Roles of Matrix Proteoglycans in Dentin Bonding

描述（由申请人提供）：将修复材料粘附到牙齿结构上已经彻底改变了牙科治疗方法，并且现在对于许多选择性牙科手术以及替换因龋齿或牙齿断裂而丢失的牙齿物质至关重要。尽管牙本质粘附技术已经取得了显著的进展，但牙本质细胞外基质（ECM）分子对牙本质粘结的贡献仍然知之甚少。纤维状I型胶原是牙本质中的主要基质成分，并且在蚀刻后维持其纤维状结构对于修复材料与牙本质之间的粘附至关重要。然而，维持结构完整性的机制尚不清楚。基于我们的初步研究，我们假设硫酸软骨素（CS-）和硫酸角质素（KS-）携带蛋白聚糖（PG）的糖胺聚糖（GAG）通过维持胶原纤维的空间结构和稳定性来促进牙本质粘附。为了解决这一假设，提出了以下具体目标： 1.评价在牙本质脱矿后，去除CS-、KS-或CS-KS对以下方面的影响： 1a.胶原纤维结构形态及胶原交联分析 1b.脱矿牙本质的极限强度与粘接树脂的粘接强度 2.通过以下方式确定再润湿后CS-和KS-GAG/PG的贡献： 2a.在CS、KS或GAG/PG去除和未去除的情况下，定量胶原再膨胀水平、胶原交联分析和纤维结构形态。 2b.在去除和不去除CS、KS或两种GAG/PG的情况下量化UTS和粘合强度 3.确定CS-和KS-GAG添加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以提供洞察CS/KS-PG在胶原稳定和牙本质粘附中的作用。

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.