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首页> 外文期刊>Micron: The international research and review journal for microscopy >Organization and quantification of the collagen fibers in bone formation during orthodontic tooth movement
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Organization and quantification of the collagen fibers in bone formation during orthodontic tooth movement

机译:正畸牙齿移动过程中骨形成中胶原纤维的组织和定量

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The organic matrix of alveolar bone is composed fundamentally of type I collagen. Polarized light microscopy provides unique information about the structure, composition and polymerization degree of a variety of organic and inorganic tissues that is not available with other techniques. The aim of this research was to compare two methodologies of polarized light analysis for collagen organization in bone formation during orthodontic tooth movement and determined maturity of collagen over the time. Thirty Wistar rats were euthanized 3, 7 and 14 days after the NiTi unilateral closed-coil spring was stretched between the upper right first molar and the incisors. The control consisted by contra-lateral site. The first molar area was fixed, decalcified and histologically processed using picrosirius pigment. The collagen birefringence of bone turnover was analyzed by color percentage and phase retardation. We observed an increase in collagen fiber organization over time with two methodologies. The Pearson coefficient correlation indicated a strong relationship (0.76) among the two polarized light analyses. In summary, there is collagen maturation over 3, 7 and 14 days. We successfully evaluated the molecular organization, arrangement, degree of polymerization and maturation process of collagen fibers in bone turnover through color percentages and phase retardation.
机译:牙槽骨的有机基质基本由I型胶原组成。偏振光显微镜提供了有关各种有机和无机组织的结构,组成和聚合度的独特信息,而其他技术则无法提供这些信息。这项研究的目的是比较两种偏振光分析方法的正畸牙齿移动过程中骨形成中胶原组织的胶原化方法以及确定的胶原成熟度。将NiTi单侧闭合线圈弹簧在右上第一磨牙和门齿之间拉伸后的3、7和14天,对30只Wistar大鼠实施安乐死。对照由对侧部位组成。使用picrosirius色素固定,脱钙和组织学处理第一磨牙区域。通过颜色百分比和相位延迟分析了骨转换的胶原双折射。我们观察到两种方法随着时间的推移胶原纤维组织的增加。皮尔逊系数的相关性表明两个偏振光分析之间存在很强的关系(0.76)。总而言之,胶原蛋白会在3、7和14天中成熟。我们通过颜色百分比和相位延迟成功地评估了骨转换中胶原纤维的分子组织,排列,聚合度和成熟过程。

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