Bildt M M, Bloemen M, Kuijpers-Jagtman A M, Von den Hoff J W
Department of Orthodontics and Oral Biology, Radboud University Nijmegen Medical Centre, Nijmegen, The Netherlands.
Eur J Orthod. 2009 Oct;31(5):529-35. doi: 10.1093/ejo/cjn127. Epub 2009 Mar 18.
Orthodontic tooth movement requires extensive re-modelling of the periodontium. Matrix metalloproteinases (MMPs) degrade the extracellular matrix during re-modelling, while their activity is regulated by the tissue inhibitors of metalloproteinases (TIMPs). The aim of this study was to investigate differences in MMP and TIMP levels in the gingival crevicular fluid (GCF) at the resorption and apposition sides of orthodontically moved teeth, and to compare these with control teeth. GCF samples were collected from eight orthodontic patients wearing fixed appliances with superelastic nickel-titanium coil springs. The samples were analysed by gelatin zymography, which allows detection of both active and latent MMPs, and reverse zymography for analysis of TIMPs. Western blotting was performed to confirm the identity of MMPs. The data were analysed using either the one-way analysis of variance or the Kruskal-Wallis test. In general, higher levels of MMPs and TIMPs were found at both the resorption and apposition sides compared with the control teeth. Remarkably, partially active MMP-1 was found in GCF from both the resorption and the apposition side but was barely present at the control teeth. TIMP-1 was strongly increased at the apposition side. Gelatinases were mainly present at the resorption side, while gelatinolytic fragments were exclusively detected at the apposition side. MMP-9, which is known to be involved in bone degradation, and a 48 kDa gelatinase were increased at the resorption side. The small increase in TIMP-1 at the resorption side might stimulate bone resorption, whereas the large increase at the apposition side reduces bone resorption. The analysis of MMPs and TIMPs may contribute to the improvement of orthodontic treatment regimens.
正畸牙齿移动需要牙周组织进行广泛的重塑。基质金属蛋白酶（MMPs）在重塑过程中降解细胞外基质，而其活性受金属蛋白酶组织抑制剂（TIMPs）调节。本研究的目的是调查正畸移动牙齿的吸收侧和附着侧龈沟液（GCF）中MMP和TIMP水平的差异，并将其与对照牙齿进行比较。从八名佩戴带有超弹性镍钛螺旋弹簧固定矫治器的正畸患者中收集GCF样本。通过明胶酶谱法分析样本，该方法可检测活性和潜伏性MMPs，并通过反向酶谱法分析TIMPs。进行蛋白质印迹法以确认MMPs的身份。使用单因素方差分析或Kruskal-Wallis检验分析数据。总体而言，与对照牙齿相比，在吸收侧和附着侧均发现较高水平的MMPs和TIMPs。值得注意的是，在吸收侧和附着侧的GCF中均发现了部分活性的MMP-1，但在对照牙齿中几乎不存在。TIMP-1在附着侧显著增加。明胶酶主要存在于吸收侧，而明胶水解片段仅在附着侧检测到。已知参与骨降解的MMP-9和一种48 kDa的明胶酶在吸收侧增加。吸收侧TIMP-1的小幅增加可能会刺激骨吸收，而附着侧的大幅增加则会减少骨吸收。对MMPs和TIMPs的分析可能有助于改善正畸治疗方案。
