STRUCTURE AND INTERACTIONS OF PROTEOGLYCANS

蛋白聚糖聚集体是蛋白聚糖的主要结构成分。 软骨细胞外基质 它们被认为是抑制 的矿化。 它们被移除并在骨骼中被替换，如 牙本质，由较小的非聚集性蛋白聚糖与不同的 以及可能的特定功能。 为了帮助研究 矿化的开始，我们建议扩大我们的工作， 软骨蛋白聚糖结构和相互作用。 我们已经报道了完整的初级序列的链接 蛋白和蛋白聚糖的透明质酸结合区。 通过DNA测序研究， 蛋白质核心的一级结构将很快完成。 因此 正确解释交联的基本信息 这里提出的实验是可行的。 这种方法应该 在分子水平上揭示了许多相互作用的本质 与蛋白多糖聚集体结合。 一个合理的基础将是 提供了随后的研究，可能是蛋白水解， 蛋白聚糖聚集体降解， 成矿 进一步的交联工作可能会明确 蛋白聚糖聚集体与其他 细胞外基质成分，从而全面了解 软骨组织 硫酸角质素是软骨和骨的成分。 他们是 不均匀和多分散。 我们建议确定是否 硫酸角质素链之间存在离散的差异 从不同的组织来源或附着在不同的部位上， 蛋白聚糖核心，作为调查这一作用的前奏， 糖胺聚糖 目前，这是一个悬而未决的问题， 某些硫酸角质素链参与特异性相互作用 与胶原纤维形成相关，或者更确切地说， 与蛋白聚糖的非特异性相互作用。

Proteoglycan aggregates are major structural constituents of cartilage extracellular matrix. They are believed to be inhibitory of mineralization. They are removed and replaced in bone, as in dentin, by smaller non-aggregative proteoglycans with different and possibly specific functions. With a view to aiding studies of the initiation of mineralization, we propose to extend our work on cartilage proteoglycan structure and interactions. We have reported on the complete primary sequence of link protein and the hyaluronate binding region of the proteoglycan. Through DNA sequencing studies, knowledge of the proteoglycan protein core primary structure will soon be complete. Thus the essential information for proper interpretation of cross-linking experiments as proposed here is available. This approach should reveal, at the molecular level, the nature of many interactions with the proteoglycan aggregate. A rational basis will be provided for subsequent studies of, presumably proteolytic, proteoglycan aggregate degradation which accompanies mineralization. Further cross-linking work may give clear indications of associations of proteoglycan aggregates with other extracellular matrix components and thus an overall view of cartilage organization. Keratan sulfates are constituents of cartilage and bone. they are heterogenous and polydisperse. We propose to determine whether there are discrete differences between keratan sulfate chains from different tissue sources or attached at different sites on the proteoglycan core, as a prelude to investigating the roles of this glycosaminoglycan. At present, it's an open question whether some keratan sulfate chains participate in specific interactions associated with collagen fibrillogenesis or rather serve to inhibit non-specific interactions with proteoglycans.