STRUCTURAL STUDIES OF CONNECTIVE TISSUES

结缔组织包括多种组织，包括 肌腱、软骨、骨、皮肤和玻璃体，这些都需要特定的 机械和结构性能适合他们 功能 这些组织都有胶原纤维作为主要的 结构组分及其所需组织特异性 依赖于分子和超分子的组织， 胶原蛋白与细胞外的其他分子一起 矩阵 我们的实验室已经开始了一项计划， 描述一系列连接词的结构差异 具有不同遗传类型和不同非胶原性的组织 组分，在分子和原纤维组织水平。 胶原蛋白结构的组织特异性变化将与 稳定这些聚集体的相互作用。 分子堆积和分子间相互作用 其特征在于由不同遗传因素形成的D-周期性纤维 胶原蛋白的种类 I、II和III型胶原的原纤维在以下方面不同： 分子密度，以及这种密度差异的调节 通过水的相互作用，序列差异和碳水化合物 内容将被审查。 次要胶原V型和1型 α，2 α，3 α可以形成纤维， 均匀的小直径并且具有轴向D周期。 原纤维 结构，原纤形成过程，和结构的影响 在完整组织形式中发现的末端肽将 以这些次要胶原蛋白为特征。 组织中原纤维的组织结构以及 将检查胶原组织上的蛋白聚糖是否为II型 脊索中的胶原。 小而均匀的II型纤维 七鳃鳗脊索有一个大的中心到中心的距离，相等 几乎是原纤维直径的两倍。 稳定这一切的力量 将研究纤维阵列，以确定它们是否涉及 平衡状态，例如原纤维上表面电荷的排斥， 或更刚性的结构，例如共价交联或涂层 纤维表面。 蛋白多糖在胶原中的作用 将通过确定以下因素的影响来检查结构 胶原蛋白分子堆积、原纤维上的蛋白聚糖去除 直径和纤维间距，以及电荷和水 胶原纤维之间的相互作用。

Connective tissues comprise a diverse group of tissues, including tendon, cartilage, bone, skin, and vitreous which require specific mechanical and structural properties appropriate to their function. These tissues all have collagen fibrils as a major structure component, and their required tissue specific properties depend on the molecular and supramolecular organization of collagen together with other molecules in the extracellular matrix. Our laboratory has embarked on a program to characterize the structural differences in a range of connective tissues with different genetic types and different non-collagenous components, at the level of molecular and fibril organization. Tissue specific variations in collagen structure will be related to the interactions which stabilize these aggregates. The molecular packing and molecular interactions will be characterized for D-periodic fibrils formed by different genetic types of collagens. Fibrils of types I, II and III collagens differ in molecular density, and the mediation of such density differences by water interactions, sequence differences and carbohydrate content will be examined. The minor collagens type V and 1 alpha, 2 alpha, 3 alpha can form fibrils which appear to be of very uniform small diameter and to have an axial D period. The fibril structures, fibril forming process, and structural effects of terminal peptides found in intact tissue forms will be characterized for these minor collagens. The organization of fibrils in tissues and the effects of proteoglycan on collagen organization will be examined for type II collagen in notochord. The small uniform type II fibrils in lamprey notochord have a large center to center distance, equal to almost twice the fibril diameter. The forces stabilizing this array of fibrils will be investigated, to determine if they involve an equilibrium state, e.g. repulsion of surface charges on fibrils, or more rigid structures, e.g. covalent cross-linking or a coating of the fibril surface. The role of proteoglycan in collagen structure will be examined by determining the effect of proteoglycan removal on collagen molecular packing, fibril diameter, and interfibrillar distance, and on the charge and water interactions between collagen fibrils.