MMP-3 Response to Compressive Forces in vitro and in vivo

Abstract

During orthodontic tooth movement, bone resorption occurs at the compression site. However, the mechanism underlying resorption remains unclear. Applying compressive force to human osteoblast-like cells grown in a 3D collagen gel, we examined gene induction by using microarray and RT-PCR analysis. Among 43 genes exhibiting significant changes, cyclo-oxygenase-2, ornithine decarboxylase, and matrix metalloproteinase-3 (MMP-3) were up-regulated, whereas membrane-bound interleukin-1 receptor accessory protein was down-regulated. The MMP-3 protein increases were further confirmed by Western blot. To ascertain whether MMP-3 is up-regulated in vivo by orthodontic force, we examined human bone samples at the compressive site by realigning the angulated molars. Immunohistochemical staining revealed MMP-3 distributed along the compressive site of the bony region within 3 days of compression. Since MMP-3 participates in degradation of a wide range of extracellular matrix molecules, we propose that MMP-3 plays an important role in bone resorption during orthodontic tooth movement.

Orthodontic tensile strain induces angiogenesis via type IV collagen degradation by matrix metalloproteinase‐12

“…In the present study, we discovered that the orthodontic tensile strain induced MMP‐12 expression in the tension zone of PDL and promoted vascular remodeling via degradation of Col‐IV in VBM. It is known that several MMPs are expressed in PDL tissue during OTM . However, there has been no report on the relationship between the expressed MMP‐12 and angiogenesis in PDL tissue from the point of the degradation of the VBM.…”

Differential regulation of collagen, lysyl oxidase and MMP‐2 in human periodontal ligament cells by low‐ and high‐level mechanical stretching

“…The levels of mRNA expressed from type I collagen alpha 1 ( COL1A1 ), type III collagen alpha 1 ( COL3A1 ), LOX , MMP2 and TIMP2 were analyzed using RT‐PCR, as described previously . Total cellular RNA was prepared from PDL cells using the TRIzol reagent (Life Technologies, Carlsbad, CA, USA).…”

Critical roles of periostin in the process of orthodontic tooth movement

“…At this stage, we do not know why and how this occurs, although the following three factors could be directly or indirectly associated with periostin function. It is known that extracellular matrix (ECM) degradation takes place through autocrine and paracrine actions (22), and an increase in matrix metalloproteinase (MMP) levels during ECM remodelling is documented (23), indicating a close linkage between ECM remodelling and MMPs' function. Next, periostin is highly expressed in collagen rich tissues subject to constant mechanical stress, colocalizes with collagen I, and displays periostin KO mice with pathological changes in fibril diameter and collagen cross-linking (24).…”