STRUCTURE AND INTERACTIONS OF PROTEOGLYCANS

蛋白多糖聚集体是蛋白质的主要结构成分 软骨细胞外基质。它们被认为是抑制性的 矿化的可能性。它们被移除并在骨头中替换，如在 牙本质，由较小的非聚集蛋白多糖组成，具有不同的 可能还有特定的功能。以期帮助研究…… 关于矿化的启动，我们建议将我们的工作扩展到 软骨蛋白多糖的结构和相互作用。 我们已经报道了链接的完整初级序列 蛋白质和蛋白多糖的透明质酸结合区。 通过DNA测序研究，了解蛋白多糖 蛋白质核心一级结构很快就会完成。因此， 正确解释交联剂的基本信息 这里提出的实验是可行的。这种方法应该 在分子水平上揭示许多相互作用的本质 蛋白多糖的聚合体。理性的基础将是 为后续研究提供了可能，可能是蛋白质水解物， 蛋白多糖聚合体的降解 矿化作用。进一步的交联工作可能会清楚地表明 蛋白多糖聚合体与其他 细胞外基质成分，从而全面了解 软骨组织。 角蛋白硫酸盐是软骨和骨骼的成分。他们是 异质性和多分散性。我们建议确定是否 角蛋白硫酸盐链之间存在离散的差异 来自不同的组织来源或附着在不同的位置 蛋白多糖核心，作为研究这一蛋白的作用的前奏 糖胺多聚糖。目前，是否会有一个悬而未决的问题 某些角蛋白硫酸酯链参与特定的相互作用 与胶原纤维形成有关，或者更确切地说，用于抑制 与蛋白多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.