Effect of recombinant human tissue inhibitor of matrix metalloproteinase-1 in mandibular distraction osteogenesis in rabbits: a computed tomographic study

Br J Oral Maxillofac Surg. 2006 Feb;44(1):5-11. doi: 10.1016/j.bjoms.2005.07.013. Epub 2005 Oct 3.

Abstract

Matrix metalloproteinases (MMPs), together with their tissue inhibitors (TIMPs), are responsible for the controlled degradation of collagen in bone. We studied the long-term stability of the regenerated bone formed by distraction osteogenesis, and the effect of recombinant human TIMP-1 on the remodelling of bone formed by mandibular distraction osteogenesis in rabbits. Nine rabbits were subjected to distraction osteogenesis of the mandible and divided into three groups: a control group with no collagen implanted; a sham-control group with a collagen sheet implanted; and an experimental group with a collagen sheet impregnated with rhTIMP-1 implanted. Computed tomograms were taken at weeks 4, 12, and 24 after distraction, and micro-computed tomograms and histological examinations were made at week 24. There was no significant resorption of regenerated bone at the site of distraction in any group after 6 months of consolidation, suggesting that the regenerated bone formed by distraction osteogenesis is stable. We found no obvious influence of rhTIMP-1 in the collagen sheet on the bony regenerate after 6 months of consolidation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Bone Regeneration / drug effects
  • Bone Remodeling / drug effects
  • Bone Resorption / diagnostic imaging
  • Bone Resorption / pathology
  • Collagen
  • Drug Carriers
  • Humans
  • Mandible / diagnostic imaging
  • Mandible / drug effects
  • Mandible / pathology
  • Mandible / surgery*
  • Membranes, Artificial
  • Osteogenesis, Distraction*
  • Protease Inhibitors / therapeutic use*
  • Rabbits
  • Recombinant Proteins
  • Time Factors
  • Tissue Inhibitor of Metalloproteinase-1 / therapeutic use*
  • Tomography, X-Ray Computed*

Substances

  • Drug Carriers
  • Membranes, Artificial
  • Protease Inhibitors
  • Recombinant Proteins
  • Tissue Inhibitor of Metalloproteinase-1
  • Collagen