Roles of Matrix Proteoglycans in Dentin Bonding

基质蛋白多糖在牙本质粘接中的作用

• 批准号: 6816009
• 负责人: PATRICIA N PEREIRA
• 金额: $ 7.3万
• 依托单位: UNIV OF NORTH CAROLINA CHAPEL HILL
• 依托单位国家: 美国
• 财政年份: 2004
• 资助国家: 美国
• 起止时间: 2004-07-01 至 2006-06-30
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6816009
• 关键词: adhesions; atomic force microscopy; chondroitin sulfates; clinical research; collagen; crosslink; dental adhesive /sealant; dental bonding material; dentin; extracellular matrix; keratin; morphology; mucopolysaccharides; proteoglycan; transmission electron microscopy

DESCRIPTION (provided by applicant): Adhesion of restorative materials to the tooth structure has revolutionized the approach of dental treatment and is now essential for numerous elective dental procedures and for the replacement of tooth substance lost by caries or tooth fracture. Although there have been significant advances in dental adhesion technology, the contribution of dentin extracellular matrix (ECM) molecules to dentin bonding is still poorly understood. Fibrillar type I collagen is the predominant matrix component in dentin, and the maintenance of its fibrillar structure upon etching is crucial for the adhesion between restorative materials and dentin. The mechanisms for the maintenance of the structural integrity, however, are unknown. Based on our preliminary studies, we hypothesize that Chondroitin sulphate (CS-) and Keratan Sulphate (KS-) glycosaminoglycans (GAGs) carrying proteoglycans (PGs) facilitate dentin adhesion by maintaining the spatial architecture and stability of collagen fibrils. To address this hypothesis, the following specific aims are proposed: 1. To evaluate, after the dentin is demineralized, the effects of CS-, KS- or CS-KS removal on: 1a. Morphology of collagen fibrillar structure and collagen cross-linking analysis 1b. Ultimate strength of demineralized dentin and bond strength of adhesive resins 2. To determine, upon rewetting, the contribution of CS- and KS- GAGs/PGs by: 2a. Quantifying the levels of collagen re-expansion, collagen cross-linking analysis, and morphology of fibrillar structure, with and without CS, KS or both GAGs/PGs removal. 2b.Quantifying the UTS and bond strength with and without CS, KS or both GAGs/PGs removal 3. To determine the effects of CS- and KS-GAG addition on collagen re-expansion This combined biomechanical and biochemical approach may provide insights into the roles of CS/KS-PGs in collagen stabilization and dentin adhesion.

描述(由申请人提供)：修复材料与牙齿结构的粘接已经彻底改变了牙齿治疗的方法，现在对于许多可选的牙科程序和替换因龋齿或牙齿折断而丢失的牙齿物质是必不可少的。虽然牙本质黏附技术已经有了很大的进步，但牙本质细胞外基质(ECM)分子对牙本质黏结的作用仍然知之甚少。I型胶原纤维是牙本质中的主要基质成分，酸蚀后保持其纤维结构对修复材料与牙本质的粘结至关重要。然而，维持结构完整性的机制尚不清楚。根据我们的初步研究，我们假设硫酸软骨素(CS-)和硫酸角蛋白(KS-)糖胺聚糖(GAG)携带蛋白多糖(PG)通过维持胶原纤维的空间结构和稳定性来促进牙本质粘连。为了解决这一假设，提出了以下具体目标： 1.在牙本质脱矿后，评估去除CS-、KS-或CS-KS对： 1A.胶原纤维结构的形态及胶原交联度分析 1B.脱矿牙本质的极限强度与粘接树脂的粘接强度 2.确定CS-和KS-GAG/PGs在再湿时的贡献： 2A。在去除和不去除CS、KS或两者都去除GAG/PGs的情况下，量化胶原再扩张水平、胶原交联度分析和纤维结构的形态。 2b.在去除和不去除CS、KS或两种GAG/PG的情况下，对UTS和结合强度进行量化 3.测定添加CS-和KS-GAG对胶原再扩张的影响 这种生物力学和生物化学相结合的方法可能对CS/KS-PGs在胶原稳定和牙本质粘连中的作用提供更深入的了解。