Scott P G, Nakano T, Dodd C M, Pringle G A, Kuc I M
Department of Oral Biology, University of Alberta, Edmonton, Canada.
Matrix. 1989 Aug;9(4):284-92. doi: 10.1016/s0934-8832(89)80004-6.
The low molecular weight proteoglycan fraction extracted from articular discs with 4 M guanidinium chloride was found to consist predominantly of an iduronate-rich dermatan sulphate proteoglycan, together with chondroitin sulphate-containing material. The dermatan sulphate proteoglycan was purified by ion-exchange and gel-filtration chromatography and its core protein isolated after digestion with chondroitinase ABC. The amino acid composition and pattern of cyanogen bromide peptides obtained from this core were closely similar to those of the protein core of bovine skin proteodermatan sulphate. Four monoclonal antibodies raised against bovine skin proteodermatan sulphate also reacted with the disc protein core and its cyanogen bromide peptides. Results of digestion with glycopeptidase F demonstrated the presence of three N-linked oligosaccharides. The combined size of these oligosaccharides appeared to be somewhat less than the size of those on skin proteodermatan sulphate. The glycosaminoglycan chain released by digestion with cathepsin C had a higher molecular weight than that from skin. These differences in glycosylated structures may be responsible for the different effects on collagen fibrillogenesis in vitro; whereas skin proteodermatan sulphate only reduced the rate of fibril growth, disc dermatan sulphate proteoglycan also increased the length of the lag-phase and the final opacity.
从关节盘中用4M氯化胍提取的低分子量蛋白聚糖部分主要由富含艾杜糖醛酸的硫酸皮肤素蛋白聚糖以及含硫酸软骨素的物质组成。通过离子交换和凝胶过滤色谱法纯化硫酸皮肤素蛋白聚糖，并在用软骨素酶ABC消化后分离其核心蛋白。从该核心获得的氨基酸组成和溴化氰肽模式与牛皮硫酸皮肤素蛋白聚糖的蛋白质核心非常相似。针对牛皮硫酸皮肤素蛋白聚糖产生的四种单克隆抗体也与椎间盘蛋白核心及其溴化氰肽发生反应。糖肽酶F消化结果表明存在三种N-连接寡糖。这些寡糖的总大小似乎略小于皮肤硫酸皮肤素蛋白聚糖上的寡糖大小。用组织蛋白酶C消化释放的糖胺聚糖链的分子量高于皮肤来源的。这些糖基化结构的差异可能是体外对胶原纤维形成产生不同影响的原因；皮肤硫酸皮肤素蛋白聚糖仅降低纤维生长速率，而椎间盘硫酸皮肤素蛋白聚糖还增加了延迟期的长度和最终的不透明度。
