HUMAN TOOTH ROOT PHOSPHOPROTEIN AND REMINERALIZATION

根面龋在成年人群中广泛存在并不断增加， 这些病变表现出不同的再分化能力。 无论是机制 也不是他们的变化的原因， 充分理解了商业化的潜力。的作用 磷蛋白，发现在人类牙齿的根，对矿化 牙根龋损伤的可能性尚未被研究。 尽管更多 磷蛋白在生物学中的作用 矿化也不清楚。 因此，本研究将首先 检查磷蛋白在再矿化中的作用;然而，由于 这两个过程之间的密切联系， 这项研究还应提供关于生物矿化作用的资料。 三 观察结果可能具有重要的临床意义 对牙根表面在口腔中矿化能力的影响。 第一、 在人类牙根中有两个磷蛋白库，一个是可溶性库， 很容易通过10%EDTA脱矿和不溶性池去除 这是只恢复使用胶原酶消化。 第二、 磷蛋白在矿化和成熟过程中降解 过程 第三，可溶性降解磷蛋白作为抑制剂 脱矿物质的成熟人根有机物的矿化 矩阵 尽管这些观察结果很重要，但进一步的研究 需要澄清各种磷蛋白在 生物矿化和生物矿化。 因此，完整和退化， 可溶性和不溶性磷蛋白将被提取、分离并 从脱矿物质的人根碎片的有机基质中纯化， 路段 这些蛋白质将在有机基质中稳定， 附着在琼脂糖珠上，然后暴露于亚稳态 商业化解决方案。 这些基质的矿化能力 将通过TEM和显微放射照相术进行检查。 最近隔离的一个 来自人类未成熟根的完整96 K磷蛋白将允许 首次进行免疫细胞化学研究， 磷蛋白及其与矿物质沉积（成核）关系 有待确定。 将产生单克隆和多克隆抗体， 可溶性和不溶性磷蛋白和蛋白质免疫印迹将 用于测定所得抗体与以下物质的交叉反应性： 完整的和降解的，可溶的和不可溶的磷蛋白。 一部小说在体内 方法将采取检查磷蛋白的影响，使用 一种口内器具。 部分和完全脱矿基质， 并且不含可溶性磷蛋白将被放置到器具中， 口腔内研究蛋白质对矿化的影响。 此外，还将测试优化的再矿化凝胶和溶液 以确定其作为预防和/或治疗疗法的潜力， 根面病变

Root surface caries is widespread and increasing in adult populations and these lesions show variable ability to remineralize. Neither the mechanism of remineralization, nor the reason for the variability of their remineralization potential is fully understood. The role of phosphoproteins, found in the roots of human teeth, on the remineralization potential of root caries lesions has not been investigated. Although more extensively studied, the role of phosphoprotein in biological mineralization is also not understood. Therefore, this study will first examine the role of phosphoprotein in remineralization; however, because of the close association between these two processes, the data generated in the study should provide information on biomineralization as well. Three observations have been made that may have important clinical implications on the ability of root surfaces to remineralize in the oral cavity. First, there are two pools of phosphoprotein in human tooth roots, a soluble pool that is easily removed by 10% EDTA demineralization and an insoluble pool that is only recovering using collagenase digestion. Second, phosphoprotein is degraded during the mineralization and maturation process. Thirdly, the soluble degraded phosphoprotein acts as an inhibitor of the remineralization of demineralized mature human root organic matrices. Despite the importance of these observations, further studies are needed to clarify the roles of the various phosphoproteins in remineralization and biomineralization. Therefore, intact and degraded, soluble and insoluble phosphoprotein will be extracted, isolated and purified from the organic matrices of demineralized human root shards and sections. These proteins will be stabilized within organic matrices and attached to agarose beads and then be exposed to metastable remineralization solutions. The ability of these substrates to mineralize will be examined by TEM and microradiography. The recent isolation of an intact 96K phosphoprotein from human immature roots will allow for the first time an immunocytochemical study which will allow the distribution of the phosphoprotein and its relationship to mineral deposition (nucleation) to be determined. Monoclonal and polyclonal antibodies will be raised to the soluble and insoluble phosphoprotein and western immunoblotting will be used to determine the cross-reactivity of the resulting antibodies with intact and degraded, soluble and insoluble phosphoprotein. A novel in vivo approach will be taken to examine the effects of the phosphoprotein using an intraoral appliance. Partially and fully demineralized matrices with and without soluble phosphoprotein will be placed into the appliance and the effects of the protein on remineralization investigated intraorally. In addition, an optimized remineralization gel and solution will be tested to determine their potential as a preventive and/or treatment therapy for root surface lesions.