HUMAN TOOTH ROOT PHOSPHOPROTEIN AND REMINERALIZATION

根面龋病在成人人群中普遍存在并呈上升趋势 这些病变表现出不同的再矿化能力。无论是这种机制，还是 再矿化的原因，也不是他们的变化的原因 重新矿化的潜力是完全理解的。的作用 在人类牙根中发现的磷蛋白对再矿化的影响 根面龋损的可能性还没有被调查。虽然更多 被广泛研究的磷蛋白在生物学中的作用 成矿作用也不是很清楚。因此，这项研究将首先 检查磷蛋白在再矿化中的作用；然而，由于 这两个进程之间的紧密关联，生成的数据 这项研究还应提供有关生物矿化的信息。三 已经进行的观察可能具有重要的临床意义 关于牙根表面在口腔中再矿化的能力。第一, 人的牙根中有两个磷蛋白池，一个可溶的池 这很容易通过10%的EDTA脱矿和不溶于水的水池去除 这只能用胶原酶消化来恢复。第二, 磷蛋白在矿化和成熟过程中被降解 进程。第三，可溶性降解的磷酸蛋白起到抑制作用。 脱矿的成熟人根有机再矿化的研究 矩阵。尽管这些观察结果很重要，但进一步的研究 需要阐明不同的磷蛋白在 再矿化和生物矿化。因此，完好无损和退化， 可溶和不可溶的磷蛋白将被提取、分离和 从脱矿的人根碎片的有机基质中提纯而成 横断面。这些蛋白质将稳定在有机基质中，并 附着在琼脂糖珠上，然后暴露在亚稳环境中 再矿化解决方案。这些底物的矿化能力 将通过透射电子显微镜和显微放射摄影术进行检查。最近隔离的一种 来自人类未成熟根的完整的96K磷酸蛋白将允许 首次进行免疫细胞化学研究，将允许分布 磷蛋白及其与矿物沉积(成核)的关系 待定。单抗和多克隆抗体将提高到 可溶性和不溶性磷蛋白和免疫印迹将被 用来确定产生的抗体与 完整的和可降解的，可溶的和不可溶的磷蛋白。一部活体小说 将采取一种方法来检查磷蛋白的效果 口腔内矫治器。部分和完全去矿化的矩阵 在没有可溶性磷蛋白的情况下，将其放入矫治器中 口腔内研究了蛋白质对再矿化的影响。 此外，还将测试一种优化的再矿化凝胶和溶液 以确定其作为预防和/或治疗方法的潜力 牙根表面受损。

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.