mediated by this protein may regulate the assembly of cartilage matrix.
在软骨中，Ⅱ型胶原蛋白以细短、随机取向的原纤维形式存在。然而在体外，Ⅱ型胶原蛋白会形成大直径的原纤维，这表明可能有其他因素参与胶原蛋白原纤维形成的调控。我们检测了一种软骨生成肿瘤的提取物中是否存在胶原蛋白结合蛋白。除纤连蛋白和连接蛋白外，还发现一种分子量为54,000的蛋白质能与胶原蛋白原纤维以及天然和变性的Ⅱ型胶原蛋白结合。使用针对该蛋白质的抗体进行的免疫学研究表明，它是一种软骨基质蛋白，不存在于骨骼或其他几种组织中。体外研究表明，分子量为54,000的蛋白质与软骨蛋白聚糖结合会降低Ⅱ型原纤维的形成速率，并使原纤维直径变小（24±8纳米）。这些研究表明，由该蛋白质介导的胶原蛋白与蛋白聚糖之间的复合物可能会调节软骨基质的组装。
