REGULATION OF COLLAGEN MINERALIZATION IN THE TOOTH

牙齿中胶原蛋白矿化的调节

• 批准号: 6176164
• 负责人: MITSUO YAMAUCHI
• 金额: $ 23.08万
• 依托单位: UNIV OF NORTH CAROLINA CHAPEL HILL
• 依托单位国家: 美国
• 财政年份: 1993
• 资助国家: 美国
• 起止时间: 1993-07-01 至 2002-03-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6176164
• 关键词: SDS polyacrylamide gel electrophoresis; animal tissue; cementum; collagen; crosslink; dentin; dipeptides; glycosylation; high performance liquid chromatography; hydroxylation; immunocytochemistry; intermolecular interaction; normal ossification; protein purification; protein structure function; proteoglycan; stereochemistry; tendons; tooth

DESCRIPTION (Adapted from investigator's Abstract): The long term goal of this investigation is to understand the mechanisms regulating the spatial and temporal aspects of collagen mineralization. During the last grant period, partial characterization of the chemical states of collagen cross-linking and the three dimensional structure of the collagen fibrils in relation to mineralization were accomplished. These findings have led to the hypothesis that, in collagen-based mineralized tissues, the orientation and stacking of mineral platelets are spatially regulated by the configuration of the nontriple helical domains (telopeptides) of the type I collagen molecules. In addition, a group of proteoglycans (many of them are collagen-associated proteoglycans) in the tooth have been identified and were found to be immunolocalized almost exclusively in the premineralizing matrices such as near pericementocytes, precementum and predentin. These proteoglycans may be inhibiting premature mineralization through their association with collagen fibrils. By using the tooth (which does not remodel) as the major model, the specific questions asked in this application are: What are the chemical states of the amino- and carboxyl-terminal nontriple helical domains in premineralizing, mineralizing and non (never)-mineralizing collagens? How do these chemical states change with mineralization? What are the structural characteristics of the proteoglycans and their spatial relationship to collagen fibrils in predentin and precementum? and how do they change in mineralizing matrix (dentin and cementum)? In order to address these questions, biochemical, physical, immunochemical and immunohistochemical techniques will be employed. The information obtained from these studies will provide insight into the regulatory mechanisms of collagen mineralization.

描述(改编自《调查员摘要》)：的长期目标 这项调查是为了了解空间调节机制。 以及胶原蛋白矿化的时间方面。在最后一次拨款期间 胶原蛋白化学状态的周期、部分表征 交联性与胶原纤维的三维结构 完成了与成矿关系的研究。这些发现导致了 该假说认为，在胶原基矿化组织中， 和矿物质血小板的堆积在空间上受 I型非三螺旋结构域(端肽)的构型 胶原蛋白分子。此外，一组蛋白多糖(其中许多是 牙中的胶原相关蛋白多糖)已被鉴定，并 几乎只在矿化前期免疫定位 基质，如近牙周细胞、前胚层和前牙本质。这些 蛋白多糖可能通过其作用抑制过早矿化 与胶原蛋白纤维结合。通过使用牙齿(它不会 REMODEL)作为主要的模型，在这篇文章中提出的具体问题 用途是：氨基和氨基的化学状态是什么？ 矿化前、成矿过程中的羧基末端非三螺旋结构域 和非矿化的胶原蛋白？这些化学状态是如何改变的 有矿化作用吗？有哪些结构特征？ 蛋白多糖及其与胶原纤维的空间关系 前牙本质和前牙本质？它们在成矿基质中是如何变化的？ (牙本质和牙骨质)？为了解决这些问题，生化， 物理、免疫化学和免疫组织化学技术将 受雇的。从这些研究中获得的信息将提供洞察力 胶原蛋白矿化的调控机制。