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Roles of Matrix Proteoglycans in Dentin Bonding

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
依托单位国家:
美国
项目类别:
财政年份:
2004
资助国家:
美国
项目状态:
已结题
起止时间:
2004-07-01 至 2006-06-30

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中文摘要
翻译
描述(由申请人提供):修复材料粘附到牙齿结构已经彻底改变了牙科治疗的方法,现在是许多选择性牙科手术和替换因龋齿或牙齿断裂而丢失的牙齿物质所必需的。尽管牙本质黏附技术已经取得了重大进展,但牙本质细胞外基质(ECM)分子对牙本质黏附的贡献仍然知之甚少。纤维状I型胶原是牙本质中主要的基质成分,在蚀刻时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,我们假设携带蛋白聚糖(pg)的硫酸软骨素(CS-)和硫酸角蛋白(KS-)糖胺聚糖(GAGs)通过维持胶原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:
英文摘要
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.
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