MOLECULAR DEVELOPMENT OF COLLAGEN FIBERS

总的目的是了解胶原纤维的生物合成。 胶原蛋白V的功能尚不清楚。 我们发现的前胶原V 在分子长度上与间质胶原蛋白相似， 前肽的加工，但发现了重要的新特征， 现在开始调查。 长寿命的中间体P-胶原（V）和 最终的胶原V均保留大量非胶原肽。 我们将 表征它们，它们与不寻常的“P-肽”的相互作用， 中间体之间的联系，以及它们的潜力， 作为纤维、细胞表面和基底膜之间的连接物。 我们已经发现了一种新的前胶原V链，它似乎是特异性的， 肌腱 它的分子功能将被研究相对于 筋芯和滑动面的差异纤维结构 和腱鞘，以及由这些细胞衍生的细胞产生 不同地区 这一信息将有助于伤口愈合的切除 肌腱 我们将确定I型前胶原的形式及其分子状态， 当它们离开成纤维细胞并存款在新生纤维上时，它们与成纤维细胞结合。 细胞外基质的超分子组装依赖于 相互作用成分的浓度。 我们将研究 分子排阻效应严重地改变了有效浓度。 在鸡胚血管中发现一种新的胶原肽。 我们将 分离它，将其与最近描述的“内膜”胶原VI进行比较， 并遵循其装配。 这对寻找新的分子生物学活性物质具有重要意义。 纤维状胶原的排列。 我们将联合收割机， 免疫学和分子电子显微镜方法 细胞外基质组装

The overall aim is to understand the biosynthesis of collagen fibers. The function of collagen V is unknown. Our discovery of procollagen V showed similarities with interstitial collagens in molecular length and processing of propeptides, but uncovered significant new features which we shall now investigate. The long-lived intermediate p-collagen (V) and the final collagen V both retain larage non-collagenous peptides. We shall characterize them, their interactions with the unusual "P-peptides" to which the intermediate becomes linked, and their potential, interesting role as linkers between fibers, cell surfaces and basement membranes. We have found a new procollagen V chain which seems to be specific for tendon. Its molecular function will be studied relative to the differential fiber structure of the core and gliding surfaces of tendons and of tendon sheaths, and its production by cells derived from these different regions. This information will help in wound healing of resected tendons. We shall determine the forms of procollagen I and their state of molecular association when they exit from fibroblasts and deposit on nascent fibers. Supramolecular assembly of extracellular matrix depends on the concentrations of the interacting components. We shall study how far molecular exclusion effects critically change the effective concentrations. In chick embryo blood vessels we found a new collagenous peptide. We will isolate it, compare it with the recently described "intima" collagen VI, and follow its assembly. This is of importance to finding new molecular arrangements in fibrous collagens. We shall combine biosynthetic, immunological and molecular electron microscopic approaches to follow extracellular matrix assembly.